The post-translational phenotype of collagen synthesized by SAOS-2 osteosarcoma cells |
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Authors: | Fernandes Russell J Harkey Michael A Weis Maryann Askew Jennifer W Eyre David R |
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Affiliation: | Department of Orthopaedics and Sports Medicine, Box 356500, University of Washington, Seattle, WA 98195-6500, USA. rjf@u.washington.edu |
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Abstract: | The human osteosarcoma-derived cell line, SAOS-2, exhibits many of the phenotypic characteristics of osteoblasts including the deposition of types I and V collagens in an extracellular matrix. Lesser amounts of collagen XI chains were also detected. The cell layer collagen contains hydroxylysyl pyridinoline cross-links but without the accompanying lysyl pyridinoline typical of human bone collagen. This indicates that the lysine residues at the two helical cross-linking loci are fully hydroxylated. The isoform of lysyl hydroxylase, LH1, known to be required for full hydroxylation at these sites, was shown to be highly expressed by SAOS-2 cells. Our findings provide insight on the mechanism of post-translational overmodification of lysine residues in collagen made by osteosarcoma tumors, and may be relevant for understanding a similar overmodification observed in osteoporotic bone. |
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