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Genistein Inhibits PDGF-stimulated Proteoglycan Synthesis in Vascular Smooth Muscle Without Blocking PDGFβ Receptor Phosphorylation

Genistein Inhibits PDGF-stimulated Proteoglycan Synthesis in Vascular Smooth Muscle Without Blocking PDGFβ Receptor Phosphorylation

Peter J Little, Robel Getachew, Hossein Babaahmadi Rezaei, Estella Sanchez-Guerrero, Levon M Khachigian, Haitao Wang, Sufen Liao, Wenhua Zheng, Mandy L Ballinger, Narin Osman

Arch Biochem Biophys. 2012 Sep 1;525(1):25-31.

PMID: 22683649

Abstract:

The signaling pathways that regulate the synthesis and structure of proteoglycans secreted by vascular smooth muscle cells are potential therapeutic targets for preventing lipid deposition in the early stage of atherosclerosis. PDGF stimulates both core protein expression and elongation of glycosaminoglycan (GAG) chains on proteoglycans. In this study we investigated the effects of the tyrosine kinase inhibitor genistein on PDGF mediated receptor phosphorylation and proteoglycan synthesis in human vascular smooth muscle cells. We demonstrate that genistein does not block phosphorylation of the activation site of the PDGF receptor at Tyr(857) and two other downstream sites Tyr(751) and Tyr(1021). Genistein blocked PDGF-mediated proteoglycan core protein synthesis however it had no effect on GAG chain elongation. These results differ markedly to two other tyrosine kinase inhibitors, imatinib and Ki11502, that block PDGF receptor phosphorylation and PDGF mediated GAG elongation. We conclude that the action of genistein on core protein synthesis does not involve the PDGF receptor and that PDGF mediates GAG elongation via the PDGF receptor.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP347155764-A	Ki11502		347155-76-4	Price

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