Inhibition of PDGF-induced phosphoinositide turnover by glucopiercidin A

Cited 0 time in scopus
Metadata Downloads
Inhibition of PDGF-induced phosphoinositide turnover by glucopiercidin A
Soon Cheol Ahn; Bo Yeon Kim; Chan Sun Park; Hyun Sun Lee; Pan Ghill Suh; Sung Ho Ryu; Hyune Mo Rho; J S Rhee; Tae Ick MheenJong Seog Ahn
Bibliographic Citation
Biochemistry and Molecular Biology International, vol. 37, no. 1, pp. 125-132
Publication Year
In the search for a substance which would specifically block a particular step in the signal transduction cascade, we identified glucopiericidin A produced by Streptomyces sp. as an inhibitor of phosphoinositide (PI)-turnover in phospholipase-Cγ1 (PLC-γ1) overexpressing NIH 3T3 fibroblasts (NIH 3T3γ1). Glucopiericidin A inhibited the formation of inositol phosphate (IP(t)) in platelet-derived growth factor (PDGF)-stimulated NIH 3T3γ1 cells with an IC50 of 5.0 μM. In vitro enzyme assay showed the compound had no inhibitory effect on PLC-γ1 even at 100 μM concentration. Glucopiericidin A reduced PDGF-induced tyrosine phosphorylations of proteins, including PDGF receptor and PLC-γ1, in the cells. In contrast, glucopiericidin A showed only a slight inhibitory effect on epidermal growth factor (EGF)-induced IP(t) production and protein tyrosine phosphorylations in A431 cells. These results suggest that glucopiericidin A inhibits PDGF-induced activation of PLC-γ1 by reducing the tyrosine kinase activity of the PDGF receptor and it more potently inhibits PI-turnover induced by PDGF than by EGF.
phospholipase Cγ1EGFglucopiericidin APDGFphosphoinositide-turnover
Appears in Collections:
Ochang Branch Institute > Chemical Biology Research Center > 1. Journal Articles
Ochang Branch Institute > Natural Product Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.

Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.