Gastrin-Releasing Peptide (Mammalian Bombesin) Gene Expression in Health and Disease

Sunday, Mary E.; Kaplan, Lee M.; Motoyama, Etsuro K.; Chin, William W.; Spindel, Eliot R.

doi:10.1007/978-1-4612-4502-5_4

Cited by 126 publications

(139 citation statements)

References 148 publications

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“…There are, however, other mechanisms by which bombesin-like peptides may stimulate cancer cell growth. GRP is known to affect the secretion of a number of gut peptides (Sunday et al, 1988) and may thus indirectly stimulate cell growth and division.…”

Section: Discussionmentioning

confidence: 99%

“…These bombesinlike peptides regulate gut motility, influence secretion of enteric peptide hormones and pancreatic exocrine secretion (reviewed in Sunday et al, 1988). The genes encoding GRP and NMB have been cloned and sequenced.…”

mentioning

confidence: 99%

“…The GRP receptor is found in the gut, from oesophagus to rectum (Sunday et al, 1988;reviewed in Spindel et al, 1993); the NMB receptor is present in the oesophageal muscularis mucosa (von Schrenck et al, 1989) and smooth muscle cells from the rectosigmoid colon (Bitar et al, 1993); and expression of the bombesin receptor subtype 3 (BRS-3) is limited, in rats, to germ cells in the testes but is present in a range of human lung cancer cells (Corjay et al, 1991;Fathi et al, 1993). The human GRP receptor and NMB receptor were cloned from placental and peripheral blood genomic libraries, and human small-cell lung cancer (SCLC) cell lines (Corjay et al, 1991).…”

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confidence: 99%

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Bombesin family receptor and ligand gene expression in human colorectal cancer and normal mucosa

et al. 2000

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Bombesin-like peptides and their receptors are widely distributed throughout the gut and are potential mitogens for a number of gastrointestinal (GI) cancers. We have analysed the expression of bombesin-like peptides and their receptor subtypes in normal and neoplastic colorectal tissue. Expression was analysed by reverse transcription polymerase chain reaction (RT-PCR) using receptor and ligand subtype-specific primers and then expression localized by in situ hybridization (ISH) with riboprobes synthesized by in vitro transcription of cloned PCR products. Colorectal cancer tissue and matched normal mucosa from 23 patients were studied. Two of these patients had synchronous adenomatous polyps and two had synchronous hepatic metastases which were also studied. An additional two patients with adenomatous polyps were studied along with matched normal mucosa. Gastrin releasing peptide (GRP) receptor and ligand expression was present in all samples but with overall greater expression in the tumour samples. Neuromedin B (NMB) receptor expression was not detectable. NMB ligand was detected in all but one mucosal sample with overall overexpression in the tumour samples. Bombesin receptor subtype 3 (BRS-3) receptor expression was not detectable. These data support the possibility that GRP may be an autocrine growth factor in colorectal cancer. © 2000 Cancer Research Campaign

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Section: Discussionmentioning

confidence: 99%

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Bombesin family receptor and ligand gene expression in human colorectal cancer and normal mucosa

et al. 2000

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“…GRP is distributed in the brain [3,15], lung [9] and genital organs [2,6,[17][18][19]. The distribution of GRP immunoreactivity in the female genital organs, however, varies among animal species, and even within the same species depending on the reproductive status, i.e., whether nonpregnant or pregnant.…”

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confidence: 99%

Immunolocalization of Gastrin-Releasing Peptide in the Bovine Uterus and Placenta.

Budipitojo

Matsuzaki

Cruzana

et al. 2001

The Journal of Veterinary Medical Science

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ABSTRACT. Gastrin-releasing peptide (GRP), a mammalian homologue of amphibian bombesin, has been suggested to be a novel regulatory peptide in the reproductive tract during pregnancy. In this study, the localization of GRP in the bovine uterus and placenta was demonstrated by immunohistochemistry. Uterine and placental samples were collected from nonpregnant and pregnant specimens, respectively. Tissue sampling was done from the caruncle and intercaruncle of the uterus, and from the placentome (caruncle and cotyledon) and intercotyledon of the placenta. In all the tissues examined, GRP was detected although its immunoreactivity was observed at various degrees. In the uterus, moderate immunoreactivity for GRP was observed in the uterine gland epithelial cells. In the placenta, strong immunoreactivity for GRP was demonstrated in the uterine gland epithelial cells; moderate in superficial epithelial cells; and weak in the trophoblasts, trophoblastic giant cells and cryptal epithelial hybrid cells. In both nonpregnant and pregnant animals, GRP was immunolocalized in the uterine gland secretions and was found predominantly in the supranuclear region of the uterine gland epithelial cells. These findings may suggest that GRP is secreted into the uterine lumen and regulates the intrauterine environment of both the nonpregnant and pregnant bovine by exocrine, autocrine and/or paracrine manner.

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“…A fully active decapeptide identical to the C-terminus of GRP ) has also been isolated from porcine and human tissue (Minamino et al, 1984;Orloff et al, 1984). GRP-like immunoreactivity (GRP-LI) and receptor binding is distributed predominantly in the brain, spinal cord, gut and lung, where it is thought to act both as a growth factor and as a neuroregulatory hormone (Moody et al, 1980;Sunday et al, 1988).…”

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Breast cancer cell-associated endopeptidase EC 24.11 modulates proliferative response to bombesin

Burns

Walker²,

Gray³

et al. 1998

Br J Cancer

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SummaryWe have investigated the production, growth and inactivation of gastrin-releasing peptide (GRP)-like peptides in human breast cancer cell lines. Radioimmunoassay detected GRP-like immunoreactivity (GRP-LI) in T47D breast cancer cells but not in the conditioned medium, indicating rapid clearance. No GRP-LI was found in the ZR-75-1 or MDA-MB-436 cells or their conditioned medium. Highperformance liquid chromatography (HPLC) analysis of the GRP-LI in the T47D cells revealed a major peak, which co-eluted with GRP 18-27 , and a minor more hydrophilic peak. In vitro stimulation of T47D cell growth by bombesin (BN) was enhanced to 138% of control levels (bombesin alone) by the addition of the selective endopeptidase EC 3.4.24.11 inhibitor phosphoramidon (0.1 ng ml -1 ). Fluorogenic analysis using whole cells confirmed low levels of this phosphoramidon-sensitive enzyme on the T47D cells. This enzyme, previously unreported in human breast cancer cells, significantly modulates both T47D growth and its response to BN-induced growth.

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Gastrin-Releasing Peptide (Mammalian Bombesin) Gene Expression in Health and Disease

Cited by 126 publications

References 148 publications

Bombesin family receptor and ligand gene expression in human colorectal cancer and normal mucosa

Bombesin family receptor and ligand gene expression in human colorectal cancer and normal mucosa

Immunolocalization of Gastrin-Releasing Peptide in the Bovine Uterus and Placenta.

Breast cancer cell-associated endopeptidase EC 24.11 modulates proliferative response to bombesin

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