Erratum to ‘Gastrin releasing peptide-preferring bombesin binding sites in human lung’ [Eur. J. Pharmacol. 265 (1994) 117–120]
0
Citation
0
Reference
10
Related Paper
Keywords:
Gastrin-releasing peptide
Human small cell lung carcinoma (SCLC) cells have been shown to contain significant levels of a bombesin-immunoreactive peptide. The 27-amino acid peptide, gastrin releasing peptide (GRP), has recently been shown to be responsible for the bombesin-like immunoreactivity found in SCLC cells. Among four lung cancer cell lines examined in vitro, GRP exhibited mitogenic activity for two SCLC subtypes, but not for a squamous carcinoma or adenocarcinoma lung cell line. The mitogenicity of the GRP molecule has been isolated to the carboxyterminal fragment, designated GRP 14-27, which is in part homologous to bombesin. The aminoterminal fragment, GRP 1-16, is no homologous to bombesin and exhibits no mitogenic activity. Thus, GRP may be an important growth regulating or autocrine factor in human SCLC.
Gastrin-releasing peptide
Cite
Citations (220)
On the basis of structural homology and similar biological activity, gastrin-releasing peptide (GRP) has been considered the mammalian equivalent of amphibian bombesin. In this paper we now show this to be incorrect. Chromatography of frog (Bombina orientalis) gut extracts demonstrated two peaks of bombesin-like immunoreactivity (BLI), one similar in size to GRP and one similar in size to amphibian bombesin. These peaks were purified by high pressure liquid chromatography then subjected to mass spectrometric analyses to determine molecular weights and amino acid sequence. Based on the amino acid sequence of the lower molecular weight BLI species, a mixed oligonucleotide probe was prepared and used to screen a B. orientalis stomach cDNA library. Sequence analysis showed that all hybridizing clones encoded a 155-amino acid protein homologous to the mammalian GRP precursor. The mass spectra of the high and low molecular weight peaks of frog gut BLI were consistent with their origin from the processing of the frog GRP (fGRP) precursor into GRP-29 and GRP-10, just like the processing of the rat GRP precursor. Sequence homology showed that the fGRP precursor is more homology showed that the fGRP precursor is more closely related to the mammalian GRP precursors than to either the frog bombesin or frog ranatensin precursors. Northern blot analysis showed that fGRP is encoded by a mRNA of 980 bases, clearly different from the 750-base mRNA which encodes frog bombesin. Northern blot analysis and in situ hybridization showed fGRP mRNA in frog brain and stomach and bombesin mRNA in frog skin, brain, and stomach. That frogs have independent genes for both GRP and bombesin raises the possibility that mammals have an as yet uncharacterized gene encoding a true mammalian bombesin.
Gastrin-releasing peptide
Cloning (programming)
Cite
Citations (79)
The effects of gastrin-releasing peptide (GRP), bombesin, GRP-(1–16) and GRP-(21–27) on guinea pig nasal mucosal secretion were studied in vivo. GRP, bombesin, and GRP-(21–27) induced significant secretion of total protein, albumin, and alkaline phosphatase. GRP induced significant secretion at lower concentrations (10(-11) and 10(-10) M) than were required for bombesin and GRP-(21–27) (10(-7) M). GRP-(1–16) did not stimulate secretion, indicating that the COOH-terminal region of GRP contained the secretagogic principle. Capsaicin, a stimulant of nociceptive sensory nerves, stimulated GRP release into nasal secretions. These data suggest that GRP is present in guinea pig nasal mucosa and that the COOH-terminal region of GRP may regulate mucosal macromolecule secretion.
Gastrin-releasing peptide
Cite
Citations (1)
Gastrin-releasing peptide
Cite
Citations (1)
AbstractGastrin-releasing peptide (GRP), the mammalian bombesin (BN), appears to be involved in the growth of several neoplasms. BN/GRP receptors (BN/GRP-Rs) are expressed in a variety of cancer cells and have limited distribution in normal human tissue. Thus inhibition of BN/GRP-Rs represents an attractive target for pharmacological treatment of some human malignancies. This review will focus on intracellular signaling pathways, which have been characterized to mediate BN/GRP-dependent receptor biological effects as well as on various approaches to target BN/GRP-Rs for therapeutic and diagnostic interventions in human malignancies.
Gastrin-releasing peptide
Cite
Citations (63)
Gastrin-releasing peptide
Cite
Citations (35)
Gastrin-releasing peptide
Rana ridibunda
Cite
Citations (21)
The objective of this study was to compare the gastrin- and gastric inhibitory peptide (GIP)-releasing actions of bombesin, gastrin-releasing peptide (GRP)-27, neuromedin B, and GRP-10 in rats. Both bombesin and GRP-27 are potent stimulants of gastrin and GIP release, whereas neuromedin B and GRP-10 are less effective, on a molar basis.
Gastrin-releasing peptide
Gastrointestinal hormone
G cell
Cite
Citations (13)
Gastrin-releasing peptide
Cite
Citations (0)