gastrin-releasing peptide

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GRP

WordNet

1. polypeptide hormone secreted by the mucous lining of the stomach; when peptides and amino acids are present in the small intestine the secretion of gastric acid is stimulated
2. amide combining the amino group of one amino acid with the carboxyl group of another; usually obtained by partial hydrolysis of protein

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/01/11 10:21:10」(JST)

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Gastrin-releasing peptide
Identifiers
Symbols	GRP ; BN; GRP-10; preproGRP; proGRP
External IDs	OMIM: 137260 MGI: 95833 HomoloGene: 1580 GeneCards: GRP Gene
Gene ontology Molecular function • receptor binding • neuropeptide hormone activity Cellular component • extracellular region • extracellular space Biological process • signal transduction • neuropeptide signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2922	225642
Ensembl	ENSG00000134443	ENSMUSG00000024517
UniProt	P07492	Q8R1I2
RefSeq (mRNA)	NM_001012512	NM_175012
RefSeq (protein)	NP_001012530	NP_778177
Location (UCSC)	Chr 18: 59.22 – 59.23 Mb	Chr 18: 65.87 – 65.89 Mb
PubMed search	[1]	[2]

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. 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. 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.

Function

Gastrin-releasing peptide is a regulatory human peptide that elicits gastrin release and regulates gastric acid secretion and enteric motor function. The post-ganglionic fibers of the vagus nerve that innervate the G cells 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

The human GRP gene is located on chromosome 18. PreproGRP (the unprocessed form of GRP) is encoded in three exons separated by two introns. Alternative splicing results in multiple transcript variants encoding different isoforms.

Synthesis

PreproGRP begins with signal peptidase cleavage to generate the proGRP, which is then processed (by proteolytic cleavages), to form smaller GRP peptides.

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.

Clinical significance

Gastrin-releasing peptide and neuromedin C, it is postulated, play a role in human cancers of the lung, colon, stomach, pancreas, breast, and prostate.

References

Further reading

• 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. 
• 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. 
• 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. 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. 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. 
• 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. 
• 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. 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. 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. 
• 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. PMID 11696365. 
• 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. 
• 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. 
• 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. 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

• Gastrin-Releasing Peptide at the US National Library of Medicine Medical Subject Headings (MeSH)
• Physiology: 6/6ch2/s6ch2_35 - Essentials of Human Physiology

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

• 1. 胃酸分泌の生理学 physiology of gastric acid secretion
• 2. ヘリコバクターピロリ感染と十二指腸潰瘍の関連性 association between helicobacter pylori infection and duodenal ulcer
• 3. 気管支神経内分泌（カルチノイド）腫瘍：疫学、危険因子、分類、組織学的検査、診断、および病期分類 bronchial neuroendocrine carcinoid tumors epidemiology risk factors classification histology diagnosis and staging
• 4. 小細胞肺癌の病理および病期分類 pathobiology and staging of small cell carcinoma of the lung
• 5. ユーイング肉腫ファミリーの腫瘍の疫学、病理、および分子遺伝学 epidemiology pathology and molecular genetics of the ewing sarcoma family of tumors

English Journal

• New radiopharmaceutical agents for the treatment of castration-resistant prostate cancer.

• Maffioli L1, Florimonte L, Costa DC, Correia Castanheira J, Grana C, Luster M, Bodei L, Chinol M.
• The quarterly journal of nuclear medicine and molecular imaging : official publication of the Italian Association of Nuclear Medicine (AIMN) [and] the International Association of Radiopharmacology (IAR), [and] Section of the Society of Radiopharmaceutical Chemistry and Biology.Q J Nucl Med Mol Imaging.2015 Dec;59(4):420-38. Epub 2015 Jul 29.
• Prostate cancer (PCa) is the fourth most common cancer worldwide in terms of incidence and third among male, but is becoming the most common cancer in developed countries. In many patients the disease will progress despite of castration levels of testosterone, to become castration-resistant PCa (CRP
• PMID 26222274

• GRPR-targeted Protein Contrast Agents for Molecular Imaging of Receptor Expression in Cancers by MRI.

• Pu F1, Qiao J1, Xue S1, Yang H2, Patel A1, Wei L1, Hekmatyar K3, Salarian M1, Grossniklaus HE2, Liu ZR1, Yang JJ1.
• Scientific reports.Sci Rep.2015 Nov 18;5:16214. doi: 10.1038/srep16214.
• Gastrin-releasing peptide receptor (GRPR) is differentially expressed on the surfaces of various diseased cells, including prostate and lung cancer. However, monitoring temporal and spatial expression of GRPR in vivo by clinical MRI is severely hampered by the lack of contrast agents with high relax
• PMID 26577829

• Effects of central gastrin-releasing peptide on glucose metabolism.

• Jha PK1, Foppen E2, Challet E3, Kalsbeek A4.
• Brain research.Brain Res.2015 Nov 2;1625:135-41. doi: 10.1016/j.brainres.2015.08.040. Epub 2015 Sep 8.
• Gastrin-releasing peptide (GRP) mediated signals in the central nervous system (CNS) influence many functions associated with energy metabolism. The purpose of the present study was to investigate the central effect of GRP on glucose metabolism in the male rat. Intracerebroventricular (icv) administ
• PMID 26358150

Japanese Journal

• 前立腺小細胞癌の1例 : 本邦報告例を用いた予後解析

• 守山 洋司,藤広 茂,仲野 正博,江原 英俊,明石 高明,出口 隆
• 泌尿器科紀要 = Acta urologica Japonica 60(12), 645-650, 2014-12
• … The urologic and radiologic outcomes including the serum levels of neuron-specific enolase and pro-gastrin releasing peptide have been satisfactory after more than 3 years of follow-up. …
• NAID 120005528116

• 集学的治療にて比較的長期予後を得られている前立腺小細胞癌の1例

• 堀江 憲吾,亀山 紘司,水谷 晃輔 [他],菅原 崇,清家 健作,土屋 朋大,安田 満,横井 繁明,仲野 正博,出口 隆,酒々井 夏子,広瀬 善信
• 泌尿器科紀要 = Acta urologica Japonica 60(10), 517-521, 2014-10
• … His levels of neuron-specific enolase (NSE) and pro-gastrin-releasing peptide (Pro-GRP) were high. …
• NAID 120005511052

• 症例 Pro-gastrin-releasing peptide (proGRP)高値を呈した孤立性肺定型カルチノイドの3例

• 髙橋 源,富澤 由雄,土屋 卓磨 [他]
• 日本呼吸器学会誌 = Annals of the Japanese Respiratory Society 3(3), 432-437, 2014-05-10
• NAID 40020110789

Related Links

• Gastrin-releasing peptide - Wikipedia, the free encyclopedia

Gastrin-releasing peptide, also known as GRP, is 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 ...

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