Isolation and structure of bombesin and alytesin, two analogous active peptides from the skin of the european amphibiansBombina andAlytes

Ánastasi, A.; Erspamer, V.; Bucci, Mariarosaria

doi:10.1007/bf02145873

Cited by 906 publications

(280 citation statements)

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“…Bombesin, a 14-amino-acid peptide first isolated from the skin of the frog Bombina bombina (Anastasi et al, 1971), is one of a family of closely related amphibian, avian and mammalian peptides which have a highly homologous C-terminal octapeptide (Walsh et al, 1979). The best characterized of the mammalian peptides are gastrin-releasing peptide, originally purified from pig gastric tissue (McDonald et al, 1979), and the neuromedins B and C, from pig spinal cord (Minamino et al, 1983(Minamino et al, , 1984.…”

Section: Introductionmentioning

confidence: 99%

Protein kinase C-mediated negative-feedback inhibition of unstimulated and bombesin-stimulated polyphosphoinositide hydrolysis in Swiss-mouse 3T3 cells

Brown

Blakeley

Hamon

et al. 1987

Biochemical Journal

113

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Bombesin-related peptides stimulate a rapid increase in polyphosphoinositide hydrolysis in Swiss-mouse 3T3 cells. These peptides generate an increase in the efflux of 45Ca2+ from pre-labelled cells, a response consistent with an inositol trisphosphate-mediated mobilization of intracellular Ca2+. The bombesin-stimulated release of cellular 45Ca2+ is inhibited by tumour-promoting phorbol esters (e.g. 12-0-tetradecanoylphorbol 13-acetate, TPA). Although there are several possible sites of action at which this effect might occur, our results indicate that TPA induces an uncoupling of bombesin-stimulated hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) without decreasing cellular binding of bombesin. In cultured cells, protein kinase C can be down-modulated by a prolonged incubation of the cells with phorbol esters. Such pretreatment greatly decreased the inhibitory effect of TPA on bombesin-stimulated PIP2 hydrolysis, suggesting that this action of the phorbol ester is mediated via protein kinase C. Since diacylglycerol is an endogenous activator of protein kinase C and a direct product of PIP2 hydrolysis, these results suggest that protein kinase C inhibition of polyphosphoinositide hydrolysis may function as a negative-feedback pathway. Cells in which protein kinase C has been down-modulated show elevated basal and bombesin-stimulated production of inositol phosphates, providing evidence that such a feedback loop limits polyphosphoinositide turnover in both unstimulated and mitogen-stimulated cells.

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Section: Introductionmentioning

confidence: 99%

Protein kinase C-mediated negative-feedback inhibition of unstimulated and bombesin-stimulated polyphosphoinositide hydrolysis in Swiss-mouse 3T3 cells

Brown

Blakeley

Hamon

et al. 1987

Biochemical Journal

113

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“…The first peptide was isolated in 1970 from the skin of Rana pipiens by Nakajima et al [1] and called ranatensin because of its contractile effects on smooth muscle cells. At the same time, Anastasi et al [2] identified bombesin in the amphibian skin of Bombina bombina. The similarity in structure between the COOH-terminal portions was the basis of a new group of peptides, called bombesin-like peptides.…”

Section: Introductionmentioning

confidence: 94%

Identification of functional GRP‐preferring bombesin receptors on human melanoma cells

Pansky

Peng

Eberhard

et al. 1997

Eur J Clin Investigation

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Abstract. Bombesin was originally isolated from amphibian skin, wherease its mammalian counterpart, gastrinreleasing peptide (GRP), was first identified in the nervous system of the gastrointestinal tract. Whether GRP is present in the human skin is not known. Bombesin-like peptides are also known to modulate growth. We therefore investigated whether human melanoma cell lines express functional GRP-preferring bombesin receptors and whether they alter growth or other specific cellular functions of these tumour cells. . Bombesin dose-dependently increased cytosolic calcium, but did not alter interleukin (IL) 1b-induced reduction of cell viability or IL-6 secretion, both A375-6-specific cell functions. Growth of A375-6 cells was not altered by bombesin or the specific GRP receptor antagonist BIM26226 as measured by [ 3 H]-thymidine incorporation or methylene blue assay, whereas insulin alone or in combination with other potential growth factors dose-dependently stimulated growth of these cells. The newly characterized GRP-preferring bombesin receptors on highly malignant human melanoma cells could initiate studies of growth effects on solid tumours or in vivo scanning using radiolabelled tracers.

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“…179 Human GRP mRNA was later isolated from a lung carcinoid and the sequence deduced. 180 The sequence was later confirmed by Orloff.…”

Section: Gastrin-releasing Peptidementioning

confidence: 99%

Circulating markers for endocrine tumours of the gastroenteropancreatic tract

Ardill

2008

Ann Clin Biochem

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The diffuse endocrine system (DES) includes a wide range of secretory cells that may be the source of tumours. Gastroenteropancreatic endocrine (GEP) tumours arising within the DES secrete a variety of peptides and amines that are found in the circulation and are responsible for the syndromes associated with these tumours. In this review, the most common tumours of the GEP tract are outlined and the circulating products of these tumours identified. Where differential diagnosis is difficult these points are addressed. The peptides most commonly secreted by GEP neuroendocrine tumours are identified and described and their biological activities are discussed. Current methods available for measurement of these peptides are described. Attention is drawn towards molecular specificity where appropriate, as many pancreatic and gut peptides fall within families which show considerable homology, such as the tachykinin family or the glucagon family. Other peptides such as gastrin circulate in multiple molecular forms. This homology and diversity may cause difficulty in the interpretation of peptide measurements in the clinical situation if assays are not specific.

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Isolation and structure of bombesin and alytesin, two analogous active peptides from the skin of the european amphibiansBombina andAlytes

Cited by 906 publications

References 0 publications

Protein kinase C-mediated negative-feedback inhibition of unstimulated and bombesin-stimulated polyphosphoinositide hydrolysis in Swiss-mouse 3T3 cells

Protein kinase C-mediated negative-feedback inhibition of unstimulated and bombesin-stimulated polyphosphoinositide hydrolysis in Swiss-mouse 3T3 cells

Identification of functional GRP‐preferring bombesin receptors on human melanoma cells

Circulating markers for endocrine tumours of the gastroenteropancreatic tract

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