Abstract
Osteopontin is expressed in many different cell types and has been proposed to play several functions. Distinct forms of the protein have been detected. Various tissues and cell lines from mouse, however, exhibit two classes of transcripts with different 5'-untranslated ends but with an identical coding region (exons II through VII). These transcripts do not arise from the alternative splicing of coding exons. These results suggest that posttranslational modifications of osteopontin, such as phosphorylation, are a major mechanism to generate different forms of the protein. Mouse osteopontin was expressed in E. coli and used as a model to study its phosphorylation.
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