The post-translational phenotype of collagen synthesized by SAOS-2 osteosarcoma cells
The post-translational phenotype of collagen synthesized by SAOS-2 osteosarcoma cells
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DOI：
10.1016/j.bone.2007.01.011
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发表时间：
2007-05-01
期刊：
影响因子：
4.1
通讯作者：
Eyre, David R.
中科院分区：
文献类型：
--
作者：
Fernandes, Russell J.;Harkey, Michael A.;Eyre, David R.
人骨肉瘤衍生的细胞系SAOS-2表现出成骨细胞的许多表型特征，包括在细胞外基质中沉积I型和V型胶原。还检测到较少量的胶原蛋白XI链。细胞层胶原蛋白含有羟赖氨酰吡啶啉交联，但不含人骨胶原蛋白典型的赖氨酰吡啶啉。这表明两个螺旋交联位点处的赖氨酸残基被完全羟基化。赖氨酰羟化酶，LH 1，已知在这些网站完全羟基化所需的亚型，被证明是高度表达的SAOS-2细胞。我们的研究结果提供了深入了解的机制，翻译后过度修饰的赖氨酸残基的胶原骨肉瘤肿瘤，并可能是相关的理解类似的过度修饰观察到的骨质疏松症。(c)2007爱思唯尔公司All rights reserved.
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. (c) 2007 Elsevier Inc. All rights reserved.