Laboratory of Connective Tissues Biology, GIGA-R, University of Liège, B-4000 Sart Tilman, Belgium.
Laboratory of Connective Tissues Biology, GIGA-R, University of Liège, B-4000 Sart Tilman, Belgium.
Matrix Biol. 2015 May-Jul;44-46:46-53. doi: 10.1016/j.matbio.2015.04.001. Epub 2015 Apr 8.
Collagen fibers are the main components of most of the extracellular matrices where they provide a structural support to cells, tissues and organs. Fibril-forming procollagens are synthetized as individual chains that associate to form homo- or hetero-trimers. They are characterized by the presence of a central triple helical domain flanked by amino and carboxy propeptides. Although there are some exceptions, these two propeptides have to be proteolytically removed to allow the almost spontaneous assembly of the trimers into collagen fibrils and fibers. While the carboxy-propeptide is mainly cleaved by proteinases from the tolloid family, the amino-propeptide is usually processed by procollagen N-proteinases: ADAMTS2, 3 and 14. This review summarizes the current knowledge concerning this subfamily of ADAMTS enzymes and discusses their potential involvement in physiopathological processes that are not directly linked to fibrillar procollagen processing.
胶原纤维是大多数细胞外基质的主要成分，为细胞、组织和器官提供结构支撑。纤维状原胶原作为单个链合成，然后组装形成同型或异型三聚体。其特征是存在中央三螺旋结构域，两侧为氨基和羧基前肽。尽管存在一些例外，这两个前肽必须被蛋白水解酶切割，才能允许三聚体几乎自发地组装成胶原原纤维和纤维。虽然羧基前肽主要被 tolloid 家族的蛋白酶切割，但氨基前肽通常由 procollagen N-蛋白水解酶处理：ADAMTS2、3 和 14。这篇综述总结了目前关于 ADAMTS 酶这一子家族的知识，并讨论了它们在与纤维状原胶原加工不直接相关的生理病理过程中的潜在作用。
