Cell type-specific post-translational modifications of mouse osteopontin are associated with different adhesive properties.

Cell type-specific post-translational modifications of mouse osteopontin are associated with different adhesive properties. Research Abstract Details 

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Cell type-specific post-translational modifications of mouse osteopontin are associated with different adhesive properties. Abstract Text:

Brian Christensen,Christian C Kazanecki,Torben E Petersen,Susan R Rittling,David T Denhardt,Esben S ,

Osteopontin (OPN) is a highly modified integrin-binding protein found in all body fluids. Expression of OPN is strongly correlated with poor prognosis in many different human cancers, suggesting an important but poorly understood role for this protein in tumorigenesis and metastasis. The protein exists in a number of different isoforms differing in the degree of post-translational modifications that are likely to exhibit different functional properties. This study examines for the first time the post-translational modifications of OPN from transformed cells and the effects of these modifications on cell biology. We have characterized the complete phosphorylation and glycosylation patterns of OPN expressed by murine ras-transformed fibroblasts (FbOPN) and differentiating osteoblasts (ObOPN) by a combination of mass spectrometric analyses and Edman degradation. Mass spectrometric analysis showed masses of 34.9 and 35.9 kDa for FbOPN and ObOPN, respectively. Enzymatic dephosphorylation, sequence, and mass analyses demonstrated that FbOPN contains approximately four phosphate groups distributed over 16 potential phosphorylation sites, whereas ObOPN contains approximately 21 phosphate groups distributed over 27 sites. Five residues are O-glycosylated in both isoforms. These residues are fully modified in FbOPN, whereas one site is partially glycosylated in ObOPN. Although both forms of OPN mediated robust integrin-mediated adhesion of mouse ras-transformed fibroblasts, the less phosphorylated FbOPN mediated binding of MDA-MD-435 human tumor cells almost 6-fold more than the heavy phosphorylated ObOPN. These results strongly support the hypothesis that the degree of phosphorylation of OPN produced by different cell types can regulate its function.

Cell type-specific post-translational modifications of mouse osteopontin are associated with different adhesive properties. Publishing Authors By Initials

B Christensen,CC Kazanecki,TE Petersen,SR Rittling,DT Denhardt,ES ,

For similar genetic processes: gene expression regulation: protein modification, translational: protein processing, post-translational research abstracts see: genetic processes: gene expression regulation: protein modification, translational: protein processing, post-translational research

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Cell type-specific post-translational modifications of mouse osteopontin are associated with different adhesive properties. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 19463-72

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 11

MONTH: 05

YEAR: 2007

Cell type-specific post-translational modifications of mouse osteopontin are associated with different adhesive properties. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Cell type-specific post-translational modifications of mouse osteopontin are associated with different adhesive properties. Keywords Mesh Terms:

KEYWORDS: Protein Processing, Post-Translational

MESH TERMS: metabolism

Chemical & Substance for Abstract: Cell type-specific post-translational modifications of mouse osteopontin are associated with different adhesive properties. Information

Substance Name: Osteopontin

Registry Number: 106441-73-0

Grant and Affiliation Information for Cell type-specific post-translational modifications of mouse osteopontin are associated with different adhesive properties.

AFFILIATION: Protein Chemistry Laboratory, Department of Molecular Biology, University of Aarhus, DK-8000 Aarhus C, Denmark.

Country: United States

AGENCY: United States NIDDK

GRANT: DK067685

ACRONYM: DK

MEDLINETA: J Biol Chem

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