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• W2022377499 abstract "In order to elucidate the mechanism of cartilage degradation in osteoarthritis (OA), we established a cell assay system. Under the stimulation of all-trans retinoic acid (ATRA), the human chondrosarcoma cell line HCS-2/8 increased proteoglycan release from inactivated bovine nasal cartilage (BNC) and the results suggested the involvement of membrane-bound metalloproteinase(s). Therefore, we focused on the induction of a disintegrin and metalloproteinase (ADAM) superfamily upon ATRA stimulation. Of all ADAMs tested, only ADAM28 was induced by ATRA in HCS-2/8 cells and also in human primary chondrocytes. We found that transfection of ADAM28 or its alternatively spliced soluble form augmented proteoglycan release in the cell assay; however, a mutant soluble form in which a portion of the disintegrin domain was deleted did not have proteoglycan-releasing activity, implying the importance of the domain for enzyme localization and substrate recognition for cartilage degradation in OA." @default.
• W2022377499 created "2016-06-24" @default.
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• W2022377499 date "2009-08-01" @default.
• W2022377499 modified "2023-09-27" @default.
• W2022377499 title "All-trans retinoic acid-induced ADAM28 degrades proteoglycans in human chondrocytes" @default.
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• W2022377499 doi "https://doi.org/10.1016/j.bbrc.2009.06.052" @default.
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