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BigScience Biomedical Datasets 126

[ { "id": "IEPA.d132.s319", "type": "", "text": [ "The effects of the fluorinated analogues were evaluated on inhibition of cress seed germination and inhibition of gibberellin-inducible alpha-amylase induction in embryoless barley half-seeds" ], "offsets": [ [ 0, 191 ] ] }, { "id": "IEPA.d132.s320", "type": "", "text": [ "(2E, 4E)-2-Fluoro-5-(1'-hydroxy-2',6', 6'-trimethyl-2'-cyclohexen-1'-yl)-3-methyl-2,4-pentadienoic acid (5b) showed potent inhibitory activity at the same level as ABA in the cress seed germination test, and 5b also inhibited gibberellin-inducible alpha-amylase induction at 4 x 10(-)(6), 3 times the concentration of ABA (1 x 10(-)(6)) for 50% inhibition of alpha-amylase production" ], "offsets": [ [ 192, 575 ] ] } ]

[ { "id": "IEPA.d132.s319.e0", "type": "", "text": [ "gibberellin" ], "offsets": [ [ 114, 125 ] ], "normalized": [] }, { "id": "IEPA.d132.s319.e1", "type": "", "text": [ "alpha-amylase" ], "offsets": [ [ 136, 149 ] ], "normalized": [] }, { "id": "IEPA.d132.s320.e0", "type": "", "text": [ "gibberellin" ], "offsets": [ [ 418, 429 ] ], "normalized": [] }, { "id": "IEPA.d132.s320.e1", "type": "", "text": [ "alpha-amylase" ], "offsets": [ [ 440, 453 ] ], "normalized": [] }, { "id": "IEPA.d132.s320.e2", "type": "", "text": [ "alpha-amylase" ], "offsets": [ [ 551, 564 ] ], "normalized": [] } ]

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[ { "id": "IEPA.d132.s319.i0", "type": "PPI", "arg1_id": "IEPA.d132.s319.e0", "arg2_id": "IEPA.d132.s319.e1", "normalized": [] }, { "id": "IEPA.d132.s320.i0", "type": "PPI", "arg1_id": "IEPA.d132.s320.e0", "arg2_id": "IEPA.d132.s320.e1", "normalized": [] } ]

[ { "id": "IEPA.d133.s321", "type": "", "text": [ "Neurotransmitters and hormones, such as arginine vasopressin (AVP) and bombesin, evoke frequency-modulated repetitive Ca2+ transients in insulin-secreting HIT-T15 cells by binding to receptors linked to phospholipase C (PLC)" ], "offsets": [ [ 0, 224 ] ] } ]

[ { "id": "IEPA.d133.s321.e0", "type": "", "text": [ "insulin" ], "offsets": [ [ 137, 144 ] ], "normalized": [] }, { "id": "IEPA.d133.s321.e1", "type": "", "text": [ "phospholipase C" ], "offsets": [ [ 203, 218 ] ], "normalized": [] } ]

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[ { "id": "IEPA.d134.s322", "type": "", "text": [ "Isolation and characterization of gibbestatin B, an inhibitor of gibberellin-induced expression of alpha-amylase, and gibbestatin C from streptomycetaes" ], "offsets": [ [ 0, 152 ] ] } ]

[ { "id": "IEPA.d134.s322.e0", "type": "", "text": [ "gibberellin" ], "offsets": [ [ 65, 76 ] ], "normalized": [] }, { "id": "IEPA.d134.s322.e1", "type": "", "text": [ "alpha-amylase" ], "offsets": [ [ 99, 112 ] ], "normalized": [] } ]

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[ { "id": "IEPA.d134.s322.i0", "type": "PPI", "arg1_id": "IEPA.d134.s322.e0", "arg2_id": "IEPA.d134.s322.e1", "normalized": [] } ]

[ { "id": "IEPA.d137.s325", "type": "", "text": [ "We previously showed that arginine vasopressin (AVP) stimulates heat shock protein 27 (HSP27) induction through protein kinase C activation in aortic smooth muscle A10 cells" ], "offsets": [ [ 0, 173 ] ] }, { "id": "IEPA.d137.s326", "type": "", "text": [ "Calphostin C and ET-18-OCH(3), inhibitors of protein kinase C, reduced the phosphorylation of p38 MAP kinase by AVP" ], "offsets": [ [ 174, 289 ] ] } ]

[ { "id": "IEPA.d137.s325.e0", "type": "", "text": [ "arginine vasopressin" ], "offsets": [ [ 26, 46 ] ], "normalized": [] }, { "id": "IEPA.d137.s325.e1", "type": "", "text": [ "protein kinase C" ], "offsets": [ [ 112, 128 ] ], "normalized": [] }, { "id": "IEPA.d137.s326.e0", "type": "", "text": [ "protein kinase C" ], "offsets": [ [ 219, 235 ] ], "normalized": [] }, { "id": "IEPA.d137.s326.e1", "type": "", "text": [ "AVP" ], "offsets": [ [ 286, 289 ] ], "normalized": [] } ]

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[ { "id": "IEPA.d137.s325.i0", "type": "PPI", "arg1_id": "IEPA.d137.s325.e0", "arg2_id": "IEPA.d137.s325.e1", "normalized": [] }, { "id": "IEPA.d137.s326.i0", "type": "PPI", "arg1_id": "IEPA.d137.s326.e0", "arg2_id": "IEPA.d137.s326.e1", "normalized": [] } ]

[ { "id": "IEPA.d138.s327", "type": "", "text": [ "Insulin-like signaling in yeast: modulation of protein phosphatase 2A, protein kinase A, cAMP-specific phosphodiesterase, and glycosyl-phosphatidylinositol-specific phospholipase C activities" ], "offsets": [ [ 0, 191 ] ] }, { "id": "IEPA.d138.s328", "type": "", "text": [ "In addition, glycosyl-phosphatidylinositol-specific phospholipase C (GPI-PLC), which in isolated rat adipocytes is activated by insulin, was stimulated to up to 5-fold by glucose and 10-fold by glucose plus insulin in both yeast spheroplasts and intact cells leading to a concentration-dependent leftward shift of the glucose-response curve for activation of the GPI-PLC" ], "offsets": [ [ 192, 562 ] ] }, { "id": "IEPA.d138.s329", "type": "", "text": [ "GPI-PLC was most pronouncedly stimulated by authentic human insulin compared to various insulin analogues and insulin-like growth factor I" ], "offsets": [ [ 563, 701 ] ] }, { "id": "IEPA.d138.s330", "type": "", "text": [ "As the GPI-PLC reaction is rate limiting, the efficiency of the two-step anchor cleavage was significantly increased when insulin was present together with glucose as compared to glucose alone" ], "offsets": [ [ 702, 894 ] ] }, { "id": "IEPA.d138.s331", "type": "", "text": [ "The insulin concentrations effective in modulating PP2A, PKA, cAMP-PDE, and GPI-PLC activities correlate well with those required for half-saturation of the specific binding sites as well as for stimulation of protein phosphorylation and glycogen accumulation" ], "offsets": [ [ 895, 1154 ] ] }, { "id": "IEPA.d138.s332", "type": "", "text": [ "The data suggest that mammalian insulin-sensitive cells and yeast share (part of) the key regulatory mechanism (consisting of PP2A, PKA, cAMP-PDE, and GPI-PLC) involved in the transduction of the insulin signal from the respective receptor systems to glycogen synthase and phosphorylase" ], "offsets": [ [ 1155, 1441 ] ] } ]

[ { "id": "IEPA.d138.s327.e0", "type": "", "text": [ "Insulin" ], "offsets": [ [ 0, 7 ] ], "normalized": [] }, { "id": "IEPA.d138.s327.e1", "type": "", "text": [ "phospholipase C" ], "offsets": [ [ 165, 180 ] ], "normalized": [] }, { "id": "IEPA.d138.s328.e0", "type": "", "text": [ "glycosyl-phosphatidylinositol-specific phospholipase C" ], "offsets": [ [ 205, 259 ] ], "normalized": [] }, { "id": "IEPA.d138.s328.e1", "type": "", "text": [ "insulin" ], "offsets": [ [ 320, 327 ] ], "normalized": [] }, { "id": "IEPA.d138.s328.e2", "type": "", "text": [ "insulin" ], "offsets": [ [ 399, 406 ] ], "normalized": [] }, { "id": "IEPA.d138.s328.e3", "type": "", "text": [ "GPI-PLC" ], "offsets": [ [ 555, 562 ] ], "normalized": [] }, { "id": "IEPA.d138.s329.e0", "type": "", "text": [ "GPI-PLC" ], "offsets": [ [ 563, 570 ] ], "normalized": [] }, { "id": "IEPA.d138.s329.e1", "type": "", "text": [ "insulin" ], "offsets": [ [ 623, 630 ] ], "normalized": [] }, { "id": "IEPA.d138.s330.e0", "type": "", "text": [ "GPI-PLC" ], "offsets": [ [ 709, 716 ] ], "normalized": [] }, { "id": "IEPA.d138.s330.e1", "type": "", "text": [ "insulin" ], "offsets": [ [ 824, 831 ] ], "normalized": [] }, { "id": "IEPA.d138.s331.e0", "type": "", "text": [ "insulin" ], "offsets": [ [ 899, 906 ] ], "normalized": [] }, { "id": "IEPA.d138.s331.e1", "type": "", "text": [ "GPI-PLC" ], "offsets": [ [ 971, 978 ] ], "normalized": [] }, { "id": "IEPA.d138.s332.e0", "type": "", "text": [ "insulin" ], "offsets": [ [ 1187, 1194 ] ], "normalized": [] }, { "id": "IEPA.d138.s332.e1", "type": "", "text": [ "GPI-PLC" ], "offsets": [ [ 1306, 1313 ] ], "normalized": [] }, { "id": "IEPA.d138.s332.e2", "type": "", "text": [ "insulin" ], "offsets": [ [ 1351, 1358 ] ], "normalized": [] } ]

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[ { "id": "IEPA.d138.s328.i0", "type": "PPI", "arg1_id": "IEPA.d138.s328.e0", "arg2_id": "IEPA.d138.s328.e1", "normalized": [] }, { "id": "IEPA.d138.s328.i1", "type": "PPI", "arg1_id": "IEPA.d138.s328.e0", "arg2_id": "IEPA.d138.s328.e2", "normalized": [] }, { "id": "IEPA.d138.s329.i0", "type": "PPI", "arg1_id": "IEPA.d138.s329.e0", "arg2_id": "IEPA.d138.s329.e1", "normalized": [] }, { "id": "IEPA.d138.s331.i0", "type": "PPI", "arg1_id": "IEPA.d138.s331.e0", "arg2_id": "IEPA.d138.s331.e1", "normalized": [] }, { "id": "IEPA.d138.s332.i0", "type": "PPI", "arg1_id": "IEPA.d138.s332.e1", "arg2_id": "IEPA.d138.s332.e2", "normalized": [] } ]

[ { "id": "IEPA.d139.s333", "type": "", "text": [ "Leptin and UCP (1 and 2) mRNA levels were determined by reverse transcription-polymerase chain reaction (RT-PCR) methodology in adipose tissue and gastrocnemius muscle" ], "offsets": [ [ 0, 167 ] ] }, { "id": "IEPA.d139.s334", "type": "", "text": [ "A negative correlation between WAT O2 consumption and UCP2 expression was found in control animals, but not in the cafeteria-fed groups, suggesting a differential response to the beta3-adrenergic compound in lean and obese animals, which is in agreement with the reported statistical interactions between obesity and Trecadrine administration found for WAT O2 consumption and muscle UCP2 expression, as well as for plasma leptin and WAT leptin expression" ], "offsets": [ [ 168, 622 ] ] } ]

[ { "id": "IEPA.d139.s333.e0", "type": "", "text": [ "Leptin" ], "offsets": [ [ 0, 6 ] ], "normalized": [] }, { "id": "IEPA.d139.s333.e1", "type": "", "text": [ "UCP" ], "offsets": [ [ 11, 14 ] ], "normalized": [] }, { "id": "IEPA.d139.s334.e0", "type": "", "text": [ "UCP2" ], "offsets": [ [ 222, 226 ] ], "normalized": [] }, { "id": "IEPA.d139.s334.e1", "type": "", "text": [ "UCP2" ], "offsets": [ [ 551, 555 ] ], "normalized": [] }, { "id": "IEPA.d139.s334.e2", "type": "", "text": [ "leptin" ], "offsets": [ [ 590, 596 ] ], "normalized": [] }, { "id": "IEPA.d139.s334.e3", "type": "", "text": [ "leptin" ], "offsets": [ [ 605, 611 ] ], "normalized": [] } ]

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[ { "id": "IEPA.d140.s335", "type": "", "text": [ "Arginine vasopressin (AVP) and lysophosphatidic acid (LPA) have been shown to stimulate protein kinase C (PKC) and mitogen-activated protein (MAP) kinases and the proliferation of vascular smooth muscle cells" ], "offsets": [ [ 0, 208 ] ] }, { "id": "IEPA.d140.s336", "type": "", "text": [ "However, AVP-induced activation of RSK2, a downstream substrate of ERK1 and ERK2, was PKC-dependent and PI 3-kinase-independent" ], "offsets": [ [ 209, 336 ] ] }, { "id": "IEPA.d140.s337", "type": "", "text": [ "PKC was necessary in AVP- but not in LPA-induced activation of p70 S6K" ], "offsets": [ [ 337, 407 ] ] } ]

[ { "id": "IEPA.d140.s335.e0", "type": "", "text": [ "Arginine vasopressin" ], "offsets": [ [ 0, 20 ] ], "normalized": [] }, { "id": "IEPA.d140.s335.e1", "type": "", "text": [ "protein kinase C" ], "offsets": [ [ 88, 104 ] ], "normalized": [] }, { "id": "IEPA.d140.s336.e0", "type": "", "text": [ "AVP" ], "offsets": [ [ 218, 221 ] ], "normalized": [] }, { "id": "IEPA.d140.s336.e1", "type": "", "text": [ "PKC" ], "offsets": [ [ 295, 298 ] ], "normalized": [] }, { "id": "IEPA.d140.s337.e0", "type": "", "text": [ "PKC" ], "offsets": [ [ 337, 340 ] ], "normalized": [] }, { "id": "IEPA.d140.s337.e1", "type": "", "text": [ "AVP" ], "offsets": [ [ 358, 361 ] ], "normalized": [] } ]

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[ { "id": "IEPA.d140.s335.i0", "type": "PPI", "arg1_id": "IEPA.d140.s335.e0", "arg2_id": "IEPA.d140.s335.e1", "normalized": [] }, { "id": "IEPA.d140.s336.i0", "type": "PPI", "arg1_id": "IEPA.d140.s336.e0", "arg2_id": "IEPA.d140.s336.e1", "normalized": [] }, { "id": "IEPA.d140.s337.i0", "type": "PPI", "arg1_id": "IEPA.d140.s337.e0", "arg2_id": "IEPA.d140.s337.e1", "normalized": [] } ]

[ { "id": "IEPA.d141.s338", "type": "", "text": [ "Tolbutamide and diazoxide modulate phospholipase C-linked Ca(2+) signaling and insulin secretion in beta-cells" ], "offsets": [ [ 0, 110 ] ] }, { "id": "IEPA.d141.s339", "type": "", "text": [ "We examined whether tolbutamide and diazoxide, which close or open ATP-sensitive K(+) channels (K(ATP) channels), respectively, interact with PLC-linked Ca(2+) signals in HIT-T15 and mouse beta-cells and with PLC-linked insulin secretion from HIT-T15 cells" ], "offsets": [ [ 111, 367 ] ] }, { "id": "IEPA.d141.s340", "type": "", "text": [ "Thus tolbutamide and diazoxide regulate both PLC-linked Ca(2+) signaling and insulin secretion from pancreatic beta-cells by modulating K(ATP) channels, thereby determining voltage-sensitive Ca(2+) influx" ], "offsets": [ [ 368, 572 ] ] } ]

[ { "id": "IEPA.d141.s338.e0", "type": "", "text": [ "phospholipase C" ], "offsets": [ [ 35, 50 ] ], "normalized": [] }, { "id": "IEPA.d141.s338.e1", "type": "", "text": [ "insulin" ], "offsets": [ [ 79, 86 ] ], "normalized": [] }, { "id": "IEPA.d141.s339.e0", "type": "", "text": [ "PLC" ], "offsets": [ [ 253, 256 ] ], "normalized": [] }, { "id": "IEPA.d141.s339.e1", "type": "", "text": [ "PLC" ], "offsets": [ [ 320, 323 ] ], "normalized": [] }, { "id": "IEPA.d141.s339.e2", "type": "", "text": [ "insulin" ], "offsets": [ [ 331, 338 ] ], "normalized": [] }, { "id": "IEPA.d141.s340.e0", "type": "", "text": [ "PLC" ], "offsets": [ [ 413, 416 ] ], "normalized": [] }, { "id": "IEPA.d141.s340.e1", "type": "", "text": [ "insulin" ], "offsets": [ [ 445, 452 ] ], "normalized": [] } ]

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[ { "id": "IEPA.d141.s338.i0", "type": "PPI", "arg1_id": "IEPA.d141.s338.e0", "arg2_id": "IEPA.d141.s338.e1", "normalized": [] }, { "id": "IEPA.d141.s339.i0", "type": "PPI", "arg1_id": "IEPA.d141.s339.e1", "arg2_id": "IEPA.d141.s339.e2", "normalized": [] }, { "id": "IEPA.d141.s340.i0", "type": "PPI", "arg1_id": "IEPA.d141.s340.e0", "arg2_id": "IEPA.d141.s340.e1", "normalized": [] } ]

[ { "id": "IEPA.d143.s343", "type": "", "text": [ "Oxytocin central injections to intact animals stimulated insulin synthesis and secretion without changing of islets area" ], "offsets": [ [ 0, 120 ] ] }, { "id": "IEPA.d143.s344", "type": "", "text": [ "Thus, oxytocin administration stimulates insulin synthesis and secretion in intact and diabetic animals and this effect is more expressed with central injections" ], "offsets": [ [ 121, 282 ] ] } ]

[ { "id": "IEPA.d143.s343.e0", "type": "", "text": [ "Oxytocin" ], "offsets": [ [ 0, 8 ] ], "normalized": [] }, { "id": "IEPA.d143.s343.e1", "type": "", "text": [ "insulin" ], "offsets": [ [ 57, 64 ] ], "normalized": [] }, { "id": "IEPA.d143.s344.e0", "type": "", "text": [ "oxytocin" ], "offsets": [ [ 127, 135 ] ], "normalized": [] }, { "id": "IEPA.d143.s344.e1", "type": "", "text": [ "insulin" ], "offsets": [ [ 162, 169 ] ], "normalized": [] } ]

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[ { "id": "IEPA.d143.s343.i0", "type": "PPI", "arg1_id": "IEPA.d143.s343.e0", "arg2_id": "IEPA.d143.s343.e1", "normalized": [] }, { "id": "IEPA.d143.s344.i0", "type": "PPI", "arg1_id": "IEPA.d143.s344.e0", "arg2_id": "IEPA.d143.s344.e1", "normalized": [] } ]

[ { "id": "IEPA.d144.s345", "type": "", "text": [ "Hypothalamic neuropeptide Y and its neuroendocrine regulation by leptin" ], "offsets": [ [ 0, 71 ] ] } ]

[ { "id": "IEPA.d144.s345.e0", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 13, 27 ] ], "normalized": [] }, { "id": "IEPA.d144.s345.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 65, 71 ] ], "normalized": [] } ]

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[ { "id": "IEPA.d144.s345.i0", "type": "PPI", "arg1_id": "IEPA.d144.s345.e0", "arg2_id": "IEPA.d144.s345.e1", "normalized": [] } ]

[ { "id": "IEPA.d146.s351", "type": "", "text": [ "Ca2+ signalling in rat vascular smooth muscle cells: a role for protein kinase C at physiological vasoconstrictor concentrations of vasopressin" ], "offsets": [ [ 0, 143 ] ] }, { "id": "IEPA.d146.s352", "type": "", "text": [ "The protein kinase C (PKC) activator 4beta-phorbol 12-myristate 13-acetate (PMA, 100 pM to 200 nM), also stimulated Ca2+ spiking and this effect was additive with a submaximal concentration of AVP (50 pM)" ], "offsets": [ [ 144, 348 ] ] }, { "id": "IEPA.d146.s353", "type": "", "text": [ "The PKC inhibitors Ro-31-8220 (1 microM) and calphostin C (250 nM) completely blocked the stimulation of Ca2+ spiking by either PMA or AVP" ], "offsets": [ [ 349, 487 ] ] }, { "id": "IEPA.d146.s354", "type": "", "text": [ "Time-dependent redistribution of PKC-alpha, -delta and -epsilon isoforms between the membrane and cytosolic fractions occurred in response to 100 pM AVP" ], "offsets": [ [ 488, 640 ] ] }, { "id": "IEPA.d146.s355", "type": "", "text": [ "Pretreatment for 24 h with 1 microM PMA downregulated expression of PKC-alpha and -delta, but not PKC-epsilon, and prevented the Ca2+-spiking responses to either 1 nM PMA or 100 pM AVP" ], "offsets": [ [ 641, 825 ] ] }, { "id": "IEPA.d146.s356", "type": "", "text": [ "We conclude that PKC activation is a necessary step in the signal transduction pathway linking low concentrations of AVP to Ca2+ spiking in A7r5 cells" ], "offsets": [ [ 826, 976 ] ] } ]

[ { "id": "IEPA.d146.s351.e0", "type": "", "text": [ "protein kinase C" ], "offsets": [ [ 64, 80 ] ], "normalized": [] }, { "id": "IEPA.d146.s351.e1", "type": "", "text": [ "vasopressin" ], "offsets": [ [ 132, 143 ] ], "normalized": [] }, { "id": "IEPA.d146.s352.e0", "type": "", "text": [ "protein kinase C" ], "offsets": [ [ 148, 164 ] ], "normalized": [] }, { "id": "IEPA.d146.s352.e1", "type": "", "text": [ "AVP" ], "offsets": [ [ 337, 340 ] ], "normalized": [] }, { "id": "IEPA.d146.s353.e0", "type": "", "text": [ "PKC inhibitors" ], "offsets": [ [ 353, 367 ] ], "normalized": [] }, { "id": "IEPA.d146.s353.e1", "type": "", "text": [ "AVP" ], "offsets": [ [ 484, 487 ] ], "normalized": [] }, { "id": "IEPA.d146.s354.e0", "type": "", "text": [ "PKC-alpha" ], "offsets": [ [ 521, 530 ] ], "normalized": [] }, { "id": "IEPA.d146.s354.e1", "type": "", "text": [ "AVP" ], "offsets": [ [ 637, 640 ] ], "normalized": [] }, { "id": "IEPA.d146.s355.e0", "type": "", "text": [ "PKC-alpha" ], "offsets": [ [ 709, 718 ] ], "normalized": [] }, { "id": "IEPA.d146.s355.e1", "type": "", "text": [ "PKC-epsilon" ], "offsets": [ [ 739, 750 ] ], "normalized": [] }, { "id": "IEPA.d146.s355.e2", "type": "", "text": [ "AVP" ], "offsets": [ [ 822, 825 ] ], "normalized": [] }, { "id": "IEPA.d146.s356.e0", "type": "", "text": [ "PKC" ], "offsets": [ [ 843, 846 ] ], "normalized": [] }, { "id": "IEPA.d146.s356.e1", "type": "", "text": [ "AVP" ], "offsets": [ [ 943, 946 ] ], "normalized": [] } ]

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[ { "id": "IEPA.d146.s351.i0", "type": "PPI", "arg1_id": "IEPA.d146.s351.e0", "arg2_id": "IEPA.d146.s351.e1", "normalized": [] }, { "id": "IEPA.d146.s353.i0", "type": "PPI", "arg1_id": "IEPA.d146.s353.e0", "arg2_id": "IEPA.d146.s353.e1", "normalized": [] }, { "id": "IEPA.d146.s354.i0", "type": "PPI", "arg1_id": "IEPA.d146.s354.e0", "arg2_id": "IEPA.d146.s354.e1", "normalized": [] }, { "id": "IEPA.d146.s356.i0", "type": "PPI", "arg1_id": "IEPA.d146.s356.e0", "arg2_id": "IEPA.d146.s356.e1", "normalized": [] } ]

[ { "id": "IEPA.d147.s357", "type": "", "text": [ "Ten protein kinases have been assayed for their ability to phosphorylate in vitro the recombinant bovine PrP (25-242) (rbPrP)" ], "offsets": [ [ 0, 125 ] ] }, { "id": "IEPA.d147.s358", "type": "", "text": [ "With regard to CK2, phosphorylation occurs at Ser 154 with a stoichiometry of about 0.1 mol phosphate/mol rbPrP, which is doubled by mild heat treatment of rbPrP" ], "offsets": [ [ 126, 287 ] ] } ]

[ { "id": "IEPA.d147.s357.e0", "type": "", "text": [ "protein kinases" ], "offsets": [ [ 4, 19 ] ], "normalized": [] }, { "id": "IEPA.d147.s357.e1", "type": "", "text": [ "recombinant bovine PrP" ], "offsets": [ [ 86, 108 ] ], "normalized": [] }, { "id": "IEPA.d147.s358.e0", "type": "", "text": [ "CK2" ], "offsets": [ [ 141, 144 ] ], "normalized": [] }, { "id": "IEPA.d147.s358.e1", "type": "", "text": [ "rbPrP" ], "offsets": [ [ 232, 237 ] ], "normalized": [] }, { "id": "IEPA.d147.s358.e2", "type": "", "text": [ "rbPrP" ], "offsets": [ [ 282, 287 ] ], "normalized": [] } ]

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[ { "id": "IEPA.d147.s358.i0", "type": "PPI", "arg1_id": "IEPA.d147.s358.e0", "arg2_id": "IEPA.d147.s358.e1", "normalized": [] } ]

[ { "id": "IEPA.d148.s359", "type": "", "text": [ "In vivo effects of CGP-12177 on the expression of leptin and uncoupling protein genes in mouse brown and white adipose tissues" ], "offsets": [ [ 0, 126 ] ] }, { "id": "IEPA.d148.s360", "type": "", "text": [ "OBJECTIVE: To assess the effect of chronic treatment with CGP-12177 a beta3-adrenergic receptor (AR) agonist with beta2/beta1-AR antagonist action, on the expression of the leptin gene and of genes coding for uncoupling proteins (ucp1, ucp2 and ucp3) in brown and white adipose tissues" ], "offsets": [ [ 127, 412 ] ] }, { "id": "IEPA.d148.s361", "type": "", "text": [ "CONCLUSION: The results reveal that simultaneous stimulation of the expression of certain ucp genes and the leptin gene can be achieved, and suggest that adrenergic regulation of the leptin gene and of genes of the ucp family in adipose tissues is the result of complex interactions between the different beta-AR pathways" ], "offsets": [ [ 413, 734 ] ] } ]

[ { "id": "IEPA.d148.s359.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 50, 56 ] ], "normalized": [] }, { "id": "IEPA.d148.s359.e1", "type": "", "text": [ "uncoupling protein" ], "offsets": [ [ 61, 79 ] ], "normalized": [] }, { "id": "IEPA.d148.s360.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 300, 306 ] ], "normalized": [] }, { "id": "IEPA.d148.s360.e1", "type": "", "text": [ "uncoupling proteins" ], "offsets": [ [ 336, 355 ] ], "normalized": [] }, { "id": "IEPA.d148.s361.e0", "type": "", "text": [ "ucp" ], "offsets": [ [ 503, 506 ] ], "normalized": [] }, { "id": "IEPA.d148.s361.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 521, 527 ] ], "normalized": [] }, { "id": "IEPA.d148.s361.e2", "type": "", "text": [ "leptin" ], "offsets": [ [ 596, 602 ] ], "normalized": [] }, { "id": "IEPA.d148.s361.e3", "type": "", "text": [ "ucp" ], "offsets": [ [ 628, 631 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "IEPA.d149.s362", "type": "", "text": [ "Furthermore, in SN-56/OBR cells both CNTF and leptin produce changes in neurotransmitter and neuropeptide phenotype characteristic of cholinergic neurons, such as an increase in choline acetyltransferase and vasoactive intestinal polypeptide, and a decrease in neuropeptide Y expression" ], "offsets": [ [ 0, 286 ] ] } ]

[ { "id": "IEPA.d149.s362.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 46, 52 ] ], "normalized": [] }, { "id": "IEPA.d149.s362.e1", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 261, 275 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d149.s362.i0", "type": "PPI", "arg1_id": "IEPA.d149.s362.e0", "arg2_id": "IEPA.d149.s362.e1", "normalized": [] } ]

[ { "id": "IEPA.d150.s363", "type": "", "text": [ "Possible central nervous system (CNS) mechanisms could mediate these responses in that leptin receptors are located on hypothalamic neurons that coexpress neuropeptide-Y (NPY) or proopiomelanocortin (POMC) and both peptides that have been implicated as mediators of the CNS action of leptin." ], "offsets": [ [ 0, 291 ] ] }, { "id": "IEPA.d150.s364", "type": "", "text": [ "Leptin has been demonstrated to decrease or down regulate NPY expression and increase POMC expression" ], "offsets": [ [ 292, 393 ] ] } ]

[ { "id": "IEPA.d150.s363.e0", "type": "", "text": [ "neuropeptide-Y" ], "offsets": [ [ 155, 169 ] ], "normalized": [] }, { "id": "IEPA.d150.s363.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 284, 290 ] ], "normalized": [] }, { "id": "IEPA.d150.s364.e0", "type": "", "text": [ "Leptin" ], "offsets": [ [ 292, 298 ] ], "normalized": [] }, { "id": "IEPA.d150.s364.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 350, 353 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d150.s363.i0", "type": "PPI", "arg1_id": "IEPA.d150.s363.e0", "arg2_id": "IEPA.d150.s363.e1", "normalized": [] }, { "id": "IEPA.d150.s364.i0", "type": "PPI", "arg1_id": "IEPA.d150.s364.e0", "arg2_id": "IEPA.d150.s364.e1", "normalized": [] } ]

[ { "id": "IEPA.d151.s365", "type": "", "text": [ "Relationship among leptin, neuropeptide Y, and galanin in young women and in postmenopausal women [see comments]" ], "offsets": [ [ 0, 112 ] ] }, { "id": "IEPA.d151.s366", "type": "", "text": [ "OBJECTIVE: To determine whether hormonal status may affect neuropeptide Y (NPY), galanin, and leptin release in postmenopausal women and in young women" ], "offsets": [ [ 113, 264 ] ] }, { "id": "IEPA.d151.s367", "type": "", "text": [ "CONCLUSIONS: Our results suggest that the differences is plasma leptin, NPY, and galanin between postmenopausal women and young women may be related to body mass index rather than to differences in hormonal status and that the higher NPY levels in both lean and obese postmenopausal women than in young women indicate that factors other than body mass index may be involved" ], "offsets": [ [ 265, 638 ] ] } ]

[ { "id": "IEPA.d151.s365.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 19, 25 ] ], "normalized": [] }, { "id": "IEPA.d151.s365.e1", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 27, 41 ] ], "normalized": [] }, { "id": "IEPA.d151.s366.e0", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 172, 186 ] ], "normalized": [] }, { "id": "IEPA.d151.s366.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 207, 213 ] ], "normalized": [] }, { "id": "IEPA.d151.s367.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 329, 335 ] ], "normalized": [] }, { "id": "IEPA.d151.s367.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 337, 340 ] ], "normalized": [] }, { "id": "IEPA.d151.s367.e2", "type": "", "text": [ "NPY" ], "offsets": [ [ 499, 502 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d151.s365.i0", "type": "PPI", "arg1_id": "IEPA.d151.s365.e0", "arg2_id": "IEPA.d151.s365.e1", "normalized": [] } ]

[ { "id": "IEPA.d152.s368", "type": "", "text": [ "We examined for the first time in young men effects of intravenous injections of NPY (4x50 or 100 microg, n = 9 and 11, respectively, at 22.00, 23.00, 24.00 and 01.00 compared to saline) on the sleep electroencephalogram (EEG; recorded from 23.00 to 07.00) and nocturnal secretion of adrenocorticotrophic hormone (ACTH), cortisol, growth hormone (GH), prolactin and leptin" ], "offsets": [ [ 0, 372 ] ] } ]

[ { "id": "IEPA.d152.s368.e0", "type": "", "text": [ "NPY" ], "offsets": [ [ 81, 84 ] ], "normalized": [] }, { "id": "IEPA.d152.s368.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 366, 372 ] ], "normalized": [] } ]

[]

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[ { "id": "IEPA.d153.s369", "type": "", "text": [ "Interestingly, both 5-HT and leptin modulate the action of NPY, which may form a part of a common output pathway for the expression of appetite" ], "offsets": [ [ 0, 143 ] ] } ]

[ { "id": "IEPA.d153.s369.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 29, 35 ] ], "normalized": [] }, { "id": "IEPA.d153.s369.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 59, 62 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d153.s369.i0", "type": "PPI", "arg1_id": "IEPA.d153.s369.e0", "arg2_id": "IEPA.d153.s369.e1", "normalized": [] } ]

[ { "id": "IEPA.d154.s370", "type": "", "text": [ "The glycosyl-phosphatidylinositol anchored protein, membrane dipeptidase (EC 3.4.13.19) is released from the surface of 3T3-L1 adipocytes in response to insulin treatment through the action of a phospholipase C" ], "offsets": [ [ 0, 210 ] ] }, { "id": "IEPA.d154.s371", "type": "", "text": [ "Although X-Pro aminopeptidase (EC 3.4.11.9) is GPI-anchored in 3T3-L1 adipocytes as shown by digestion with bacterial phosphatidylinositol-specific phospholipase C, it was not released upon insulin treatment of the cells, indicating that only a subset of the GPI-anchored proteins are susceptible to insulin-stimulated release" ], "offsets": [ [ 211, 537 ] ] } ]

[ { "id": "IEPA.d154.s370.e0", "type": "", "text": [ "insulin" ], "offsets": [ [ 153, 160 ] ], "normalized": [] }, { "id": "IEPA.d154.s370.e1", "type": "", "text": [ "phospholipase C" ], "offsets": [ [ 195, 210 ] ], "normalized": [] }, { "id": "IEPA.d154.s371.e0", "type": "", "text": [ "phospholipase C" ], "offsets": [ [ 359, 374 ] ], "normalized": [] }, { "id": "IEPA.d154.s371.e1", "type": "", "text": [ "insulin" ], "offsets": [ [ 401, 408 ] ], "normalized": [] }, { "id": "IEPA.d154.s371.e2", "type": "", "text": [ "insulin" ], "offsets": [ [ 511, 518 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d154.s370.i0", "type": "PPI", "arg1_id": "IEPA.d154.s370.e0", "arg2_id": "IEPA.d154.s370.e1", "normalized": [] } ]

[ { "id": "IEPA.d155.s372", "type": "", "text": [ "However, neither progesterone nor insulin increased phosphotyrosine on PLCgamma" ], "offsets": [ [ 0, 79 ] ] } ]

[ { "id": "IEPA.d155.s372.e0", "type": "", "text": [ "insulin" ], "offsets": [ [ 34, 41 ] ], "normalized": [] }, { "id": "IEPA.d155.s372.e1", "type": "", "text": [ "PLCgamma" ], "offsets": [ [ 71, 79 ] ], "normalized": [] } ]

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[ { "id": "IEPA.d156.s373", "type": "", "text": [ "Leptin is a satiety factor which acts within the hypothalamus to decrease the levels of several neuropeptides stimulating food intake (among them, neuropeptide Y [NPY]), while increasing those that inhibit food intake" ], "offsets": [ [ 0, 217 ] ] } ]

[ { "id": "IEPA.d156.s373.e0", "type": "", "text": [ "Leptin" ], "offsets": [ [ 0, 6 ] ], "normalized": [] }, { "id": "IEPA.d156.s373.e1", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 147, 161 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d156.s373.i0", "type": "PPI", "arg1_id": "IEPA.d156.s373.e0", "arg2_id": "IEPA.d156.s373.e1", "normalized": [] } ]

[ { "id": "IEPA.d157.s374", "type": "", "text": [ "We have studied the effects of neomycin, a potent inhibitor of inositol phospholipid-specific phospholipase C (PLC), on the germination of rice seed and the gibberellin-induced expression of alpha-amylase in the aleurone layer and the scutellar tissues" ], "offsets": [ [ 0, 252 ] ] }, { "id": "IEPA.d157.s375", "type": "", "text": [ "It was shown that, in the absence of exogenous Ca2+, neomycin markedly reduced the germination speed and seedling growth of rice seeds and inhibited the gibberellin-induced expression of alpha-amylase in both secretory tissues" ], "offsets": [ [ 253, 479 ] ] }, { "id": "IEPA.d157.s376", "type": "", "text": [ "These results strongly suggest that the phosphoinositide-Ca2+ signal transduction pathway may play an important role in the gibberellin-induced expression of alpha-amylase molecules closely related to the germination processes of rice seed" ], "offsets": [ [ 480, 719 ] ] } ]

[ { "id": "IEPA.d157.s374.e0", "type": "", "text": [ "gibberellin" ], "offsets": [ [ 157, 168 ] ], "normalized": [] }, { "id": "IEPA.d157.s374.e1", "type": "", "text": [ "alpha-amylase" ], "offsets": [ [ 191, 204 ] ], "normalized": [] }, { "id": "IEPA.d157.s375.e0", "type": "", "text": [ "gibberellin" ], "offsets": [ [ 406, 417 ] ], "normalized": [] }, { "id": "IEPA.d157.s375.e1", "type": "", "text": [ "alpha-amylase" ], "offsets": [ [ 440, 453 ] ], "normalized": [] }, { "id": "IEPA.d157.s376.e0", "type": "", "text": [ "gibberellin" ], "offsets": [ [ 604, 615 ] ], "normalized": [] }, { "id": "IEPA.d157.s376.e1", "type": "", "text": [ "alpha-amylase" ], "offsets": [ [ 638, 651 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d157.s374.i0", "type": "PPI", "arg1_id": "IEPA.d157.s374.e0", "arg2_id": "IEPA.d157.s374.e1", "normalized": [] }, { "id": "IEPA.d157.s375.i0", "type": "PPI", "arg1_id": "IEPA.d157.s375.e0", "arg2_id": "IEPA.d157.s375.e1", "normalized": [] }, { "id": "IEPA.d157.s376.i0", "type": "PPI", "arg1_id": "IEPA.d157.s376.e0", "arg2_id": "IEPA.d157.s376.e1", "normalized": [] } ]

[ { "id": "IEPA.d158.s377", "type": "", "text": [ "NPY-leptin: opposing effects on appetitive and consummatory ingestive behavior and sexual behavior" ], "offsets": [ [ 0, 98 ] ] }, { "id": "IEPA.d158.s378", "type": "", "text": [ "Many studies have indicated that neuropeptide Y (NPY) stimulates and leptin inhibits food intake" ], "offsets": [ [ 99, 195 ] ] }, { "id": "IEPA.d158.s379", "type": "", "text": [ "In line with this, intracerebroventricular injection of NPY (10 microg) stimulated and leptin (10 microg) inhibited intake of a sucrose solution when female rats were required to obtain the solution from a bottle" ], "offsets": [ [ 196, 408 ] ] }, { "id": "IEPA.d158.s380", "type": "", "text": [ "However, NPY inhibited and leptin stimulated intake if the solution was infused intraorally" ], "offsets": [ [ 409, 500 ] ] }, { "id": "IEPA.d158.s381", "type": "", "text": [ "Thus NPY stimulates the responses used to obtain food but inhibits those used to consume food, and leptin has the opposite effects" ], "offsets": [ [ 501, 631 ] ] } ]

[ { "id": "IEPA.d158.s377.e0", "type": "", "text": [ "NPY" ], "offsets": [ [ 0, 3 ] ], "normalized": [] }, { "id": "IEPA.d158.s377.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 4, 10 ] ], "normalized": [] }, { "id": "IEPA.d158.s378.e0", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 132, 146 ] ], "normalized": [] }, { "id": "IEPA.d158.s378.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 168, 174 ] ], "normalized": [] }, { "id": "IEPA.d158.s379.e0", "type": "", "text": [ "NPY" ], "offsets": [ [ 252, 255 ] ], "normalized": [] }, { "id": "IEPA.d158.s379.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 283, 289 ] ], "normalized": [] }, { "id": "IEPA.d158.s380.e0", "type": "", "text": [ "NPY" ], "offsets": [ [ 418, 421 ] ], "normalized": [] }, { "id": "IEPA.d158.s380.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 436, 442 ] ], "normalized": [] }, { "id": "IEPA.d158.s381.e0", "type": "", "text": [ "NPY" ], "offsets": [ [ 506, 509 ] ], "normalized": [] }, { "id": "IEPA.d158.s381.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 600, 606 ] ], "normalized": [] } ]

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[ { "id": "IEPA.d159.s382", "type": "", "text": [ "In the fasting state UCP-2 expression correlated inversely with body mass index (r = -0.45; P = 0.026), percent body fat (r = -0.41; P = 0.05), plasma insulin (r = -0.47; P = 0.02), epigastric venous fatty acids (r = -0.45; P = 0.04), and leptin (r = -0.50; P = 0.018)" ], "offsets": [ [ 0, 268 ] ] }, { "id": "IEPA.d159.s383", "type": "", "text": [ "UCP-2 expression remained inversely related with plasma leptin after controlling for percent body (r = -0.45; P = 0.038)" ], "offsets": [ [ 269, 389 ] ] }, { "id": "IEPA.d159.s384", "type": "", "text": [ "In conclusion, 1) UCP-2 messenger ribonucleic acid expression in sc adipose tissue is inversely related to adiposity and independently linked to local plasma leptin levels; and 2) UCP-2 expression is not acutely regulated by food intake, insulin, or fatty acids" ], "offsets": [ [ 390, 651 ] ] } ]

[ { "id": "IEPA.d159.s382.e0", "type": "", "text": [ "UCP-2" ], "offsets": [ [ 21, 26 ] ], "normalized": [] }, { "id": "IEPA.d159.s382.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 239, 245 ] ], "normalized": [] }, { "id": "IEPA.d159.s383.e0", "type": "", "text": [ "UCP-2" ], "offsets": [ [ 269, 274 ] ], "normalized": [] }, { "id": "IEPA.d159.s383.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 325, 331 ] ], "normalized": [] }, { "id": "IEPA.d159.s384.e0", "type": "", "text": [ "UCP-2" ], "offsets": [ [ 408, 413 ] ], "normalized": [] }, { "id": "IEPA.d159.s384.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 548, 554 ] ], "normalized": [] }, { "id": "IEPA.d159.s384.e2", "type": "", "text": [ "UCP-2" ], "offsets": [ [ 570, 575 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d159.s382.i0", "type": "PPI", "arg1_id": "IEPA.d159.s382.e0", "arg2_id": "IEPA.d159.s382.e1", "normalized": [] }, { "id": "IEPA.d159.s383.i0", "type": "PPI", "arg1_id": "IEPA.d159.s383.e0", "arg2_id": "IEPA.d159.s383.e1", "normalized": [] }, { "id": "IEPA.d159.s384.i0", "type": "PPI", "arg1_id": "IEPA.d159.s384.e0", "arg2_id": "IEPA.d159.s384.e1", "normalized": [] } ]

[ { "id": "IEPA.d160.s385", "type": "", "text": [ "Thus, highly expressed in human adipocytes, the Y(1) receptor sustains the strong antilipolytic effect of NPY and exerts a positive action on leptin secretion" ], "offsets": [ [ 0, 158 ] ] } ]

[ { "id": "IEPA.d160.s385.e0", "type": "", "text": [ "NPY" ], "offsets": [ [ 106, 109 ] ], "normalized": [] }, { "id": "IEPA.d160.s385.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 142, 148 ] ], "normalized": [] } ]

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[ { "id": "IEPA.d161.s386", "type": "", "text": [ "Induction of fatty acid translocase/CD36, peroxisome proliferator-activated receptor-gamma2, leptin, uncoupling proteins 2 and 3, and tumor necrosis factor-alpha gene expression in human subcutaneous fat by lipid infusion" ], "offsets": [ [ 0, 221 ] ] }, { "id": "IEPA.d161.s387", "type": "", "text": [ "Using reverse transcriptase-polymerase chain reaction analysis, the mRNA expression of fatty acid translocase (FAT)/CD36, PPAR-gamma2, leptin, uncoupling protein (UCP)-2 and UCP-3, and tumor necrosis factor (TNF)-alpha was investigated in gluteal subcutaneous fat biopsies before and after 5 h infusions of saline or Intralipid (Pharmacia and Upjohn, Milan, Italy) plus heparin, which does not modify insulinemia" ], "offsets": [ [ 222, 634 ] ] }, { "id": "IEPA.d161.s388", "type": "", "text": [ "Marked increases in FAT/CD36 (724+/-18%; P < 0.05), PPAR-gamma2 (200+/-8%; P < 0.05), leptin (110+/-13%; P < 0.05), UCP-2 (120+/-7%; P < 0.05), UCP-3 (80+/-5%; P < 0.05), and TNF-alpha mRNA (130+/-12%; P < 0.05) were observed in comparison with pretreatment levels, whereas there was no change after saline infusion" ], "offsets": [ [ 635, 950 ] ] }, { "id": "IEPA.d161.s389", "type": "", "text": [ "These data suggest that the in vivo gene expression of FAT/CD36, PPAR-gamma2, leptin, UCP-2, UCP-3, and TNF-alpha in subcutaneous adipose tissue is regulated by circulating lipids independent of insulin and that prolonged hyperlipidemia may therefore contribute to increased fat metabolism and storage as a result of the increased expression of these proteins" ], "offsets": [ [ 951, 1310 ] ] } ]

[ { "id": "IEPA.d161.s386.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 93, 99 ] ], "normalized": [] }, { "id": "IEPA.d161.s386.e1", "type": "", "text": [ "uncoupling proteins 2" ], "offsets": [ [ 101, 122 ] ], "normalized": [] }, { "id": "IEPA.d161.s386.e2", "type": "", "text": [ "3" ], "offsets": [ [ 127, 128 ] ], "normalized": [] }, { "id": "IEPA.d161.s387.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 357, 363 ] ], "normalized": [] }, { "id": "IEPA.d161.s387.e1", "type": "", "text": [ "uncoupling protein (UCP)-2" ], "offsets": [ [ 365, 391 ] ], "normalized": [] }, { "id": "IEPA.d161.s387.e2", "type": "", "text": [ "UCP-3" ], "offsets": [ [ 396, 401 ] ], "normalized": [] }, { "id": "IEPA.d161.s388.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 721, 727 ] ], "normalized": [] }, { "id": "IEPA.d161.s388.e1", "type": "", "text": [ "UCP-2" ], "offsets": [ [ 751, 756 ] ], "normalized": [] }, { "id": "IEPA.d161.s388.e2", "type": "", "text": [ "UCP-3" ], "offsets": [ [ 779, 784 ] ], "normalized": [] }, { "id": "IEPA.d161.s389.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 1029, 1035 ] ], "normalized": [] }, { "id": "IEPA.d161.s389.e1", "type": "", "text": [ "UCP-2" ], "offsets": [ [ 1037, 1042 ] ], "normalized": [] }, { "id": "IEPA.d161.s389.e2", "type": "", "text": [ "UCP-3" ], "offsets": [ [ 1044, 1049 ] ], "normalized": [] } ]

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[]

[ { "id": "IEPA.d162.s390", "type": "", "text": [ "We previously reported that adiposity and serum leptin levels increase with age in male F-344xBN rats and that when physiological levels of serum leptin are manipulated by fasting, there is a corresponding reciprocal change in hypothalamic neuropeptide Y (NPY) mRNA in young rats, but there are no changes in older rats" ], "offsets": [ [ 0, 319 ] ] }, { "id": "IEPA.d162.s391", "type": "", "text": [ "These findings suggest that the regulation of hypothalamic NPY mRNA by leptin may be impaired with age" ], "offsets": [ [ 320, 422 ] ] }, { "id": "IEPA.d162.s392", "type": "", "text": [ "We examined daily food consumption, body weight, whole-body oxygen consumption, serum leptin, and NPY mRNA in the hypothalamus" ], "offsets": [ [ 423, 549 ] ] }, { "id": "IEPA.d162.s393", "type": "", "text": [ "Leptin infusion diminished hypothalamic NPY levels by nearly 50% compared with pair-fed young rats, whereas there were no changes in the hypothalamic NPY mRNA levels in senescent rats" ], "offsets": [ [ 550, 733 ] ] }, { "id": "IEPA.d162.s394", "type": "", "text": [ "These diminished responses to leptin were associated with and may be the result of an impaired suppression of hypothalamic NPY mRNA levels" ], "offsets": [ [ 734, 872 ] ] } ]

[ { "id": "IEPA.d162.s390.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 48, 54 ] ], "normalized": [] }, { "id": "IEPA.d162.s390.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 146, 152 ] ], "normalized": [] }, { "id": "IEPA.d162.s390.e2", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 240, 254 ] ], "normalized": [] }, { "id": "IEPA.d162.s391.e0", "type": "", "text": [ "NPY" ], "offsets": [ [ 379, 382 ] ], "normalized": [] }, { "id": "IEPA.d162.s391.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 391, 397 ] ], "normalized": [] }, { "id": "IEPA.d162.s392.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 509, 515 ] ], "normalized": [] }, { "id": "IEPA.d162.s392.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 521, 524 ] ], "normalized": [] }, { "id": "IEPA.d162.s393.e0", "type": "", "text": [ "Leptin" ], "offsets": [ [ 550, 556 ] ], "normalized": [] }, { "id": "IEPA.d162.s393.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 590, 593 ] ], "normalized": [] }, { "id": "IEPA.d162.s393.e2", "type": "", "text": [ "NPY" ], "offsets": [ [ 700, 703 ] ], "normalized": [] }, { "id": "IEPA.d162.s394.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 764, 770 ] ], "normalized": [] }, { "id": "IEPA.d162.s394.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 857, 860 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d162.s391.i0", "type": "PPI", "arg1_id": "IEPA.d162.s391.e0", "arg2_id": "IEPA.d162.s391.e1", "normalized": [] }, { "id": "IEPA.d162.s393.i0", "type": "PPI", "arg1_id": "IEPA.d162.s393.e0", "arg2_id": "IEPA.d162.s393.e1", "normalized": [] } ]

[ { "id": "IEPA.d163.s395", "type": "", "text": [ "C75 inhibited expression of the prophagic signal neuropeptide Y in the hypothalamus and acted in a leptin-independent manner that appears to be mediated by malonyl-coenzyme A" ], "offsets": [ [ 0, 174 ] ] } ]

[ { "id": "IEPA.d163.s395.e0", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 49, 63 ] ], "normalized": [] }, { "id": "IEPA.d163.s395.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 99, 105 ] ], "normalized": [] } ]

[]

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[ { "id": "IEPA.d164.s396", "type": "", "text": [ "The aims of this study were: (1) to assess the effects of maternal undernutrition during pregnancy on adult offspring with regard to growth, body composition and plasma levels of glucose, insulin and corticosterone, and (2) to investigate whether oxytocin treatment early in life could ameliorate the adverse effects of food restriction in utero" ], "offsets": [ [ 0, 345 ] ] } ]

[ { "id": "IEPA.d164.s396.e0", "type": "", "text": [ "insulin" ], "offsets": [ [ 188, 195 ] ], "normalized": [] }, { "id": "IEPA.d164.s396.e1", "type": "", "text": [ "oxytocin" ], "offsets": [ [ 247, 255 ] ], "normalized": [] } ]

[]

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[ { "id": "IEPA.d165.s397", "type": "", "text": [ "Interactions between leptin and NPY affecting lipid mobilization in adipose tissue" ], "offsets": [ [ 0, 82 ] ] }, { "id": "IEPA.d165.s398", "type": "", "text": [ "The aim of the current investigations was focused on the study of the involvement of leptin and neuropeptide Y in lipid mobilization" ], "offsets": [ [ 83, 215 ] ] }, { "id": "IEPA.d165.s399", "type": "", "text": [ "The lipolytic rate was assessed through glycerol release after incubation with leptin and NPY at concentrations ranging from 10(-6) to 10(-12) M in isolated adipocytes obtained from female rats" ], "offsets": [ [ 216, 409 ] ] }, { "id": "IEPA.d165.s400", "type": "", "text": [ "At equimolar concentrations of leptin and NPY (10(-12) to 10(-6) M) the observed lipolytic activity is comparable to the basal lipolytic activity, except at a concentration of 10(-9) M where upon a significant increase in lipolysis is observed" ], "offsets": [ [ 410, 653 ] ] }, { "id": "IEPA.d165.s401", "type": "", "text": [ "Summing up, new evidence suggests that NPY and leptin may interact in a homeostatic loop to regulate body-fat mass and energy balance not only at the central nervous system level, but also directly at the adipocyte level" ], "offsets": [ [ 654, 874 ] ] } ]

[ { "id": "IEPA.d165.s397.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 21, 27 ] ], "normalized": [] }, { "id": "IEPA.d165.s397.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 32, 35 ] ], "normalized": [] }, { "id": "IEPA.d165.s398.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 168, 174 ] ], "normalized": [] }, { "id": "IEPA.d165.s398.e1", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 179, 193 ] ], "normalized": [] }, { "id": "IEPA.d165.s399.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 295, 301 ] ], "normalized": [] }, { "id": "IEPA.d165.s399.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 306, 309 ] ], "normalized": [] }, { "id": "IEPA.d165.s400.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 441, 447 ] ], "normalized": [] }, { "id": "IEPA.d165.s400.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 452, 455 ] ], "normalized": [] }, { "id": "IEPA.d165.s401.e0", "type": "", "text": [ "NPY" ], "offsets": [ [ 693, 696 ] ], "normalized": [] }, { "id": "IEPA.d165.s401.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 701, 707 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d165.s397.i0", "type": "PPI", "arg1_id": "IEPA.d165.s397.e0", "arg2_id": "IEPA.d165.s397.e1", "normalized": [] }, { "id": "IEPA.d165.s401.i0", "type": "PPI", "arg1_id": "IEPA.d165.s401.e0", "arg2_id": "IEPA.d165.s401.e1", "normalized": [] } ]

[ { "id": "IEPA.d166.s402", "type": "", "text": [ "The protein kinase C specific inhibitor Go-6983 further enhanced the inhibitory effect of VACM-1 on AVP-stimulated cAMP production" ], "offsets": [ [ 0, 130 ] ] } ]

[ { "id": "IEPA.d166.s402.e0", "type": "", "text": [ "protein kinase C" ], "offsets": [ [ 4, 20 ] ], "normalized": [] }, { "id": "IEPA.d166.s402.e1", "type": "", "text": [ "AVP" ], "offsets": [ [ 100, 103 ] ], "normalized": [] } ]

[]

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[ { "id": "IEPA.d168.s404", "type": "", "text": [ "Involvement of thyroid hormones in the effect of intracerebroventricular leptin infusion on uncoupling protein-3 expression in rat muscle" ], "offsets": [ [ 0, 137 ] ] }, { "id": "IEPA.d168.s405", "type": "", "text": [ "A reduction of food intake imposed on control rats (pair-feeding), aimed at mimicking leptin-induced hyperphagia, produced a marked decrease in the expression of muscle uncoupling protein-3 (UCP-3), whereas ICV infusion of leptin prevented such a decrease in UCP-3" ], "offsets": [ [ 138, 402 ] ] }, { "id": "IEPA.d168.s406", "type": "", "text": [ "To further substantiate an involvement of thyroid hormones in the effect of leptin on muscle UCP-3 expression, hypothyroid rats were ICV infused with leptin or vehicle" ], "offsets": [ [ 403, 570 ] ] }, { "id": "IEPA.d168.s407", "type": "", "text": [ "It was observed that in hypothyroid rats, ICV leptin was unable to maintain muscle UCP-3 expression at values measured in ad libitum fed controls" ], "offsets": [ [ 571, 716 ] ] }, { "id": "IEPA.d168.s408", "type": "", "text": [ "These results suggest that central leptin stimulates T3 production via an activation of T4 to T3 conversion, and that this stimulation could be responsible for the effect of leptin on muscle UCP-3 expression" ], "offsets": [ [ 717, 924 ] ] } ]

[ { "id": "IEPA.d168.s404.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 73, 79 ] ], "normalized": [] }, { "id": "IEPA.d168.s404.e1", "type": "", "text": [ "uncoupling protein-3" ], "offsets": [ [ 92, 112 ] ], "normalized": [] }, { "id": "IEPA.d168.s405.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 224, 230 ] ], "normalized": [] }, { "id": "IEPA.d168.s405.e1", "type": "", "text": [ "uncoupling protein-3" ], "offsets": [ [ 307, 327 ] ], "normalized": [] }, { "id": "IEPA.d168.s405.e2", "type": "", "text": [ "leptin" ], "offsets": [ [ 361, 367 ] ], "normalized": [] }, { "id": "IEPA.d168.s405.e3", "type": "", "text": [ "UCP-3" ], "offsets": [ [ 397, 402 ] ], "normalized": [] }, { "id": "IEPA.d168.s406.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 479, 485 ] ], "normalized": [] }, { "id": "IEPA.d168.s406.e1", "type": "", "text": [ "UCP-3" ], "offsets": [ [ 496, 501 ] ], "normalized": [] }, { "id": "IEPA.d168.s406.e2", "type": "", "text": [ "leptin" ], "offsets": [ [ 553, 559 ] ], "normalized": [] }, { "id": "IEPA.d168.s407.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 617, 623 ] ], "normalized": [] }, { "id": "IEPA.d168.s407.e1", "type": "", "text": [ "UCP-3" ], "offsets": [ [ 654, 659 ] ], "normalized": [] }, { "id": "IEPA.d168.s408.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 752, 758 ] ], "normalized": [] }, { "id": "IEPA.d168.s408.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 891, 897 ] ], "normalized": [] }, { "id": "IEPA.d168.s408.e2", "type": "", "text": [ "UCP-3" ], "offsets": [ [ 908, 913 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d168.s404.i0", "type": "PPI", "arg1_id": "IEPA.d168.s404.e0", "arg2_id": "IEPA.d168.s404.e1", "normalized": [] }, { "id": "IEPA.d168.s405.i0", "type": "PPI", "arg1_id": "IEPA.d168.s405.e0", "arg2_id": "IEPA.d168.s405.e1", "normalized": [] }, { "id": "IEPA.d168.s405.i1", "type": "PPI", "arg1_id": "IEPA.d168.s405.e2", "arg2_id": "IEPA.d168.s405.e3", "normalized": [] }, { "id": "IEPA.d168.s406.i0", "type": "PPI", "arg1_id": "IEPA.d168.s406.e0", "arg2_id": "IEPA.d168.s406.e1", "normalized": [] }, { "id": "IEPA.d168.s407.i0", "type": "PPI", "arg1_id": "IEPA.d168.s407.e0", "arg2_id": "IEPA.d168.s407.e1", "normalized": [] }, { "id": "IEPA.d168.s408.i0", "type": "PPI", "arg1_id": "IEPA.d168.s408.e1", "arg2_id": "IEPA.d168.s408.e2", "normalized": [] } ]

[ { "id": "IEPA.d169.s409", "type": "", "text": [ "The body mass index (BMI), leptin, plasma neuropeptide Y (NPY), serotonin, thyroxine (T4), triiodothyronine (T3) and reverse triiodothyronine (rT3) in serum were evaluated for each subject" ], "offsets": [ [ 0, 188 ] ] } ]

[ { "id": "IEPA.d169.s409.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 27, 33 ] ], "normalized": [] }, { "id": "IEPA.d169.s409.e1", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 42, 56 ] ], "normalized": [] } ]

[]

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[ { "id": "IEPA.d171.s415", "type": "", "text": [ "Phospholipase C (PLC) activity was investigated by stimulation of membrane preparations obtained from insulin (beta-TC3)-, somatostatin (Rin 1027-B2)-, and glucagon (INR1-G9)-producing pancreatic cell lines using the non-hydrolyzable GTP analogue GTPgammaS alone, the C-terminal octapeptide cholecystokinin (CCK-8), or gastrin" ], "offsets": [ [ 0, 326 ] ] } ]

[ { "id": "IEPA.d171.s415.e0", "type": "", "text": [ "Phospholipase C" ], "offsets": [ [ 0, 15 ] ], "normalized": [] }, { "id": "IEPA.d171.s415.e1", "type": "", "text": [ "insulin" ], "offsets": [ [ 102, 109 ] ], "normalized": [] } ]

[]

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[ { "id": "IEPA.d172.s416", "type": "", "text": [ "Therefore, it was examined whether stimulation of Swiss 3T3 cells with insulin causes changes in the subcellular distribution of EGF receptors and phospholipase Cgamma1 that could potentially explain the observed synergy or costimulation." ], "offsets": [ [ 0, 238 ] ] }, { "id": "IEPA.d172.s417", "type": "", "text": [ "However, both EGF and insulin stimulated the accumulation of phospholipase Cgamma1 at the actin arc, which was coincident with the EGF receptor in the case of insulin- stimulated cells." ], "offsets": [ [ 239, 424 ] ] }, { "id": "IEPA.d172.s418", "type": "", "text": [ "Therefore, it is suggested that the insulin-induced coclustering of the EGF receptor with phospholipase Cgamma1 at the actin arc may allow for greater efficiency of signal transduction, resulting in the synergy observed for these two hormones in stimulation of DNA synthesis." ], "offsets": [ [ 425, 700 ] ] } ]

[ { "id": "IEPA.d172.s416.e0", "type": "", "text": [ "insulin" ], "offsets": [ [ 71, 78 ] ], "normalized": [] }, { "id": "IEPA.d172.s416.e1", "type": "", "text": [ "phospholipase Cgamma1" ], "offsets": [ [ 147, 168 ] ], "normalized": [] }, { "id": "IEPA.d172.s417.e0", "type": "", "text": [ "insulin" ], "offsets": [ [ 261, 268 ] ], "normalized": [] }, { "id": "IEPA.d172.s417.e1", "type": "", "text": [ "phospholipase Cgamma1" ], "offsets": [ [ 300, 321 ] ], "normalized": [] }, { "id": "IEPA.d172.s417.e2", "type": "", "text": [ "insulin" ], "offsets": [ [ 398, 405 ] ], "normalized": [] }, { "id": "IEPA.d172.s418.e0", "type": "", "text": [ "insulin" ], "offsets": [ [ 461, 468 ] ], "normalized": [] }, { "id": "IEPA.d172.s418.e1", "type": "", "text": [ "phospholipase Cgamma1" ], "offsets": [ [ 515, 536 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d172.s416.i0", "type": "PPI", "arg1_id": "IEPA.d172.s416.e0", "arg2_id": "IEPA.d172.s416.e1", "normalized": [] }, { "id": "IEPA.d172.s417.i0", "type": "PPI", "arg1_id": "IEPA.d172.s417.e0", "arg2_id": "IEPA.d172.s417.e1", "normalized": [] }, { "id": "IEPA.d172.s418.i0", "type": "PPI", "arg1_id": "IEPA.d172.s418.e0", "arg2_id": "IEPA.d172.s418.e1", "normalized": [] } ]

[ { "id": "IEPA.d173.s419", "type": "", "text": [ "We have established that the recovery of secreted N1 is increased by the protein kinase C agonists PDBu and PMA in a time- and dose-dependent manner in both cell lines" ], "offsets": [ [ 0, 167 ] ] }, { "id": "IEPA.d173.s420", "type": "", "text": [ "In contrast, secretion of N1 remains unaffected by the inactive PDBu analog alphaPDD and by the protein kinase A effectors dibutyryl cAMP and forskolin" ], "offsets": [ [ 168, 319 ] ] }, { "id": "IEPA.d173.s421", "type": "", "text": [ "Overall, our data indicate that the normal processing of PrP(c) is up-regulated by protein kinase C but not protein kinase A in human cells and murine neurons" ], "offsets": [ [ 320, 478 ] ] } ]

[ { "id": "IEPA.d173.s419.e0", "type": "", "text": [ "N1" ], "offsets": [ [ 50, 52 ] ], "normalized": [] }, { "id": "IEPA.d173.s419.e1", "type": "", "text": [ "protein kinase C" ], "offsets": [ [ 73, 89 ] ], "normalized": [] }, { "id": "IEPA.d173.s420.e0", "type": "", "text": [ "N1" ], "offsets": [ [ 194, 196 ] ], "normalized": [] }, { "id": "IEPA.d173.s420.e1", "type": "", "text": [ "protein kinase A" ], "offsets": [ [ 264, 280 ] ], "normalized": [] }, { "id": "IEPA.d173.s421.e0", "type": "", "text": [ "PrP(c)" ], "offsets": [ [ 377, 383 ] ], "normalized": [] }, { "id": "IEPA.d173.s421.e1", "type": "", "text": [ "protein kinase C" ], "offsets": [ [ 403, 419 ] ], "normalized": [] }, { "id": "IEPA.d173.s421.e2", "type": "", "text": [ "protein kinase A" ], "offsets": [ [ 428, 444 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d173.s421.i0", "type": "PPI", "arg1_id": "IEPA.d173.s421.e0", "arg2_id": "IEPA.d173.s421.e1", "normalized": [] } ]

[ { "id": "IEPA.d174.s422", "type": "", "text": [ "Dietary intakes of flavonols, flavones and isoflavones by Japanese women and the inverse correlation between quercetin intake and plasma LDL cholesterol concentration" ], "offsets": [ [ 0, 166 ] ] }, { "id": "IEPA.d174.s423", "type": "", "text": [ "The total intake of flavonoids was inversely correlated with the plasma total cholesterol concentration (TC) (r = -0.236, P: < 0.05) and plasma LDL cholesterol concentration (LDL-C) (r = -0.220, P: < 0.05), after the adjustment for age, body mass index and total energy intake" ], "offsets": [ [ 167, 443 ] ] } ]

[ { "id": "IEPA.d174.s422.e0", "type": "", "text": [ "flavonols" ], "offsets": [ [ 19, 28 ] ], "normalized": [] }, { "id": "IEPA.d174.s422.e1", "type": "", "text": [ "flavones" ], "offsets": [ [ 30, 38 ] ], "normalized": [] }, { "id": "IEPA.d174.s422.e2", "type": "", "text": [ "isoflavones" ], "offsets": [ [ 43, 54 ] ], "normalized": [] }, { "id": "IEPA.d174.s422.e3", "type": "", "text": [ "cholesterol" ], "offsets": [ [ 141, 152 ] ], "normalized": [] }, { "id": "IEPA.d174.s423.e0", "type": "", "text": [ "flavonoids" ], "offsets": [ [ 187, 197 ] ], "normalized": [] }, { "id": "IEPA.d174.s423.e1", "type": "", "text": [ "cholesterol" ], "offsets": [ [ 245, 256 ] ], "normalized": [] }, { "id": "IEPA.d174.s423.e2", "type": "", "text": [ "cholesterol" ], "offsets": [ [ 315, 326 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d174.s422.i0", "type": "PPI", "arg1_id": "IEPA.d174.s422.e0", "arg2_id": "IEPA.d174.s422.e3", "normalized": [] }, { "id": "IEPA.d174.s422.i1", "type": "PPI", "arg1_id": "IEPA.d174.s422.e1", "arg2_id": "IEPA.d174.s422.e3", "normalized": [] }, { "id": "IEPA.d174.s422.i2", "type": "PPI", "arg1_id": "IEPA.d174.s422.e2", "arg2_id": "IEPA.d174.s422.e3", "normalized": [] }, { "id": "IEPA.d174.s423.i0", "type": "PPI", "arg1_id": "IEPA.d174.s423.e0", "arg2_id": "IEPA.d174.s423.e1", "normalized": [] }, { "id": "IEPA.d174.s423.i1", "type": "PPI", "arg1_id": "IEPA.d174.s423.e0", "arg2_id": "IEPA.d174.s423.e2", "normalized": [] } ]

[ { "id": "IEPA.d175.s424", "type": "", "text": [ "Although the above data are consistent with a direct ability of leptin to promote TRH biosynthesis through actions on TRH neurons, addition of a-MSH produced a 3.5 fold increase in TRH biosynthesis and release, whereas NPY treatment suppressed ~3 fold proTRH biosynthesis" ], "offsets": [ [ 0, 271 ] ] } ]

[ { "id": "IEPA.d175.s424.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 64, 70 ] ], "normalized": [] }, { "id": "IEPA.d175.s424.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 219, 222 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "IEPA.d176.s425", "type": "", "text": [ "For example, leptin suppresses neuropeptide Y (NPY) expression in the arcuate nucleus" ], "offsets": [ [ 0, 85 ] ] } ]

[ { "id": "IEPA.d176.s425.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 13, 19 ] ], "normalized": [] }, { "id": "IEPA.d176.s425.e1", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 31, 45 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d176.s425.i0", "type": "PPI", "arg1_id": "IEPA.d176.s425.e0", "arg2_id": "IEPA.d176.s425.e1", "normalized": [] } ]

[ { "id": "IEPA.d177.s426", "type": "", "text": [ "As expected, in fusion of NPY alone (18 microg/day) augmented food intake (191.6% over the initial control, P < 0.05) and produced a 25.1% weight gain in conjunction with a 10-fold increase in serum leptin concentrations at the end of the 7-day period" ], "offsets": [ [ 0, 251 ] ] }, { "id": "IEPA.d177.s427", "type": "", "text": [ "Interestingly, coinfusion of this regimen of NPY with the highly effective anorectic and body reducing effects of CNTF (5.0 microg/day) not only prevented the CNTF-induced anorexia and weight loss, but also normalized serum leptin concentrations and hypothalamic NPY gene expression" ], "offsets": [ [ 252, 534 ] ] }, { "id": "IEPA.d177.s428", "type": "", "text": [ "These results demonstrate that chronic central infusion to produce a persistent elevation of the cytokine at pathophysiological levels (a situation that may normally manifest during infection, injury and inflammation) produced severe anorexia and weight loss in conjunction with reduction in both serum leptin concentrations and hypothalamic NPY gene expression" ], "offsets": [ [ 535, 896 ] ] } ]

[ { "id": "IEPA.d177.s426.e0", "type": "", "text": [ "NPY" ], "offsets": [ [ 26, 29 ] ], "normalized": [] }, { "id": "IEPA.d177.s426.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 199, 205 ] ], "normalized": [] }, { "id": "IEPA.d177.s427.e0", "type": "", "text": [ "NPY" ], "offsets": [ [ 297, 300 ] ], "normalized": [] }, { "id": "IEPA.d177.s427.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 476, 482 ] ], "normalized": [] }, { "id": "IEPA.d177.s427.e2", "type": "", "text": [ "NPY" ], "offsets": [ [ 515, 518 ] ], "normalized": [] }, { "id": "IEPA.d177.s428.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 838, 844 ] ], "normalized": [] }, { "id": "IEPA.d177.s428.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 877, 880 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d177.s426.i0", "type": "PPI", "arg1_id": "IEPA.d177.s426.e0", "arg2_id": "IEPA.d177.s426.e1", "normalized": [] }, { "id": "IEPA.d177.s427.i0", "type": "PPI", "arg1_id": "IEPA.d177.s427.e0", "arg2_id": "IEPA.d177.s427.e1", "normalized": [] } ]

[ { "id": "IEPA.d178.s429", "type": "", "text": [ "A caveolin-1-dependent coupling of PrPc to the tyrosine kinase Fyn was observed" ], "offsets": [ [ 0, 79 ] ] } ]

[ { "id": "IEPA.d178.s429.e0", "type": "", "text": [ "PrPc" ], "offsets": [ [ 35, 39 ] ], "normalized": [] }, { "id": "IEPA.d178.s429.e1", "type": "", "text": [ "tyrosine kinase Fyn" ], "offsets": [ [ 47, 66 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d178.s429.i0", "type": "PPI", "arg1_id": "IEPA.d178.s429.e0", "arg2_id": "IEPA.d178.s429.e1", "normalized": [] } ]

[ { "id": "IEPA.d179.s430", "type": "", "text": [ "Recently several significant advances have been made in this area, including the identification of the appetite regulating hormone, leptin, and a detailed understanding of its targets in the central nervous system (CNS), such as neuropeptide Y (NPY) and the melanocortin-4 receptor" ], "offsets": [ [ 0, 281 ] ] } ]

[ { "id": "IEPA.d179.s430.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 132, 138 ] ], "normalized": [] }, { "id": "IEPA.d179.s430.e1", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 229, 243 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d179.s430.i0", "type": "PPI", "arg1_id": "IEPA.d179.s430.e0", "arg2_id": "IEPA.d179.s430.e1", "normalized": [] } ]

[ { "id": "IEPA.d180.s431", "type": "", "text": [ "A loop system exists between hypothalamic neuropeptide Y (NPY) and peripheral adipose tissue leptin to maintain normal body homeostasis" ], "offsets": [ [ 0, 135 ] ] }, { "id": "IEPA.d180.s432", "type": "", "text": [ "When infused i.c.v. to normal rats to mimic its central effects, leptin decreases NPY levels, thus food intake and body weight" ], "offsets": [ [ 136, 262 ] ] }, { "id": "IEPA.d180.s433", "type": "", "text": [ "Circadian fluctuations of NPY and leptin levels maintain normal body homeostasis" ], "offsets": [ [ 263, 343 ] ] }, { "id": "IEPA.d180.s434", "type": "", "text": [ "Leptin increases the expression of uncoupling proteins (UCP-1, -2, -3) and thus energy dissipation" ], "offsets": [ [ 344, 442 ] ] } ]

[ { "id": "IEPA.d180.s431.e0", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 42, 56 ] ], "normalized": [] }, { "id": "IEPA.d180.s431.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 93, 99 ] ], "normalized": [] }, { "id": "IEPA.d180.s432.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 201, 207 ] ], "normalized": [] }, { "id": "IEPA.d180.s432.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 218, 221 ] ], "normalized": [] }, { "id": "IEPA.d180.s433.e0", "type": "", "text": [ "NPY" ], "offsets": [ [ 289, 292 ] ], "normalized": [] }, { "id": "IEPA.d180.s433.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 297, 303 ] ], "normalized": [] }, { "id": "IEPA.d180.s434.e0", "type": "", "text": [ "Leptin" ], "offsets": [ [ 344, 350 ] ], "normalized": [] }, { "id": "IEPA.d180.s434.e1", "type": "", "text": [ "uncoupling proteins" ], "offsets": [ [ 379, 398 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d180.s431.i0", "type": "PPI", "arg1_id": "IEPA.d180.s431.e0", "arg2_id": "IEPA.d180.s431.e1", "normalized": [] }, { "id": "IEPA.d180.s432.i0", "type": "PPI", "arg1_id": "IEPA.d180.s432.e0", "arg2_id": "IEPA.d180.s432.e1", "normalized": [] }, { "id": "IEPA.d180.s434.i0", "type": "PPI", "arg1_id": "IEPA.d180.s434.e0", "arg2_id": "IEPA.d180.s434.e1", "normalized": [] } ]

[ { "id": "IEPA.d181.s435", "type": "", "text": [ "Activity and expression of the three UCP's are stimulated by several neuromediators and hormones such as noradrenaline, tri-iodothyronine and leptin" ], "offsets": [ [ 0, 148 ] ] } ]

[ { "id": "IEPA.d181.s435.e0", "type": "", "text": [ "UCP" ], "offsets": [ [ 37, 40 ] ], "normalized": [] }, { "id": "IEPA.d181.s435.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 142, 148 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d181.s435.i0", "type": "PPI", "arg1_id": "IEPA.d181.s435.e0", "arg2_id": "IEPA.d181.s435.e1", "normalized": [] } ]

[ { "id": "IEPA.d182.s436", "type": "", "text": [ "The effect of leptin in adult rats appears to be exerted at hypothalamic level by regulating growth hormone releasing hormone (GHRH), somatostatin and neuropeptide Y (NPY)-producing neurones" ], "offsets": [ [ 0, 190 ] ] } ]

[ { "id": "IEPA.d182.s436.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 14, 20 ] ], "normalized": [] }, { "id": "IEPA.d182.s436.e1", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 151, 165 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d182.s436.i0", "type": "PPI", "arg1_id": "IEPA.d182.s436.e0", "arg2_id": "IEPA.d182.s436.e1", "normalized": [] } ]

[ { "id": "IEPA.d183.s437", "type": "", "text": [ "Plasma insulin, cholecystokinin, galanin, neuropeptide Y and leptin levels in obese women with and without type 2 diabetes mellitus" ], "offsets": [ [ 0, 131 ] ] }, { "id": "IEPA.d183.s438", "type": "", "text": [ "Experimental studies provided evidences that leptin, cholecystokinin (CCK), galanin (GAL), neuropeptide Y (NPY) and insulin are involved in feeding behaviour" ], "offsets": [ [ 132, 289 ] ] }, { "id": "IEPA.d183.s439", "type": "", "text": [ "Plasma concentrations of FSH, leptin, CCK, GAL, NPY and insulin were determined using commercial RIA kits" ], "offsets": [ [ 290, 395 ] ] }, { "id": "IEPA.d183.s440", "type": "", "text": [ "Our results, ie higher mean plasma NPY levels in postmenopausal diabetic women and positive correlation of CCK with leptin and insulin, may suggest the role of these neuropeptides in metabolic disorders leading to type 2 diabetes mellitus" ], "offsets": [ [ 396, 634 ] ] } ]

[ { "id": "IEPA.d183.s437.e0", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 42, 56 ] ], "normalized": [] }, { "id": "IEPA.d183.s437.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 61, 67 ] ], "normalized": [] }, { "id": "IEPA.d183.s438.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 177, 183 ] ], "normalized": [] }, { "id": "IEPA.d183.s438.e1", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 223, 237 ] ], "normalized": [] }, { "id": "IEPA.d183.s439.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 320, 326 ] ], "normalized": [] }, { "id": "IEPA.d183.s439.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 338, 341 ] ], "normalized": [] }, { "id": "IEPA.d183.s440.e0", "type": "", "text": [ "NPY" ], "offsets": [ [ 431, 434 ] ], "normalized": [] }, { "id": "IEPA.d183.s440.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 512, 518 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "IEPA.d184.s441", "type": "", "text": [ "These results suggest that T3 may increase UCP family expression independent of leptin action" ], "offsets": [ [ 0, 93 ] ] } ]

[ { "id": "IEPA.d184.s441.e0", "type": "", "text": [ "UCP" ], "offsets": [ [ 43, 46 ] ], "normalized": [] }, { "id": "IEPA.d184.s441.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 80, 86 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "IEPA.d185.s442", "type": "", "text": [ "The ARC NPY neurones are stimulated by starvation, probably mediated by falls in circulating leptin and insulin (which both inhibit these neurones), and contribute to the increased hunger in this and other conditions of energy deficit" ], "offsets": [ [ 0, 234 ] ] }, { "id": "IEPA.d185.s443", "type": "", "text": [ "ARC NPY neurones also mediate hyperphagia and obesity in the ob/ob and db/db mice and fa/fa rat, in which leptin inhibition is lost through mutations affecting leptin or its receptor" ], "offsets": [ [ 235, 417 ] ] } ]

[ { "id": "IEPA.d185.s442.e0", "type": "", "text": [ "NPY" ], "offsets": [ [ 8, 11 ] ], "normalized": [] }, { "id": "IEPA.d185.s442.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 93, 99 ] ], "normalized": [] }, { "id": "IEPA.d185.s443.e0", "type": "", "text": [ "NPY" ], "offsets": [ [ 239, 242 ] ], "normalized": [] }, { "id": "IEPA.d185.s443.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 341, 347 ] ], "normalized": [] }, { "id": "IEPA.d185.s443.e2", "type": "", "text": [ "leptin" ], "offsets": [ [ 395, 401 ] ], "normalized": [] } ]

[]

[]

[]

[ { "id": "IEPA.d186.s444", "type": "", "text": [ "Insulin secretion, inositol phosphate levels, and phospholipase C isozymes in rodent pancreatic islets" ], "offsets": [ [ 0, 102 ] ] }, { "id": "IEPA.d186.s445", "type": "", "text": [ "These findings are consistent with the concept that the underexpression of the nutrient-activated PLC isozyme may account for the minimal inositol phosphate (IP) and second-phase insulin secretory response from mouse islets" ], "offsets": [ [ 103, 326 ] ] } ]

[ { "id": "IEPA.d186.s444.e0", "type": "", "text": [ "Insulin" ], "offsets": [ [ 0, 7 ] ], "normalized": [] }, { "id": "IEPA.d186.s444.e1", "type": "", "text": [ "phospholipase C" ], "offsets": [ [ 50, 65 ] ], "normalized": [] }, { "id": "IEPA.d186.s445.e0", "type": "", "text": [ "PLC" ], "offsets": [ [ 201, 204 ] ], "normalized": [] }, { "id": "IEPA.d186.s445.e1", "type": "", "text": [ "insulin" ], "offsets": [ [ 282, 289 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d186.s445.i0", "type": "PPI", "arg1_id": "IEPA.d186.s445.e0", "arg2_id": "IEPA.d186.s445.e1", "normalized": [] } ]

[ { "id": "IEPA.d187.s446", "type": "", "text": [ "Gibbestatin B inhibits the GA-induced expression of alpha-amylase expression in cereal seeds [In Process Citation]" ], "offsets": [ [ 0, 114 ] ] }, { "id": "IEPA.d187.s447", "type": "", "text": [ "The expression of alpha-amylase in aleurone layers of barley is known to be induced by gibberellin A3 (GA)." ], "offsets": [ [ 115, 222 ] ] }, { "id": "IEPA.d187.s448", "type": "", "text": [ "In the present study, gibbestatin B (GNB) was isolated from Streptomyces sp. C-39 as an inhibitor of the GA-induced expression of alpha-amylase in barley and rice, with IC50 values of 125 and 70 microM, respectively." ], "offsets": [ [ 223, 439 ] ] }, { "id": "IEPA.d187.s449", "type": "", "text": [ "GNB suppressed accumulation of GA-induced barley high-pI type B and rice RAmylA alpha-amylase transcripts." ], "offsets": [ [ 440, 546 ] ] }, { "id": "IEPA.d187.s450", "type": "", "text": [ "These analyses indicate that GNB inhibits the GA-induced expression of alpha-amylase by regulating one of the steps involved in ABA signaling, but not by acting as a weak ABA analog." ], "offsets": [ [ 547, 729 ] ] } ]

[ { "id": "IEPA.d187.s446.e0", "type": "", "text": [ "GA" ], "offsets": [ [ 27, 29 ] ], "normalized": [] }, { "id": "IEPA.d187.s446.e1", "type": "", "text": [ "alpha-amylase" ], "offsets": [ [ 52, 65 ] ], "normalized": [] }, { "id": "IEPA.d187.s447.e0", "type": "", "text": [ "alpha-amylase" ], "offsets": [ [ 133, 146 ] ], "normalized": [] }, { "id": "IEPA.d187.s447.e1", "type": "", "text": [ "gibberellin A3" ], "offsets": [ [ 202, 216 ] ], "normalized": [] }, { "id": "IEPA.d187.s448.e0", "type": "", "text": [ "GA" ], "offsets": [ [ 328, 330 ] ], "normalized": [] }, { "id": "IEPA.d187.s448.e1", "type": "", "text": [ "alpha-amylase" ], "offsets": [ [ 353, 366 ] ], "normalized": [] }, { "id": "IEPA.d187.s449.e0", "type": "", "text": [ "GA" ], "offsets": [ [ 471, 473 ] ], "normalized": [] }, { "id": "IEPA.d187.s449.e1", "type": "", "text": [ "alpha-amylase" ], "offsets": [ [ 520, 533 ] ], "normalized": [] }, { "id": "IEPA.d187.s450.e0", "type": "", "text": [ "GA" ], "offsets": [ [ 593, 595 ] ], "normalized": [] }, { "id": "IEPA.d187.s450.e1", "type": "", "text": [ "alpha-amylase" ], "offsets": [ [ 618, 631 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d187.s446.i0", "type": "PPI", "arg1_id": "IEPA.d187.s446.e0", "arg2_id": "IEPA.d187.s446.e1", "normalized": [] }, { "id": "IEPA.d187.s447.i0", "type": "PPI", "arg1_id": "IEPA.d187.s447.e0", "arg2_id": "IEPA.d187.s447.e1", "normalized": [] }, { "id": "IEPA.d187.s448.i0", "type": "PPI", "arg1_id": "IEPA.d187.s448.e0", "arg2_id": "IEPA.d187.s448.e1", "normalized": [] }, { "id": "IEPA.d187.s449.i0", "type": "PPI", "arg1_id": "IEPA.d187.s449.e0", "arg2_id": "IEPA.d187.s449.e1", "normalized": [] }, { "id": "IEPA.d187.s450.i0", "type": "PPI", "arg1_id": "IEPA.d187.s450.e0", "arg2_id": "IEPA.d187.s450.e1", "normalized": [] } ]

[ { "id": "IEPA.d188.s451", "type": "", "text": [ "We also determined whether well known hypothalamic neuropeptide targets, e.g. neuropeptide Y (NPY), proopiomelanocortin (POMC), agouti-related peptide (AGRP) and cocaine and amphetamine-regulated transcript (CART) were regulated in a pattern consistent with their presumed roles as mediators of leptin action" ], "offsets": [ [ 0, 308 ] ] }, { "id": "IEPA.d188.s452", "type": "", "text": [ "In contrast, leptin decreased body weight and adiposity, increased CART and suppressed NPY and AGRP mRNA expression in adult mice" ], "offsets": [ [ 309, 438 ] ] } ]

[ { "id": "IEPA.d188.s451.e0", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 78, 92 ] ], "normalized": [] }, { "id": "IEPA.d188.s451.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 295, 301 ] ], "normalized": [] }, { "id": "IEPA.d188.s452.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 322, 328 ] ], "normalized": [] }, { "id": "IEPA.d188.s452.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 396, 399 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d188.s451.i0", "type": "PPI", "arg1_id": "IEPA.d188.s451.e0", "arg2_id": "IEPA.d188.s451.e1", "normalized": [] }, { "id": "IEPA.d188.s452.i0", "type": "PPI", "arg1_id": "IEPA.d188.s452.e0", "arg2_id": "IEPA.d188.s452.e1", "normalized": [] } ]

[ { "id": "IEPA.d190.s454", "type": "", "text": [ "Leptin effects on pulsatile gonadotropin releasing hormone secretion from the adult rat hypothalamus and interaction with cocaine and amphetamine regulated transcript peptide and neuropeptide Y [In Process Citation]" ], "offsets": [ [ 0, 215 ] ] }, { "id": "IEPA.d190.s455", "type": "", "text": [ "Leptin may act as a negative feedback signal to the hypothalamic control of appetite through suppression of neuropeptide Y (NPY) secretion and stimulation of cocaine and amphetamine regulated transcript (CART)." ], "offsets": [ [ 216, 426 ] ] }, { "id": "IEPA.d190.s456", "type": "", "text": [ "We aimed at studying the effects of leptin, CART and NPY on the hypothalamic control of the pituitary-gonadal system." ], "offsets": [ [ 427, 544 ] ] }, { "id": "IEPA.d190.s457", "type": "", "text": [ "The increase in GnRH pulse amplitude caused by leptin was totally prevented by coincubation with an anti-CART antiserum whereas it was not affected by coincubation with the NPY Y5-receptor antagonist (10(-7) M)." ], "offsets": [ [ 545, 756 ] ] }, { "id": "IEPA.d190.s458", "type": "", "text": [ "In conclusion, leptin and NPY show separate permissive effects on GnRH secretion in the adult rat hypothalamus." ], "offsets": [ [ 757, 868 ] ] } ]

[ { "id": "IEPA.d190.s454.e0", "type": "", "text": [ "Leptin" ], "offsets": [ [ 0, 6 ] ], "normalized": [] }, { "id": "IEPA.d190.s454.e1", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 179, 193 ] ], "normalized": [] }, { "id": "IEPA.d190.s455.e0", "type": "", "text": [ "Leptin" ], "offsets": [ [ 216, 222 ] ], "normalized": [] }, { "id": "IEPA.d190.s455.e1", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 324, 338 ] ], "normalized": [] }, { "id": "IEPA.d190.s456.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 463, 469 ] ], "normalized": [] }, { "id": "IEPA.d190.s456.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 480, 483 ] ], "normalized": [] }, { "id": "IEPA.d190.s457.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 592, 598 ] ], "normalized": [] }, { "id": "IEPA.d190.s457.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 718, 721 ] ], "normalized": [] }, { "id": "IEPA.d190.s458.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 772, 778 ] ], "normalized": [] }, { "id": "IEPA.d190.s458.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 783, 786 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d190.s454.i0", "type": "PPI", "arg1_id": "IEPA.d190.s454.e0", "arg2_id": "IEPA.d190.s454.e1", "normalized": [] }, { "id": "IEPA.d190.s455.i0", "type": "PPI", "arg1_id": "IEPA.d190.s455.e0", "arg2_id": "IEPA.d190.s455.e1", "normalized": [] } ]

[ { "id": "IEPA.d191.s459", "type": "", "text": [ "Similarly, central leptin treatment also had a greater effect in suppressing hypothalamic NPY mRNA expression in young (-23+/-4%) than in old (-8+/-4%) rats compared with their age-matched pair-fed treated rats" ], "offsets": [ [ 0, 210 ] ] } ]

[ { "id": "IEPA.d191.s459.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 19, 25 ] ], "normalized": [] }, { "id": "IEPA.d191.s459.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 90, 93 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d191.s459.i0", "type": "PPI", "arg1_id": "IEPA.d191.s459.e0", "arg2_id": "IEPA.d191.s459.e1", "normalized": [] } ]

[ { "id": "IEPA.d192.s460", "type": "", "text": [ "Compared with the wild type, GA induction of alpha-amylase activity in aleurone cells of d1 was greatly reduced" ], "offsets": [ [ 0, 111 ] ] }, { "id": "IEPA.d192.s461", "type": "", "text": [ "Relative to the wild type, the GA(3)-treated aleurone layer of d1 had lower expression of Ramy1A, which encodes alpha-amylase, and OsGAMYB, which encodes a GA-inducible transcriptional factor, and no increase in expression of Ca(2 +)-ATPase" ], "offsets": [ [ 112, 352 ] ] }, { "id": "IEPA.d192.s462", "type": "", "text": [ "However, in the presence of high GA concentrations, alpha-amylase induction occurred even in d1" ], "offsets": [ [ 353, 448 ] ] }, { "id": "IEPA.d192.s463", "type": "", "text": [ "All these results suggest that d1 affects a part of the GA-signaling pathway, namely the induction of alpha-amylase in the aleurone layer and internode elongation" ], "offsets": [ [ 449, 611 ] ] } ]

[ { "id": "IEPA.d192.s460.e0", "type": "", "text": [ "GA" ], "offsets": [ [ 29, 31 ] ], "normalized": [] }, { "id": "IEPA.d192.s460.e1", "type": "", "text": [ "alpha-amylase" ], "offsets": [ [ 45, 58 ] ], "normalized": [] }, { "id": "IEPA.d192.s461.e0", "type": "", "text": [ "GA" ], "offsets": [ [ 143, 145 ] ], "normalized": [] }, { "id": "IEPA.d192.s461.e1", "type": "", "text": [ "alpha-amylase" ], "offsets": [ [ 224, 237 ] ], "normalized": [] }, { "id": "IEPA.d192.s461.e2", "type": "", "text": [ "GA" ], "offsets": [ [ 268, 270 ] ], "normalized": [] }, { "id": "IEPA.d192.s462.e0", "type": "", "text": [ "GA" ], "offsets": [ [ 386, 388 ] ], "normalized": [] }, { "id": "IEPA.d192.s462.e1", "type": "", "text": [ "alpha-amylase" ], "offsets": [ [ 405, 418 ] ], "normalized": [] }, { "id": "IEPA.d192.s463.e0", "type": "", "text": [ "GA" ], "offsets": [ [ 505, 507 ] ], "normalized": [] }, { "id": "IEPA.d192.s463.e1", "type": "", "text": [ "alpha-amylase" ], "offsets": [ [ 551, 564 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d192.s460.i0", "type": "PPI", "arg1_id": "IEPA.d192.s460.e0", "arg2_id": "IEPA.d192.s460.e1", "normalized": [] }, { "id": "IEPA.d192.s461.i0", "type": "PPI", "arg1_id": "IEPA.d192.s461.e0", "arg2_id": "IEPA.d192.s461.e1", "normalized": [] }, { "id": "IEPA.d192.s462.i0", "type": "PPI", "arg1_id": "IEPA.d192.s462.e0", "arg2_id": "IEPA.d192.s462.e1", "normalized": [] }, { "id": "IEPA.d192.s463.i0", "type": "PPI", "arg1_id": "IEPA.d192.s463.e0", "arg2_id": "IEPA.d192.s463.e1", "normalized": [] } ]

[ { "id": "IEPA.d193.s464", "type": "", "text": [ "Finally, recent evidences suggest that melanocortins could be involved in mediating the effects of leptin, and in controlling the expression of neuropeptide Y (NPY)" ], "offsets": [ [ 0, 164 ] ] } ]

[ { "id": "IEPA.d193.s464.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 99, 105 ] ], "normalized": [] }, { "id": "IEPA.d193.s464.e1", "type": "", "text": [ "neuropeptide Y" ], "offsets": [ [ 144, 158 ] ], "normalized": [] } ]

[]

[]

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[ { "id": "IEPA.d194.s465", "type": "", "text": [ "Insulin-induced phospholipase D1 and phospholipase D2 activity in human embryonic kidney-293 cells mediated by the phospholipase Cgamma and protein kinase Calpha signalling cascade." ], "offsets": [ [ 0, 181 ] ] }, { "id": "IEPA.d194.s466", "type": "", "text": [ "Co-expression of PLD1 with phospholipase C (PLC)gamma has the same effect, while co-expression of PLD2 with PLCgamma allows PLD2 activity to be stimulated in an insulin-dependent manner." ], "offsets": [ [ 182, 368 ] ] }, { "id": "IEPA.d194.s467", "type": "", "text": [ "The PKC-specific inhibitors bisindolylmaleimide and Go 6976 abolish insulin-induced PLD2 activation in HEK-293 cells co-expressing the insulin receptor, PLCgamma and PLD2, confirming that not only PLD1, but PLD2 as well, is regulated in a PKC-dependent manner." ], "offsets": [ [ 369, 629 ] ] }, { "id": "IEPA.d194.s468", "type": "", "text": [ "In summary, we demonstrate that insulin treatment results in activation of both PLD1 and PLD2 in appropriate cell types when the appropriate upstream intermediate signalling components, i.e. PKCalpha and PLCgamma, are expressed at sufficient levels." ], "offsets": [ [ 630, 879 ] ] } ]

[ { "id": "IEPA.d194.s465.e0", "type": "", "text": [ "Insulin" ], "offsets": [ [ 0, 7 ] ], "normalized": [] }, { "id": "IEPA.d194.s465.e1", "type": "", "text": [ "phospholipase Cgamma" ], "offsets": [ [ 115, 135 ] ], "normalized": [] }, { "id": "IEPA.d194.s466.e0", "type": "", "text": [ "phospholipase C (PLC)gamma" ], "offsets": [ [ 209, 235 ] ], "normalized": [] }, { "id": "IEPA.d194.s466.e1", "type": "", "text": [ "PLCgamma" ], "offsets": [ [ 290, 298 ] ], "normalized": [] }, { "id": "IEPA.d194.s466.e2", "type": "", "text": [ "insulin" ], "offsets": [ [ 343, 350 ] ], "normalized": [] }, { "id": "IEPA.d194.s467.e0", "type": "", "text": [ "insulin" ], "offsets": [ [ 437, 444 ] ], "normalized": [] }, { "id": "IEPA.d194.s467.e1", "type": "", "text": [ "PLCgamma" ], "offsets": [ [ 522, 530 ] ], "normalized": [] }, { "id": "IEPA.d194.s468.e0", "type": "", "text": [ "insulin" ], "offsets": [ [ 662, 669 ] ], "normalized": [] }, { "id": "IEPA.d194.s468.e1", "type": "", "text": [ "PLCgamma" ], "offsets": [ [ 834, 842 ] ], "normalized": [] } ]

[]

[]

[ { "id": "IEPA.d194.s465.i0", "type": "PPI", "arg1_id": "IEPA.d194.s465.e0", "arg2_id": "IEPA.d194.s465.e1", "normalized": [] }, { "id": "IEPA.d194.s468.i0", "type": "PPI", "arg1_id": "IEPA.d194.s468.e0", "arg2_id": "IEPA.d194.s468.e1", "normalized": [] } ]

[ { "id": "IEPA.d196.s476", "type": "", "text": [ "Both receive information about the nutritional status and the level of energy storage through insulin and leptin signaling mediated by specific receptors located on POMC and NPY neurons present predominantly in the arcuate nucleus (ARC)." ], "offsets": [ [ 0, 237 ] ] }, { "id": "IEPA.d196.s477", "type": "", "text": [ "When leptin signaling is defective, through a defect in either the receptor (Zucker fa/fa rat, cp/cp rat, and db/db mouse) or in the peptide itself (ob/ob mouse), the NPY system is upregulated as shown by mRNA overexpression and increased peptide release, whereas the content and/or release of some inhibitory peptides (neurotensin, cholecystokinin) are diminished." ], "offsets": [ [ 238, 603 ] ] } ]

[ { "id": "IEPA.d196.s476.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 106, 112 ] ], "normalized": [] }, { "id": "IEPA.d196.s476.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 174, 177 ] ], "normalized": [] }, { "id": "IEPA.d196.s477.e0", "type": "", "text": [ "leptin" ], "offsets": [ [ 243, 249 ] ], "normalized": [] }, { "id": "IEPA.d196.s477.e1", "type": "", "text": [ "NPY" ], "offsets": [ [ 405, 408 ] ], "normalized": [] } ]

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[ { "id": "IEPA.d197.s478", "type": "", "text": [ "Bovine prion protein as a modulator of protein kinase CK2" ], "offsets": [ [ 0, 57 ] ] }, { "id": "IEPA.d197.s479", "type": "", "text": [ "On the basis of far-Western blot and plasmon resonance (BIAcore) experiments, we show here that recombinant bovine prion protein (bPrP) (25-242) strongly interacts with the catalytic alpha/alpha' subunits of protein kinase CK2 (also termed 'casein kinase 2')" ], "offsets": [ [ 58, 316 ] ] }, { "id": "IEPA.d197.s480", "type": "", "text": [ "We also show that bPrP counteracts the inhibition of calmodulin phosphorylation promoted by the regulatory beta subunits of CK2" ], "offsets": [ [ 317, 444 ] ] }, { "id": "IEPA.d197.s481", "type": "", "text": [ "A truncated form of bPrP encompassing the C-terminal domain (residues 105-242) interacts with CK2 but does not affect its catalytic activity" ], "offsets": [ [ 445, 585 ] ] }, { "id": "IEPA.d197.s482", "type": "", "text": [ "These results disclose the potential of the PrP to modulate the activity of CK2, a pleiotropic protein kinase that is particularly abundant in the brain" ], "offsets": [ [ 586, 738 ] ] } ]

[ { "id": "IEPA.d197.s478.e0", "type": "", "text": [ "Bovine prion protein" ], "offsets": [ [ 0, 20 ] ], "normalized": [] }, { "id": "IEPA.d197.s478.e1", "type": "", "text": [ "protein kinase CK2" ], "offsets": [ [ 39, 57 ] ], "normalized": [] }, { "id": "IEPA.d197.s479.e0", "type": "", "text": [ "bovine prion protein" ], "offsets": [ [ 166, 186 ] ], "normalized": [] }, { "id": "IEPA.d197.s479.e1", "type": "", "text": [ "protein kinase CK2" ], "offsets": [ [ 266, 284 ] ], "normalized": [] }, { "id": "IEPA.d197.s480.e0", "type": "", "text": [ "bPrP" ], "offsets": [ [ 335, 339 ] ], "normalized": [] }, { "id": "IEPA.d197.s480.e1", "type": "", "text": [ "CK2" ], "offsets": [ [ 441, 444 ] ], "normalized": [] }, { "id": "IEPA.d197.s481.e0", "type": "", "text": [ "bPrP" ], "offsets": [ [ 465, 469 ] ], "normalized": [] }, { "id": "IEPA.d197.s481.e1", "type": "", "text": [ "CK2" ], "offsets": [ [ 539, 542 ] ], "normalized": [] }, { "id": "IEPA.d197.s482.e0", "type": "", "text": [ "PrP" ], "offsets": [ [ 630, 633 ] ], "normalized": [] }, { "id": "IEPA.d197.s482.e1", "type": "", "text": [ "CK2" ], "offsets": [ [ 662, 665 ] ], "normalized": [] }, { "id": "IEPA.d197.s482.e2", "type": "", "text": [ "protein kinase" ], "offsets": [ [ 681, 695 ] ], "normalized": [] } ]

[]

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[ { "id": "IEPA.d197.s478.i0", "type": "PPI", "arg1_id": "IEPA.d197.s478.e0", "arg2_id": "IEPA.d197.s478.e1", "normalized": [] }, { "id": "IEPA.d197.s479.i0", "type": "PPI", "arg1_id": "IEPA.d197.s479.e0", "arg2_id": "IEPA.d197.s479.e1", "normalized": [] }, { "id": "IEPA.d197.s481.i0", "type": "PPI", "arg1_id": "IEPA.d197.s481.e0", "arg2_id": "IEPA.d197.s481.e1", "normalized": [] }, { "id": "IEPA.d197.s482.i0", "type": "PPI", "arg1_id": "IEPA.d197.s482.e0", "arg2_id": "IEPA.d197.s482.e1", "normalized": [] } ]

[ { "id": "IEPA.d198.s483", "type": "", "text": [ "Arcuate nucleus NPY mRNA increased in rats given protein-free diet, correlating with leptin rather than decreased feeding" ], "offsets": [ [ 0, 121 ] ] } ]

[ { "id": "IEPA.d198.s483.e0", "type": "", "text": [ "NPY" ], "offsets": [ [ 16, 19 ] ], "normalized": [] }, { "id": "IEPA.d198.s483.e1", "type": "", "text": [ "leptin" ], "offsets": [ [ 85, 91 ] ], "normalized": [] } ]

[]

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[ { "id": "IEPA.d198.s483.i0", "type": "PPI", "arg1_id": "IEPA.d198.s483.e0", "arg2_id": "IEPA.d198.s483.e1", "normalized": [] } ]

[ { "id": "IEPA.d199.s484", "type": "", "text": [ "The induction of alpha-amylase triggered by gibberellic acid in barley embryos is repressed by sugars" ], "offsets": [ [ 0, 101 ] ] }, { "id": "IEPA.d199.s485", "type": "", "text": [ "Our results indicate that glucose represses gibberellin signalling late along this hormone transduction pathway, downstream of transcription of the gibberellin-modulated transcriptional activator (GAMYB) needed for alpha-amylase induction" ], "offsets": [ [ 102, 340 ] ] } ]

[ { "id": "IEPA.d199.s484.e0", "type": "", "text": [ "alpha-amylase" ], "offsets": [ [ 17, 30 ] ], "normalized": [] }, { "id": "IEPA.d199.s484.e1", "type": "", "text": [ "gibberellic acid" ], "offsets": [ [ 44, 60 ] ], "normalized": [] }, { "id": "IEPA.d199.s485.e0", "type": "", "text": [ "gibberellin" ], "offsets": [ [ 146, 157 ] ], "normalized": [] }, { "id": "IEPA.d199.s485.e1", "type": "", "text": [ "gibberellin" ], "offsets": [ [ 250, 261 ] ], "normalized": [] }, { "id": "IEPA.d199.s485.e2", "type": "", "text": [ "alpha-amylase" ], "offsets": [ [ 317, 330 ] ], "normalized": [] } ]

[]

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[ { "id": "IEPA.d199.s484.i0", "type": "PPI", "arg1_id": "IEPA.d199.s484.e0", "arg2_id": "IEPA.d199.s484.e1", "normalized": [] } ]