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Am J Physiol Renal Physiol (June 20, 2007). doi:10.1152/ajprenal.00497.2006
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Submitted on December 14, 2006
Accepted on June 8, 2007

HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN K CONTRIBUTES TO ANGIOTENSIN II STIMULATION OF VASCULAR ENDOTHELIAL GROWTH FACTOR mRNA TRANSLATION

Denis Feliers1*, Myung-Ja Lee1, Goutam Ghosh-Choudhury1, Karol Bomsztyk2, and Balakuntalam S Kasinath1

1 Medicine, UTHSCSA, San Antonio, Texas, United States
2 School of Medicine Lake Union, University of Washington, Seattle, Washington, United States

* To whom correspondence should be addressed. E-mail: feliers{at}uthscsa.edu.

Angiotensin II (Ang II) rapidly increases VEGF synthesis in proximal tubular epithelial cells through mRNA translation. The role of heterogeneous nuclear ribonucleoprotein K (hnRNP K) in Ang II regulation of VEGF mRNA translation initiation was examined. Ang II activated hnRNP K as judged by binding to poly(C)- and poly(U)-agarose. Ang II increased hnRNP K binding to VEGF mRNA at the same time as it stimulated its translation, suggesting that hnRNP K contributes to VEGF mRNA translation. Inhibition of hnRNP K expression by RNA interference significantly reduced Ang II stimulation of VEGF synthesis. Ang II increased hnRNP K phosphorylation on both tyrosine and serine residues with distinct time-courses; only Ser302 phosphorylation paralleled binding to VEGF mRNA. Src inhibition using PP2 or RNA interference inhibited PKC{delta} activity and prevented hnRNP K phosphorylation on both tyrosine and serine residues and its binding to VEGF mRNA. Under these conditions, Ang II-induced VEGF synthesis was inhibited. Ang II treatment induced redistribution of both VEGF mRNA and hnRNP K protein from light to heavy polysomal fractions, suggesting increased binding of hnRNP K to VEGF mRNA that is targeted for increased translation. This study shows that hnRNP K augments efficiency of VEGF mRNA translation stimulated by Ang II.




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