Literature DB >> 2557246

Histamine and bradykinin stimulate the phosphoinositide turnover in human umbilical vein endothelial cells via different G-proteins.

T A Voyno-Yasenetskaya1, M P Panchenko, E V Nupenko, V O Rybin, V A Tkachuk.   

Abstract

The G-proteins which regulate hormonal turnover of phosphoinositide (PI) in human umbilical vein endothelial cells have been investigated. A 40-41 kDa doublet present in the membranes of these cells was selectively ADP ribosylated by pertussis toxin (PTx), and this doublet was Gi alpha 2 and Gi alpha 3 according to immunoblotting with specific antisera. By contrast, a doublet of 24-26 kDa proteins in the same membrane preparations was ADP ribosylated by the C3 component of botulinum toxin (BoTx). PTx-dependent ADP ribosylation blocked stimulation of PI turnover by histamine, but did not affect stimulation by bradykinin, whereas BoTx (C2 + C3 components) had the opposite effect. Thus two different groups of G-proteins may be involved in hormone-dependent stimulation of PI turnover in human umbilical vein endothelial cells.

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Year:  1989        PMID: 2557246     DOI: 10.1016/0014-5793(89)81496-6

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  A role for heterotrimeric GTP-binding proteins and ERK1/2 in insulin-mediated, nitric-oxide-dependent, cyclic GMP production in human umbilical vein endothelial cells.

Authors:  O Konopatskaya; A C Shore; J E Tooke; J L Whatmore
Journal:  Diabetologia       Date:  2005-03-01       Impact factor: 10.122

2.  G-protein-mediated regulation of a Ca(2+)-dependent K+ channel in cultured vascular endothelial cells.

Authors:  L Vaca; W P Schilling; D L Kunze
Journal:  Pflugers Arch       Date:  1992-10       Impact factor: 3.657

3.  Interactions of bradykinin, calcium, G-protein and protein kinase in the activation of phospholipase A2 in bovine pulmonary artery endothelial cells.

Authors:  D Ricupero; L Taylor; P Polgar
Journal:  Agents Actions       Date:  1993-09
  3 in total

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