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Originally published In Press as doi:10.1074/jbc.M909174199 on April 13, 2000

J. Biol. Chem., Vol. 275, Issue 26, 20197-20203, June 30, 2000
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Phosphorylation of Osteopontin Is Required for Inhibition of Vascular Smooth Muscle Cell Calcification*

Shuichi JonoDagger §, Christopher Peinado, and Cecilia M. Giachelli||

From the  Department of Bioengineering, University of Washington, Seattle, Washington 98195 and the Dagger  Second Department of Internal Medicine, Osaka City University Medical School, Osaka 545, Japan

Osteopontin (OPN) is a non-collagenous, glycosylated phosphoprotein associated with biomineralization in osseous tissues, as well as ectopic calcification. We previously reported that osteopontin was co-localized with calcified deposits in atherosclerotic lesions, and that osteopontin potently inhibits calcium deposition in a human smooth muscle cell (HSMC) culture model of vascular calcification. In this report, the role of phosphorylation in osteopontin's mineralization inhibitory function was examined. The ability of OPN to inhibit calcification completely depended on post-translational modifications, since bacteria-derived recombinant OPN did not inhibit HSMC mineralization. Following casein kinase II treatment, phosphorylated OPN (P-OPN) dose-dependently inhibited calcification of HSMC cultured in vitro about as effectively as native OPN. The inhibitory effect of osteopontin depended on the extent of phosphorylation. To determine the specific structural domains of OPN important for inhibition of calcification, we compared OPN fragments (N-terminal, C-terminal, and full-length), and compared the inhibitory effect of both phosphorylated and non-phosphorylated fragments. While none of the non-phosphorylated OPN fragments effected calcification, P-OPN caused dose dependent inhibition of HSMC calcification. P-OPN was treated with alkaline phosphatase to create dephosphorylated OPN. Dephosphorylated OPN did not have an inhibitory effect on calcification. The expression of OPN mRNA and P-OPN secretion by HSMC were decreased in a time-dependent manner during culture calcification. These results indicate that phosphorylation is required for the inhibitory effect of OPN on HSMC calcification, and that regulation of OPN phosphorylation represents one way in which mineralization may be controlled by cells.

* This work was supported in part by Grant R01 Hl62329-01 and National Science Foundation Grant EEC9529161.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Recipient of a grant from the Lilly Fellowship Program for Bone and Mineral Research (Ely Lilly Japan, KK, and the Japan Osteoporosis Foundation).

|| Established Investigator of the American Heart Association. To whom all correspondence and reprint requests should be addressed: Bioengineering Dept., Box 351720, University of Washington, Bagley Hall Rm. 479, Seattle, WA 98195. Tel.: 206-543-0205; Fax: 206-616-9763; E-mail: ceci@u.washington.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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