Platelet-derived growth factor increases the in vivo activity of phospholipase C-gamma 1 and phospholipase C-gamma 2.

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In: Molecular and Cellular Biology, 11(1991), 4, S. 2018 - 2025
Format: E-Artikel
Sprache: Unbestimmt
veröffentlicht: American Society for Microbiology
ISSN: 0270-7306
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finc.mega_collection American Society for Microbiology (CrossRef) ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9tY2IuMTEuNC4yMDE4
finc.source_id 49
ris.type EJOUR
rft.atitle Platelet-derived growth factor increases the in vivo activity of phospholipase C-gamma 1 and phospholipase C-gamma 2.
rft.epage 2025
rft.genre article
rft.issn 0270-7306
rft.issue 4
rft.jtitle Molecular and Cellular Biology
rft.tpages 8
rft.pages 2018-2025 American Society for Microbiology 1991-04-01 1991-04-01T00:00:00Z
rft.spage 2018
rft.volume 11
abstract <jats:p>Upon binding to its cell surface receptor, platelet-derived growth factor (PDGF) causes the tyrosine phosphorylation of phospholipase C-gamma 1 (PLC-gamma 1) and stimulates the production of diacylglycerol and inositol 1,4,5-triphosphate. We showed that following stimulation by PDGF, rat-2 cells overexpressing PLC-gamma 1 display an increase in the levels of both tyrosine-phosphorylated PLC-gamma 1 and inositol phosphates compared with the parental rat-2 cells. This increased responsiveness to PDGF is a direct effect of PLC-gamma 1 overexpression, as a cell line expressing similar levels of an enzymatically inactive point mutant of PLC-gamma 1, PLC-gamma 1 335Q, did not show elevated inositol phosphate production in response to PDGF. Hematopoietic cells express PLC-gamma 2, a PLC isoform that is closely related to PLC-gamma 1. When rat-2 cells overexpressing PLC-gamma 2 were treated with PDGF, an increase in both the tyrosine phosphorylation and the in vivo activity of PLC-gamma 2 was observed. Aluminum fluoride (AIF4-), a universal activator of PLC linked to G-proteins, did not produce an increase in the levels of inositol phosphates in either of the overexpressing cell lines compared with parental rat-2 cells, demonstrating that PLC-gamma isoforms respond specifically to a receptor with tyrosine kinase activity.</jats:p>
authors Sultzman L
Ellis C
Lin L L
Pawson T
Knopf J
doi 10.1128/mcb.11.4.2018
languages und
version 0.9
x.subjects Cell Biology
Molecular Biology
x.type journal-article
x.oa 1