Genistein inhibits calcium release by platelet-derived growth factor but not bradykinin or cadmium in human fibroblasts.

Abstract:

:Cd2+ provokes inositol trisphosphate production and releases stored Ca2+, apparently by binding to a zinc site in the external domain of an orphan receptor. One microM Cd2+ evokes an immediate spike in cytosolic free Ca2+, which is similar to that evoked by bradykinin. Platelet-derived growth factor (PDGF) also increases free Ca2+ in human dermal fibroblasts, but there is a distinct lag before free Ca2+ rises in response to PDGF. Genistein, which selectively inhibits tyrosine kinases, markedly inhibited Ca2+ mobilization evoked by PDGF. Calcium mobilization triggered by cadmium or bradykinin was relatively insensitive to genistein. The PDGF receptor is known to be a tyrosine kinase, which phosphorylates and thereby activates phospholipase C gamma, whereas a G protein couples the bradykinin receptor to another phospholipase C isoform. These findings support the hypothesis that the orphan receptor triggered by cadmium is coupled to phospholipase C via a G protein.

journal_name

Cell Biol Toxicol

authors

Lyu RM,Smith JB

doi

10.1007/BF00757576

subject

Has Abstract

pub_date

1993-04-01 00:00:00

pages

141-8

issue

2

eissn

0742-2091

issn

1573-6822

journal_volume

9

pub_type

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