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 G α 2 and G α 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 C 3 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 (C 2 + C 3 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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