Tyrosine kinase-dependent phosphatidylinostiol turnover and functional responses in the Fc epsilon R1 signalling pathway.

Abstract:

:In RBL-2H3 rat basophilic leukemia cells, Fc epsilon R1 crosslinking by multivalent antigen stimulates phosphatidylinositol (PI) turnover and Ca2+ influx and causes functional responses that include secretion, membrane ruffling and actin polymerization. Here, we show that the tyrosine kinase inhibitor, genistein, inhibits antigen-induced PI turnover, determined from assays of 1,4,5-inositol trisphosphate production, and impairs receptor-mediated secretion, ruffling and actin polymerization. Genistein has little effect on several functional responses to stimuli that bypass PI hydrolysis (ionomycin-induced secretion, phorbol ester-induced ruffling) but it inhibits phorbol ester-induced actin polymerization. These data implicate a common tyrosine kinase-dependent event, most likely the activation of phospholipase C gamma, in the Fc epsilon R1-mediated stimulation of PI turnover, secretion and ruffling. There may be additional tyrosine kinase-mediated events in the actin assembly pathway.

authors

Deanin GG,Martinez AM,Pfeiffer JR,Gardner ME,Oliver JM

doi

10.1016/0006-291x(91)91406-3

subject

Has Abstract

pub_date

1991-08-30 00:00:00

pages

551-7

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(91)91406-3

journal_volume

179

pub_type

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