Gastrin-releasing peptide, also known as GRP, is a neuropeptide, a regulatory molecule that has been implicated in a number of physiological and pathophysiological processes. Most notably, GRP stimulates the release of gastrin from the G cells of the stomach.
The gene from which GRP is derived encodes a number of bombesin-like peptides.[5][6][7][8] Its 148-amino acidpreproprotein, following cleavage of a signal peptide, is further processed to produce either the 27-amino acid gastrin-releasing peptide or the 10-amino acid neuromedin C.[9] These smaller peptides regulate numerous functions of the gastrointestinal and central nervous systems, including release of gastrointestinal hormones, smooth muscle cell contraction, and epithelial cell proliferation.[5]
Gastrin-releasing peptide is a regulatory human peptide that elicits gastrin release and regulates gastric acid secretion and enteric motor function.[10] The post-ganglionic fibers of the vagus nerve that innervate bombesin/GRP neurons of the stomach release GRP, which stimulates the G cells to release gastrin.
Furthermore, GRP seems to mediate certain aspects of stress. This is the reason for the observed fact that atropine does not block the vagal effect on gastrin release.
GeneEdit
The human GRP gene is located on chromosome 18q21. PreproGRP (the unprocessed form of GRP) is encoded in three exons separated by two introns.[8]Alternative splicing results in multiple transcript variants encoding different isoforms.[5]
SynthesisEdit
PreproGRP begins with signal peptidase cleavage to generate the proGRP, which is then processed by proteolytic cleavages, to form smaller GRP peptides.[10]
These smaller peptides are released by the post-ganglionic fibers of the vagus nerve, which innervate the G cells of the stomach and stimulate them to release gastrin. GRP regulates numerous functions of the gastrointestinal and central nervous systems, including release of gastrointestinal hormones, smooth muscle cell contraction, and epithelial cell proliferation.[10]
Clinical significanceEdit
Gastrin-releasing peptide and neuromedin C, it is postulated, play a role in human cancers of the lung, colon, stomach, pancreas, breast, and prostate.[5]
^ abcMerali Z, McIntosh J, Anisman H (October 1999). "Role of bombesin-related peptides in the control of food intake". Neuropeptides. 33 (5): 376–86. doi:10.1054/npep.1999.0054. PMID 10657515. S2CID 22270584.
Further readingEdit
Merali Z, McIntosh J, Anisman H (2000). "Role of bombesin-related peptides in the control of food intake". Neuropeptides. 33 (5): 376–86. doi:10.1054/npep.1999.0054. PMID 10657515. S2CID 22270584.
Baraniuk JN, Lundgren JD, Shelhamer JH, Kaliner MA (1992). "Gastrin releasing peptide (GRP) binding sites in human bronchi". Neuropeptides. 21 (2): 81–4. doi:10.1016/0143-4179(92)90518-2. PMID 1557184. S2CID 40083693.
Spindel ER, Zilberberg MD, Habener JF, Chin WW (1986). "Two prohormones for gastrin-releasing peptide are encoded by two mRNAs differing by 19 nucleotides". Proc. Natl. Acad. Sci. U.S.A. 83 (1): 19–23. Bibcode:1986PNAS...83...19S. doi:10.1073/pnas.83.1.19. PMC322782. PMID 3001723.
Sausville EA, Lebacq-Verheyden AM, Spindel ER, et al. (1986). "Expression of the gastrin-releasing peptide gene in human small cell lung cancer. Evidence for alternative processing resulting in three distinct mRNAs". J. Biol. Chem. 261 (5): 2451–7. doi:10.1016/S0021-9258(17)35956-2. PMID 3003116.
Lebacq-Verheyden AM, Bertness V, Kirsch I, et al. (1987). "Human gastrin-releasing peptide gene maps to chromosome band 18q21". Somat. Cell Mol. Genet. 13 (1): 81–6. doi:10.1007/BF02422302. PMID 3027901. S2CID 28347998.
Naylor SL, Sakaguchi AY, Spindel E, Chin WW (1987). "Human gastrin-releasing peptide gene is located on chromosome 18". Somat. Cell Mol. Genet. 13 (1): 87–91. doi:10.1007/BF02422303. PMID 3027902. S2CID 7514856.
Lebacq-Verheyden AM, Kasprzyk PG, Raum MG, et al. (1989). "Posttranslational processing of endogenous and of baculovirus-expressed human gastrin-releasing peptide precursor". Mol. Cell. Biol. 8 (8): 3129–35. doi:10.1128/MCB.8.8.3129. PMC363540. PMID 3211139.
Spindel ER, Chin WW, Price J, et al. (1984). "Cloning and characterization of cDNAs encoding human gastrin-releasing peptide". Proc. Natl. Acad. Sci. U.S.A. 81 (18): 5699–703. Bibcode:1984PNAS...81.5699S. doi:10.1073/pnas.81.18.5699. PMC391778. PMID 6207529.
Benya RV, Kusui T, Pradhan TK, et al. (1995). "Expression and characterization of cloned human bombesin receptors". Mol. Pharmacol. 47 (1): 10–20. PMID 7838118.
Moody TW, Zia F, Venugopal R, et al. (1994). "Corticotropin-releasing factor stimulates cyclic AMP, arachidonic acid release, and growth of lung cancer cells". Peptides. 15 (2): 281–5. doi:10.1016/0196-9781(94)90013-2. PMID 8008632. S2CID 44503352.
Frankel A, Tsao MS, Viallet J (1994). "Receptor subtype expression and responsiveness to bombesin in cultured human bronchial epithelial cells". Cancer Res. 54 (7): 1613–6. PMID 8137267.
Lü F, Jin T, Drucker DJ (1996). "Proglucagon gene expression is induced by gastrin-releasing peptide in a mouse enteroendocrine cell line". Endocrinology. 137 (9): 3710–6. doi:10.1210/en.137.9.3710. PMID 8756537.
Bertenshaw GP, Turk BE, Hubbard SJ, et al. (2001). "Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity". J. Biol. Chem. 276 (16): 13248–55. doi:10.1074/jbc.M011414200. PMID 11278902.
Lambeir AM, Durinx C, Proost P, et al. (2001). "Kinetic study of the processing by dipeptidyl-peptidase IV/CD26 of neuropeptides involved in pancreatic insulin secretion". FEBS Lett. 507 (3): 327–30. doi:10.1016/S0014-5793(01)02982-9. hdl:10067/366910151162165141. PMID 11696365. S2CID 26891876.
Mason S, Smart D, Marshall IC, et al. (2002). "Identification and characterisation of functional bombesin receptors in human astrocytes". Eur. J. Pharmacol. 438 (1–2): 25–34. doi:10.1016/S0014-2999(02)01268-2. PMID 11906707.
Carroll RE, Matkowskyj K, Saunthararajah Y, et al. (2002). "Contribution of gastrin-releasing peptide and its receptor to villus development in the murine and human gastrointestinal tract". Mech. Dev. 113 (2): 121–30. doi:10.1016/S0925-4773(02)00032-1. PMID 11960700. S2CID 15515339.
Uchida K, Kojima A, Morokawa N, et al. (2003). "Expression of progastrin-releasing peptide and gastrin-releasing peptide receptor mRNA transcripts in tumor cells of patients with small cell lung cancer". J. Cancer Res. Clin. Oncol. 128 (12): 633–40. doi:10.1007/s00432-002-0392-8. PMID 12474049. S2CID 23764903.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC139241. PMID 12477932.
Schneider J, Philipp M, Velcovsky HG, et al. (2003). "Pro-gastrin-releasing peptide (ProGRP), neuron specific enolase (NSE), carcinoembryonic antigen (CEA) and cytokeratin 19-fragments (CYFRA 21-1) in patients with lung cancer in comparison to other lung diseases". Anticancer Res. 23 (2A): 885–93. PMID 12820318.
External linksEdit
Gastrin-Releasing+Peptide at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Nosek, Thomas M. . Essentials of Human Physiology. Archived from the original on 2016-03-24.
October 19, 2023
gastrin, releasing, peptide, also, known, neuropeptide, regulatory, molecule, that, been, implicated, number, physiological, pathophysiological, processes, most, notably, stimulates, release, gastrin, from, cells, stomach, grpavailable, structurespdbortholog, . Gastrin releasing peptide also known as GRP is a neuropeptide a regulatory molecule that has been implicated in a number of physiological and pathophysiological processes Most notably GRP stimulates the release of gastrin from the G cells of the stomach GRPAvailable structuresPDBOrtholog search PDBe RCSBList of PDB id codes2N0B 2N0C 2N0D 2N0E 2N0F 2N0G 2N0HIdentifiersAliasesGRP BN GRP 10 preproprogastrin releasing peptideExternal IDsOMIM 137260 MGI 95833 HomoloGene 1580 GeneCards GRPGene location Human Chr Chromosome 18 human 1 Band18q21 32Start59 220 158 bp 1 End59 230 774 bp 1 Gene location Mouse Chr Chromosome 18 mouse 2 Band18 E1 18 38 98 cMStart66 005 891 bp 2 End66 019 667 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inhair folliclegastric mucosaspermlactiferous ductcingulate gyrustibiahippocampus properprefrontal cortexamygdalabronchial epithelial cellTop expressed insubiculumsuprachiasmatic nucleusbarrel cortexventral tegmental areahippocampus properexternal carotid arterydorsomedial hypothalamic nucleusinternal carotid arteryamygdalaRegion I of hippocampus properMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionsignaling receptor binding neuropeptide hormone activityCellular componentextracellular region extracellular space secretory granule lumen cytoplasmic vesicleBiological processneuropeptide signaling pathway signal transduction social behavior psychomotor behavior response to external biotic stimulus positive regulation of peptide hormone secretion positive regulation of phospholipase C activating G protein coupled receptor signaling pathway regulation of signaling receptor activity G protein coupled receptor signaling pathwaySources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez2922225642EnsemblENSG00000134443ENSMUSG00000024517UniProtP07492Q8R1I2RefSeq mRNA NM 001012512NM 001012513NM 002091NM 175012RefSeq protein NP 002082NP 001012531NP 001012530NP 778177Location UCSC Chr 18 59 22 59 23 MbChr 18 66 01 66 02 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseThe gene from which GRP is derived encodes a number of bombesin like peptides 5 6 7 8 Its 148 amino acid preproprotein following cleavage of a signal peptide is further processed to produce either the 27 amino acid gastrin releasing peptide or the 10 amino acid neuromedin C 9 These smaller peptides regulate numerous functions of the gastrointestinal and central nervous systems including release of gastrointestinal hormones smooth muscle cell contraction and epithelial cell proliferation 5 Contents 1 Function 2 Gene 3 Synthesis 4 Clinical significance 5 See also 6 References 7 Further reading 8 External linksFunction EditGastrin releasing peptide is a regulatory human peptide that elicits gastrin release and regulates gastric acid secretion and enteric motor function 10 The post ganglionic fibers of the vagus nerve that innervate bombesin GRP neurons of the stomach release GRP which stimulates the G cells to release gastrin GRP is also involved in the biology of the circadian system playing a role in the signaling of light to the master circadian oscillator in the suprachiasmatic nuclei of the hypothalamus Furthermore GRP seems to mediate certain aspects of stress This is the reason for the observed fact that atropine does not block the vagal effect on gastrin release Gene EditThe human GRP gene is located on chromosome 18q21 PreproGRP the unprocessed form of GRP is encoded in three exons separated by two introns 8 Alternative splicing results in multiple transcript variants encoding different isoforms 5 Synthesis EditPreproGRP begins with signal peptidase cleavage to generate the proGRP which is then processed by proteolytic cleavages to form smaller GRP peptides 10 These smaller peptides are released by the post ganglionic fibers of the vagus nerve which innervate the G cells of the stomach and stimulate them to release gastrin GRP regulates numerous functions of the gastrointestinal and central nervous systems including release of gastrointestinal hormones smooth muscle cell contraction and epithelial cell proliferation 10 Clinical significance EditGastrin releasing peptide and neuromedin C it is postulated play a role in human cancers of the lung colon stomach pancreas breast and prostate 5 See also EditPro Gastrin Releasing Peptide BombesinReferences Edit a b c GRCh38 Ensembl release 89 ENSG00000134443 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000024517 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine a b c d Entrez Gene GRP gastrin releasing peptide Spindel ER Chin WW Price J Rees LH Besser GM Habener JF September 1984 Cloning and characterization of cDNAs encoding human gastrin releasing peptide Proc Natl Acad Sci U S A 81 18 5699 703 Bibcode 1984PNAS 81 5699S doi 10 1073 pnas 81 18 5699 PMC 391778 PMID 6207529 Spindel ER Zilberberg MD Habener JF Chin WW January 1986 Two prohormones for gastrin releasing peptide are encoded by two mRNAs differing by 19 nucleotides Proc Natl Acad Sci U S A 83 1 19 23 Bibcode 1986PNAS 83 19S doi 10 1073 pnas 83 1 19 PMC 322782 PMID 3001723 a b Lebacq Verheyden AM Bertness V Kirsch I Hollis GF McBride OW Battey J January 1987 Human gastrin releasing peptide gene maps to chromosome band 18q21 Somat Cell Mol Genet 13 1 81 6 doi 10 1007 BF02422302 PMID 3027901 S2CID 28347998 Neuromedin C pubchem ncbi nlm nih gov a b c Merali Z McIntosh J Anisman H October 1999 Role of bombesin related peptides in the control of food intake Neuropeptides 33 5 376 86 doi 10 1054 npep 1999 0054 PMID 10657515 S2CID 22270584 Further reading EditMerali Z McIntosh J Anisman H 2000 Role of bombesin related peptides in the control of food intake Neuropeptides 33 5 376 86 doi 10 1054 npep 1999 0054 PMID 10657515 S2CID 22270584 Baraniuk JN Lundgren JD Shelhamer JH Kaliner MA 1992 Gastrin releasing peptide GRP binding sites in human bronchi Neuropeptides 21 2 81 4 doi 10 1016 0143 4179 92 90518 2 PMID 1557184 S2CID 40083693 Spindel ER Zilberberg MD Habener JF Chin WW 1986 Two prohormones for gastrin releasing peptide are encoded by two mRNAs differing by 19 nucleotides Proc Natl Acad Sci U S A 83 1 19 23 Bibcode 1986PNAS 83 19S doi 10 1073 pnas 83 1 19 PMC 322782 PMID 3001723 Sausville EA Lebacq Verheyden AM Spindel ER et al 1986 Expression of the gastrin releasing peptide gene in human small cell lung cancer Evidence for alternative processing resulting in three distinct mRNAs J Biol Chem 261 5 2451 7 doi 10 1016 S0021 9258 17 35956 2 PMID 3003116 Lebacq Verheyden AM Bertness V Kirsch I et al 1987 Human gastrin releasing peptide gene maps to chromosome band 18q21 Somat Cell Mol Genet 13 1 81 6 doi 10 1007 BF02422302 PMID 3027901 S2CID 28347998 Naylor SL Sakaguchi AY Spindel E Chin WW 1987 Human gastrin releasing peptide gene is located on chromosome 18 Somat Cell Mol Genet 13 1 87 91 doi 10 1007 BF02422303 PMID 3027902 S2CID 7514856 Lebacq Verheyden AM Kasprzyk PG Raum MG et al 1989 Posttranslational processing of endogenous and of baculovirus expressed human gastrin releasing peptide precursor Mol Cell Biol 8 8 3129 35 doi 10 1128 MCB 8 8 3129 PMC 363540 PMID 3211139 Spindel ER Chin WW Price J et al 1984 Cloning and characterization of cDNAs encoding human gastrin releasing peptide Proc Natl Acad Sci U S A 81 18 5699 703 Bibcode 1984PNAS 81 5699S doi 10 1073 pnas 81 18 5699 PMC 391778 PMID 6207529 Benya RV Kusui T Pradhan TK et al 1995 Expression and characterization of cloned human bombesin receptors Mol Pharmacol 47 1 10 20 PMID 7838118 Moody TW Zia F Venugopal R et al 1994 Corticotropin releasing factor stimulates cyclic AMP arachidonic acid release and growth of lung cancer cells Peptides 15 2 281 5 doi 10 1016 0196 9781 94 90013 2 PMID 8008632 S2CID 44503352 Frankel A Tsao MS Viallet J 1994 Receptor subtype expression and responsiveness to bombesin in cultured human bronchial epithelial cells Cancer Res 54 7 1613 6 PMID 8137267 Lu F Jin T Drucker DJ 1996 Proglucagon gene expression is induced by gastrin releasing peptide in a mouse enteroendocrine cell line Endocrinology 137 9 3710 6 doi 10 1210 en 137 9 3710 PMID 8756537 Bertenshaw GP Turk BE Hubbard SJ et al 2001 Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity J Biol Chem 276 16 13248 55 doi 10 1074 jbc M011414200 PMID 11278902 Lambeir AM Durinx C Proost P et al 2001 Kinetic study of the processing by dipeptidyl peptidase IV CD26 of neuropeptides involved in pancreatic insulin secretion FEBS Lett 507 3 327 30 doi 10 1016 S0014 5793 01 02982 9 hdl 10067 366910151162165141 PMID 11696365 S2CID 26891876 Mason S Smart D Marshall IC et al 2002 Identification and characterisation of functional bombesin receptors in human astrocytes Eur J Pharmacol 438 1 2 25 34 doi 10 1016 S0014 2999 02 01268 2 PMID 11906707 Carroll RE Matkowskyj K Saunthararajah Y et al 2002 Contribution of gastrin releasing peptide and its receptor to villus development in the murine and human gastrointestinal tract Mech Dev 113 2 121 30 doi 10 1016 S0925 4773 02 00032 1 PMID 11960700 S2CID 15515339 Uchida K Kojima A Morokawa N et al 2003 Expression of progastrin releasing peptide and gastrin releasing peptide receptor mRNA transcripts in tumor cells of patients with small cell lung cancer J Cancer Res Clin Oncol 128 12 633 40 doi 10 1007 s00432 002 0392 8 PMID 12474049 S2CID 23764903 Strausberg RL Feingold EA Grouse LH et al 2003 Generation and initial analysis of more than 15 000 full length human and mouse cDNA sequences Proc Natl Acad Sci U S A 99 26 16899 903 Bibcode 2002PNAS 9916899M doi 10 1073 pnas 242603899 PMC 139241 PMID 12477932 Schneider J Philipp M Velcovsky HG et al 2003 Pro gastrin releasing peptide ProGRP neuron specific enolase NSE carcinoembryonic antigen CEA and cytokeratin 19 fragments CYFRA 21 1 in patients with lung cancer in comparison to other lung diseases Anticancer Res 23 2A 885 93 PMID 12820318 External links EditGastrin Releasing Peptide at the U S National Library of Medicine Medical Subject Headings MeSH Nosek Thomas M Section 6 6ch2 s6ch2 35 Essentials of Human Physiology Archived from the original on 2016 03 24 Retrieved from https en wikipedia org w index php title Gastrin releasing peptide amp oldid 1114113900, wikipedia, wiki, book, books, library,
