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Obestatin

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the recombinant proghrelin precursor by cleavage at the single basic residue required for generation of the obestatin sequence. Thus the physiological generation of this particular peptide sequence remains unproven. Obestatin has opposite action to ghrelin on food intake and plays a role in energy balance. Circuit-resistance exercise resulted in a significant change in GH levels, but had no effect on plasma Obestatin levels.
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Obestatin opposes the actions of ghrelin which are growth hormone secretion and increased appetite. The purpose of producing two hormones with opposing effects is not clear: removing the ghrelin gene from mice did not significantly reduce food intake. No secretory convertase is capable of cleaving
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The obestatin structure to the right was determined by NMR. The length of the polypeptide was found to be 24 residues with a secondary structure 29% helical. Specifically 2 helices and 7 residues are formed.
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Zhang N, Yuan C, Li Z, Li J, Li X, Li C, Li R, Wang SR (January 2011). "Meta-analysis of the relationship between obestatin and ghrelin levels and the ghrelin/obestatin ratio with respect to obesity".
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Qi X, Li L, Yang G, Liu J, Li K, Tang Y, Liou H, Boden G (April 2007). "Circulating obestatin levels in normal subjects and in patients with impaired glucose regulation and type 2 diabetes mellitus".
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Zhang JV, Ren PG, Avsian-Kretchmer O, Luo CW, Rauch R, Klein C, Hsueh AJ (November 2005). "Obestatin, a peptide encoded by the ghrelin gene, opposes ghrelin's effects on food intake".
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Scrima M, Campiglia P, Esposito C, Gomez-Monterrey I, Novellino E, D'Ursi AM (November 2007). "Obestatin conformational features: a strategy to unveil obestatin's biological role?".
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Seim I, Amorim L, Walpole C, Carter S, Chopin LK, Herington AC (2010). "Ghrelin gene-related peptides: multifunctional endocrine / autocrine modulators in health and disease".
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is a hormone that is produced in specialized epithelial cells of the stomach and small intestine of several animals including humans. Obestatin was originally identified as an
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Harsch IA, Koebnick C, Tasi AM, Hahn EG, Konturek PC (October 2009). "Ghrelin and obestatin levels in type 2 diabetic patients with and without delayed gastric emptying".
860:"Altered distribution of adiponectin isoforms in children with Prader-Willi syndrome (PWS): association with insulin sensitivity and circulating satiety peptide hormones" 36: 292:
Studies on the obestatin/ghrelin ratio in the gastrointestinal tract and plasma are associated with some diseases such as irritable bowel syndrome (IBS), obesity,
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Ghanbari-Niaki A, Saghebjoo M, Rahbarizadeh F (2008). "single circuit-resistance exercise has no effect on plasma obestatin levels in female college students".
71: 1066: 430:"The ghrelin/obestatin balance in the physiological and pathological control of growth hormone secretion, body composition and food intake" 95: 83: 76: 772:
Sjölund K, Ekman R, Wierup N (June 2010). "Covariation of plasma ghrelin and motilin in irritable bowel syndrome".
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Dong XY, He JM, Tang SQ, Li HY, Jiang QY, Zou XT (February 2009). "Is GPR39 the natural receptor of obestatin?".
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gene has four exons. Five products of similar structure and function arise: the first is the 117-amino acid
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Haqq AM, Muehlbauer M, Svetkey LP, Newgard CB, Purnell JQ, Grambow SC, Freemark MS (December 2007).
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functioned as an obestatin receptor, however more recent findings suggest that this is unlikely.
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As yet no biochemical studies of circulating obestatin have been carried out.
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approach: by computer search of the sequenced genomes of several organisms.
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peptide, but its effect on food intake remains controversial.
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Zizzari P, Longchamps R, Epelbaum J, Bluet-Pajot MT (2007).
235:. (It is homologous to promotilin; both are members of the 633:"Production of bioactive peptides in an in vitro system" 223:Obestatin is encoded by the same gene that encodes 171: 161: 156: 135: 130: 118: 106: 94: 82: 70: 60: 55: 21: 1033:Obestatin, A New Physiological Opponent of Ghrelin 998:Holst B, Egerod KL, Schild E, et al. (2007). 523: 378:Gourcerol G, St-Pierre DH, TachĂ© Y (June 2007). 227:, a peptide hormone. The mRNA produced from the 423: 421: 328: 326: 243:which is cleaved to produce a 28-amino acid 8: 525:"In Study, Hormone Reduced Appetite in Mice" 428:Hassouna R, Zizzari P, Tolle V (July 2010). 255:is presumed to be cleaved from C-ghrelin. 153: 29: 1049:at the U.S. National Library of Medicine 1015: 883: 705: 656: 631:Ozawa A, Cai Y, Lindberg I (April 2007). 445: 322: 16:Hormone that is produced in the stomach 18: 7: 522:Denise Grady (November 11, 2005). 239:family). It is cleaved to produce 14: 296:, and type II diabetes mellitus. 202:Obestatin was discovered using a 921:10.1111/j.1365-2265.2007.02776.x 876:10.1111/j.1365-2265.2007.02991.x 559:10.1111/j.1440-1681.2009.05241.x 447:10.1111/j.1365-2826.2010.02019.x 263:It was originally proposed that 1035:, PHOENIX PHARMACEUTICALS, INC. 23:ghrelin/obestatin preprohormone 786:10.1016/j.peptides.2010.03.021 743:10.1016/j.peptides.2007.11.002 602:10.1016/j.peptides.2008.09.022 1: 345:Biochem. Biophys. Res. Commun 829:10.1097/MAJ.0b013e3181ec41ed 396:10.1016/j.regpep.2006.12.023 1067:Genes on human chromosome 3 1093: 547:Clin Exp Pharmacol Physiol 357:10.1016/j.bbrc.2007.08.200 964:10.1007/s10620-008-0622-2 152: 28: 1051:Medical Subject Headings 649:10.1016/j.ab.2007.04.020 499:10.1126/science.1117255 219:Gene and transcription 294:Prader–Willi syndrome 288:Clinical significance 1017:10.1210/en.2006-0933 698:10.1210/en.2006-1231 491:2005Sci...310..996Z 530:The New York Times 434:J. Neuroendocrinol 247:(unacylated) and 185: 184: 181: 180: 1084: 1072:Peptide hormones 1047:obestatin, human 1029: 1019: 984: 983: 947: 941: 940: 909:Clin. Endocrinol 904: 898: 897: 887: 864:Clin. Endocrinol 855: 849: 848: 812: 806: 805: 769: 763: 762: 726: 720: 719: 709: 677: 671: 670: 660: 628: 622: 621: 585: 579: 578: 542: 536: 533: 527: 518: 474: 468: 467: 449: 425: 416: 415: 375: 369: 368: 340: 330: 154: 33: 19: 1092: 1091: 1087: 1086: 1085: 1083: 1082: 1081: 1057: 1056: 1043: 1038: 997: 993: 991:Further reading 988: 987: 949: 948: 944: 906: 905: 901: 857: 856: 852: 817:Am. J. Med. Sci 814: 813: 809: 771: 770: 766: 728: 727: 723: 679: 678: 674: 630: 629: 625: 587: 586: 582: 544: 543: 539: 521: 485:(5750): 996–9. 476: 475: 471: 427: 426: 419: 377: 376: 372: 342: 332: 331: 324: 319: 302: 290: 281: 273: 261: 221: 212: 200: 51: 17: 12: 11: 5: 1090: 1088: 1080: 1079: 1074: 1069: 1059: 1058: 1055: 1054: 1042: 1041:External links 1039: 1037: 1036: 1030: 994: 992: 989: 986: 985: 958:(10): 2161–6. 942: 899: 850: 807: 780:(6): 1109–12. 764: 737:(3): 487–490. 721: 692:(4): 1648–53. 672: 623: 580: 537: 535: 534: 469: 440:(7): 793–804. 417: 370: 321: 320: 318: 315: 314: 313: 308: 301: 298: 289: 286: 280: 277: 272: 269: 260: 257: 220: 217: 211: 208: 204:bioinformatics 199: 196: 183: 182: 179: 178: 173: 169: 168: 163: 159: 158: 150: 149: 139: 133: 132: 128: 127: 122: 116: 115: 110: 104: 103: 98: 92: 91: 86: 80: 79: 74: 68: 67: 62: 58: 57: 53: 52: 34: 26: 25: 15: 13: 10: 9: 6: 4: 3: 2: 1089: 1078: 1075: 1073: 1070: 1068: 1065: 1064: 1062: 1052: 1048: 1045: 1044: 1040: 1034: 1031: 1027: 1023: 1018: 1013: 1009: 1005: 1004:Endocrinology 1001: 996: 995: 990: 981: 977: 973: 969: 965: 961: 957: 953: 952:Dig. Dis. 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Pept 166:Swiss-model 56:Identifiers 1061:Categories 317:References 311:Nesfatin-1 241:proghrelin 162:Structures 157:Search for 131:Other data 35:Obestatin 341:​; 253:Obestatin 249:C-ghrelin 210:Structure 198:Discovery 192:anorectic 188:Obestatin 113:NM_016362 72:NCBI gene 50:solution. 1026:16959833 980:27182413 972:19082715 937:24834549 929:17371480 894:17666087 845:11960114 837:21139496 802:11646192 794:20338210 774:Peptides 759:20008762 751:18308154 731:Peptides 716:17204551 667:17540328 618:34448850 610:18977259 590:Peptides 575:21657818 567:19566830 515:22391046 507:16284174 464:43518257 456:20456603 412:45148053 404:17321609 365:17904104 300:See also 279:Function 259:Receptor 176:InterPro 48:micellar 1077:Obesity 885:2605973 707:1890395 658:2128726 487:Bibcode 479:Science 306:Ghrelin 245:ghrelin 237:motilin 225:ghrelin 172:Domains 146:p26-p25 120:UniProt 1053:(MeSH) 1024:  978:  970:  935:  927:  892:  882:  843:  835:  800:  792:  757:  749:  714:  704:  665:  655:  616:  608:  573:  565:  513:  505:  462:  454:  410:  402:  363:  142:Chr. 3 125:Q9UBU3 108:RefSeq 101:605353 61:Symbol 976:S2CID 933:S2CID 841:S2CID 798:S2CID 755:S2CID 614:S2CID 571:S2CID 511:S2CID 460:S2CID 408:S2CID 265:GPR39 137:Locus 89:18129 77:51738 1022:PMID 968:PMID 925:PMID 890:PMID 833:PMID 790:PMID 747:PMID 712:PMID 663:PMID 606:PMID 563:PMID 503:PMID 452:PMID 400:PMID 361:PMID 338:2JSH 229:GHRL 96:OMIM 84:HGNC 65:GHRL 1012:doi 1008:148 960:doi 917:doi 880:PMC 872:doi 825:doi 821:341 782:doi 739:doi 702:PMC 694:doi 690:148 653:PMC 645:doi 641:366 598:doi 555:doi 495:doi 483:310 442:doi 392:doi 388:141 353:doi 349:363 334:PDB 45:DPC 41:SDS 39:in 1063:: 1020:. 1006:. 1002:. 974:. 966:. 956:54 954:. 931:. 923:. 913:66 911:. 888:. 878:. 868:67 866:. 862:. 839:. 831:. 819:. 796:. 788:. 778:31 776:. 753:. 745:. 735:29 733:. 710:. 700:. 688:. 684:. 661:. 651:. 639:. 635:. 612:. 604:. 594:30 592:. 569:. 561:. 551:37 549:. 528:. 509:. 501:. 493:. 481:. 458:. 450:. 438:22 436:. 432:. 420:^ 406:. 398:. 386:. 382:. 359:. 347:. 336:: 325:^ 43:/ 1028:. 1014:: 982:. 962:: 939:. 919:: 896:. 874:: 847:. 827:: 804:. 784:: 761:. 741:: 718:. 696:: 669:. 647:: 620:. 600:: 577:. 557:: 532:. 517:. 497:: 489:: 466:. 444:: 414:. 394:: 367:. 355::

Index

ghrelin/obestatin preprohormone

NMR structure
SDS
DPC
micellar
GHRL
NCBI gene
51738
HGNC
18129
OMIM
605353
RefSeq
NM_016362
UniProt
Q9UBU3
Locus
Chr. 3
p26-p25
Swiss-model
InterPro
anorectic
bioinformatics
ghrelin
motilin
GPR39
Prader–Willi syndrome
Ghrelin
Nesfatin-1

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