Bombesin Receptors on Gastrin Cells a
Bombesin Receptors on Gastrin Cells a
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胃泌素细胞上的铃蟾肽受体
DOI:
--
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发表时间:
1988
影响因子:
5.2
通讯作者:
P. Mantyh
中科院分区:
文献类型:
--
作者:
S. Vigna;A. Giraud;A. Soll;J. Walsh;P. Mantyh
As discussed in detail elsewhere in this volume, bombesin is an amphibian skin peptide with a wide spectrum of biological actions on the central nervous system and on peripheral tissues in mammals. The mammalian counterpart of bombesin is called gastrin-releasing peptide (GRP), because gastrin release in response to potcine gastric extracts was used as the assay of activity in the purification of porcine GRP from such extracts.' When porcine G R P was isolated and sequenced,2 it was found to be chemically as well as biologically homologous to amphibian bombesin. The carboxylterminal nonapeptide sequence of G R P is identical to that of bombesin except for the single substitution of a histidine for a glutamine residue at position 8 from the carboxyl terminus. It has been demonstrated that the carboxyl-terminal nonapeptkle sequence of bombesin is required for full biological activity.' The minimum bombePin fragment with measurable biological activity is the carboxyl-terminal heptapeptider the carboxyl-terminal octapeptide is intermediate in potency between the hepaand nonapeptide.' It is not surprising then that the carboxyl-terminal region of bombesin and of GRP have been highly conserved in evolution, since this region is the most important determinant of biological activity in this family of regulatory peptides. Although the identifying action of bombesin and G R P in mammals is stimulation of the release of gastrin, little is known about the mechanism of this actian. Bombesin stimulates gastrin secretion in vivo in dogs: rats,' and humans! However, the site of action of bombesin and GRP to release gastrin has not been conclusively demonstrated in any species. One of the first requirements for analysis of the mechanism of action of regulatory substances is to identify the target cell. Indirect evidence suggests a direct action of bombesin and G R P on antral gastrin cells, but there has been no unequivocal demonstration of this. Isolated, perfused rat stomachs have been shown to release gastrin into the circulation when bombesin is administered, but somatostatin is also released.'.' Bombesin causes release of gastrin, but not somatostatin, from rat antral glands in vitro.9 Finally, preparations of canine antral mucosal cells enriched in gastrin cells, but also containing other mucosal cell types, have recently been shown to release gastrin into the culture medium in response to bombesin.lO*" Thus, the focus has been increasingly narrowed from whole animals down to isolated stomachs, to isolated
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DOI:
10.1016/s0021-9258(18)32209-9
发表时间:
1983-06
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
J. Westendorf;A. Schonbrunn
通讯作者:
J. Westendorf;A. Schonbrunn
影响因子:
29.4
作者:
Vigna,SR;Mantyh,CR;Giraud,AS;Soll,AH;Walsh,JH;Mantyh,PW
通讯作者:
Mantyh,PW
影响因子:
29.4
作者:
Martindale,R;Kauffman,GL;Levin,S;Walsh,JH;Yamada,T
通讯作者:
Yamada,T
DOI:
10.1172/jci112904
发表时间:
1987
期刊:
The Journal of clinical investigation
影响因子:
--
作者:
Sugano,K;Park,J;Soll,AH;Yamada,T
通讯作者:
Yamada,T