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Identification of osteopontin phosphorylation sites involved in bone remodeling and inhibition of pathological calcification

✍ Scribed by Fawzy A. Saad; Erdjan Salih; Melvin J. Glimcher

Publisher: John Wiley and Sons
Year: 2008
Tongue: English
Weight: 98 KB
Volume: 103
Category: Article
ISSN: 0730-2312
DOI: 10.1002/jcb.21453

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✦ Synopsis

Abstract

Osteopontin is a noncollagenous, phosphorylated extracellular glycoprotein, expressed in mineralized and nonmineralized tissues, organs and body fluids. The protein contains an RGD tripeptide cell‐binding motif, and is subjected to a variety of posttranslational modifications that play important roles in its multiple biological functions, such as bone remodeling and inhibition of pathological calcification. In this study, we have expressed bovine osteopontin in a prokaryotic system and identified the seven amino acid residues phosphorylated in vitro by CKII. J. Cell. Biochem. 103: 852–856, 2008. © 2007 Wiley‐Liss, Inc.

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