Lamandé S R, Bateman J F
Department of Paediatrics, University of Melbourne, Royal Children's Hospital, Parkville, Victoria, Australia.
Semin Cell Dev Biol. 1999 Oct;10(5):455-64. doi: 10.1006/scdb.1999.0317.
Procollagen assembly occurs within the endoplasmic reticulum, where the C-propeptide domains of three polypeptide alpha-chains fold individually, and then interact and trimerise to initiate folding of the triple helical region. This highly complex folding and assembly pathway requires the co-ordinated action of a large number of endoplasmic reticulum-resident enzymes and molecular chaperones. Disease-causing mutations in the procollagens disturb folding and assembly and lead to prolonged interactions with molecular chaperones, retention in the endoplasmic reticulum, and intracellular degradation. This review focuses predominantly on prolyl 1-hydroxylase, an essential collagen modifying enzyme, and HSP47, a collagen-specific binding protein, and their proposed roles as molecular chaperones involved in fibrillar procollagen folding and assembly, quality control, and secretion.
前胶原组装发生在内质网中，三条多肽α链的C-前肽结构域在其中单独折叠，然后相互作用并三聚化，以启动三螺旋区域的折叠。这种高度复杂的折叠和组装途径需要大量内质网驻留酶和分子伴侣的协同作用。前胶原中的致病突变会干扰折叠和组装，并导致与分子伴侣的相互作用延长、滞留在内质网中以及细胞内降解。本综述主要关注脯氨酰1-羟化酶（一种必需的胶原修饰酶）和HSP47（一种胶原特异性结合蛋白），以及它们作为参与纤维状前胶原折叠、组装、质量控制和分泌的分子伴侣的假定作用。
