상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

Inhibition of PDGF-induced phospholipase C activation by herbimycin A

Authors 

Bo Yeon KimSoon Cheol AhnDae Ook KangHack Ryong KoWon Keun OhHyun Sun LeeTae Ick MheenHyune Mo RhoJong Seog Ahn

Publisher 

Elsevier

Issue Date 

1996

Citation 

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, vol. 1311, no. 1, pp. 33-36

Keywords 

herbimycin Aphospholipase Cγ1phospholipase Dplate-derived growth factorherbimycin ainositol phosphatephosphatidylethanolaminephospholipase cplatelet derived growth factoranimal cell

Abstract 

Herbimycin A, an inhibitor of protein tyrosine kinases, dose-dependently reduced PDGF-induced inositol phosphates (IF,) accumulation without effect on phosphatidylethanol (PEt) formation in PLC-γ-overexpressing NIH 3T3 (NIH 3T3γ1) cells. The compound also reduced tyrosine phosphorylations of some proteins including PLC-γ1 in response to PDGF. On the other hand, phorbol 12-myristate 13-acetate (PMA)-induced phospholipase D (PLD) activation was reduced by herbimycin A in the cells, indicating that the pathways for PLD activation by PDGF and PMA are different from each other. Also, these results suggest that PLC-γ1 activation is not always an upstream event for PLD activation and that tyrosine phosphorylation of one or more proteins not affected by herbimycin A should be indispensable for PLD activation in PDGF-stimulated NIH 3T3γ1 cells.

ISSN 

0167-4889

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


There are no files associated with this item.
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)