【摘 要】
：
Mass spectrometry-based proteomic analyses performed on cartilage tissue extracts identified the serine protease HtrA1 as a major protein component of human
【机 构】
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Departments of Women 's Health and Musculoskeletal Biology
【出 处】
：
2007 Enzyme Engineering Conference(国际酶工程学术会议)
论文部分内容阅读
Mass spectrometry-based proteomic analyses performed on cartilage tissue extracts identified the serine protease HtrA1 as a major protein component of human articular cartilage,with elevated levels occurring in association with osteoarthritis[1].Adenoviral infection of primary human chondrocytes with constructs encoding HtrA1 revealed that overexpression of the protease caused a marked reduction in proteoglycan content in chondrocyte-seeded alginate cultures.In addition,TGF--induced proteoglycan synthesis was repressed by HtrA1,and this inhibitory influence of HtrA1 was dependent on its proteolytic activity,since an active site mutant (Ser328A1a) failed to show an effect.
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