Pre- and post-translational regulation of osteopontin in cancer

• Published in: Journal of cell communication and signaling Vol. 5; no. 2; pp. 111 - 122
• Main Authors: Anborgh, Pieter H., Mutrie, Jennifer C., Tuck, Alan B., Chambers, Ann F.
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Netherlands 01-06-2011; John Wiley & Sons, Inc
• Subjects: Alternative splicing; Biomedical and Life Sciences; Biomedicine; Body fluids; Bone remodeling; Cancer; CD44 antigen; Cell Biology; Cell surface; Glycosylation; Immune response; Integrins; Isoforms; Life Sciences; Malignancy; Matricellular protein; Metastases; Metastasis; Milk; Osteopontin; Phosphorylation; Post-translation; Post‐translational modification; Proteolysis; Review; Translation; Tumors; Urine; Post-translational modification; Osteopontin; Alternative splicing; Metastasis; Matricellular protein; Cancer
• ISSN: 1873-9601; 1873-961X
• DOI: 10.1007/s12079-011-0130-6

Osteopontin (OPN) is a matricellular protein that binds to a number of cell surface receptors including integrins and CD44. It is expressed in many tissues and secreted into body fluids including blood, milk and urine. OPN plays important physiological roles in bone remodeling, immune response and inflammation. It is also a tumour-associated protein, and elevated OPN levels are associated with tumour formation, progression and metastasis. Research has revealed a promising role for OPN as a cancer biomarker. OPN is subject to alternative splicing, as well as post-translational modifications such as phosphorylation, glycosylation and proteolytic cleavage. Functional differences have been revealed for different isoforms and post-translational modifications. The pattern of isoform expression and post-translational modification is cell-type specific and may influence the potential role of OPN in malignancy and as a cancer biomarker.