The post-translational phenotype of collagen synthesized by SAOS-2 osteosarcoma cells

• Published in: Bone (New York, N.Y.) N.Y.), 2007-05, Vol.40 (5), p.1343-1351
• Main Authors: Fernandes, Russell J, Harkey, Michael A, Weis, Maryann, Askew, Jennifer W, Eyre, David R
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Biological and medical sciences; Bone; Cell Line, Tumor; Collagen - biosynthesis; Collagen - chemistry; Diseases of the osteoarticular system; Gene Expression Regulation; Genome, Human - genetics; Humans; Liver - enzymology; Lysyl hydroxylase; Medical sciences; Molecular Sequence Data; Orthopedics; Osteoporosis. Osteomalacia. Paget disease; Osteosarcoma; Osteosarcoma - metabolism; Phenotype; Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase - genetics; Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase - metabolism; Protein mass spectrometry; Protein Processing, Post-Translational; Pyridinoline; RNA, Messenger - genetics; Tumors of striated muscle and skeleton; Type I collagen; Type V collagen
• ISSN: 8756-3282; 1873-2763
• DOI: 10.1016/j.bone.2007.01.011

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.