HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 277, Issue 37, 33537-33540, September 13, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/37/33537    most recent C200342200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Mishra-Gorur, K. Articles by Castellot, J. J. Search for Related Content PubMed PubMed Citation Articles by Mishra-Gorur, K. Articles by Castellot, J. J., Jr.

ACCELERATED PUBLICATION
The S18 Ribosomal Protein Is a Putative Substrate for Ca²⁺/Calmodulin-activated Protein Kinase II^*

Ketu Mishra-Gorur, Harold A. Singer^§, and John J. Castellot Jr.^¶

From the  Program in Cell, Molecular, and Developmental Biology, Sackler School of Biomedical Sciences, Tufts University, Boston, Massachusetts 02111, ^§ Center for Cardiovascular Sciences, Albany Medical College, Albany, New York 12208, and ^¶ Department of Anatomy and Cell Biology, Tufts University School of Medicine, Boston, Massachusetts 02111

The -isoform of Ca²⁺/calmodulin-activated protein kinase II (CaMK II) is abundantly expressed in vascular smooth muscle, but relatively little is known about its regulation or its potential cellular substrates. There are few, if any, known substrates of CaMK II that are physiologically relevant in vascular smooth muscle cells. Studies presented earlier (Mishra-Gorur, K., Singer, H. A., and Castellot, J. J., Jr. (2002) Am. J. Pathol., in press) by our laboratory show an inhibitory effect of heparin on CaMK II phosphorylation and activity. During these studies we observed the specific co-immunoprecipitation of a 20-kDa protein with CaMK II. Purification and sequence analysis indicate that this protein is the S18 protein of the 40 S ribosome. S18 was found to be abundantly phosphorylated in response to serum treatment, and this effect was strongly inhibited by heparin. In addition, KN-93, a specific CaMK II inhibitor, blocks S18 phosphorylation in vascular smooth muscle cells; a concomitant 24% reduction in protein synthesis was observed. Taken together these data support the idea that S18 could be a novel substrate for CaMK II, thus providing a potential link between Ca²⁺-mobilizing agents and protein translation.

This article has been cited by other articles:

				S. J. House, R. G. Ginnan, S. E. Armstrong, and H. A. Singer Calcium/calmodulin-dependent protein kinase II-{delta} isoform regulation of vascular smooth muscle cell proliferation Am J Physiol Cell Physiol, June 1, 2007; 292(6): C2276 - C2287. [Abstract] [Full Text] [PDF]

				S. Fasciano, R. C. Patel, I. Handy, and C. V. Patel Regulation of Vascular Smooth Muscle Proliferation by Heparin: INHIBITION OF CYCLIN-DEPENDENT KINASE 2 ACTIVITY BY p27kip1 J. Biol. Chem., April 22, 2005; 280(16): 15682 - 15689. [Abstract] [Full Text] [PDF]

				J. Dresios, A. Aschrafi, G. C. Owens, P. W. Vanderklish, G. M. Edelman, and V. P. Mauro Cold stress-induced protein Rbm3 binds 60S ribosomal subunits, alters microRNA levels, and enhances global protein synthesis PNAS, February 8, 2005; 102(6): 1865 - 1870. [Abstract] [Full Text] [PDF]