UAP56 is a novel interacting partner of Bcr in regulating vascular smooth muscle cell DNA synthesis.

Abstract

Bcr is a serine/threonine kinase that is a critical regulator of vascular smooth muscle cell inflammation and proliferation. We have previously demonstrated that Bcr acts in part via phosphorylation and inhibition of PPARγ. We have identified the RNA helicase UAP56 as another substrate of Bcr. In this report we demonstrate that knockdown of UAP56 blocks Bcr induced DNA synthesis in vascular smooth muscle cells (VSMC). We also found that over expression of Bcr increased the expression of cyclin E and decreased the expression of p27. Knockdown of UAP56 reversed the effect of Bcr on cyclin E and p27 expression. Furthermore, we found that Bcr binds to UAP56 and demonstrate that binding of UAP56 to Bcr is critical for Bcr induced DNA synthesis in VSMC. Our data identify UAP56 as an important binding partner of Bcr and a novel target for inhibiting vascular smooth muscle cell proliferation.

• Authors: Abha Sahni, Nadan Wang, Jeffrey D Alexis
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 420 Issue 3 Pg. 511-5 (Apr 13 2012) ISSN: 1090-2104 [Electronic] United States
• PMID: 22446327 (Publication Type: Journal Article, Research Support, N.I.H., Extramural)
• Copyright: Copyright © 2012 Elsevier Inc. All rights reserved.

Chemical References

• GTPase-Activating Proteins
• Bcr protein, rat
• Protein Serine-Threonine Kinases
• DDX39B protein, human
• DEAD-box RNA Helicases

Topics

• Animals
• Cells, Cultured
• DEAD-box RNA Helicases (genetics, metabolism)
• DNA Replication
• GTPase-Activating Proteins
• Gene Knockdown Techniques
• HeLa Cells
• Humans
• Muscle, Smooth, Vascular (metabolism)
• Myocytes, Smooth Muscle (metabolism)
• Protein Serine-Threonine Kinases (metabolism)
• Rats