Canty Elizabeth G, Kadler Karl E
Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, The University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, UK.
J Cell Sci. 2005 Apr 1;118(Pt 7):1341-53. doi: 10.1242/jcs.01731.
Collagen fibrils in the extracellular matrix allow connective tissues such as tendon, skin and bone to withstand tensile forces. The fibrils are indeterminate in length, insoluble and form elaborate three-dimensional arrays that extend over numerous cell lengths. Studies of the molecular basis of collagen fibrillogenesis have provided insight into the trafficking of procollagen (the precursor of collagen) through the cellular secretory pathway, the conversion of procollagen to collagen by the procollagen metalloproteinases, and the directional deposition of fibrils involving the plasma membrane and late secretory pathway. Fibril-associated molecules are targeted to the surface of collagen fibrils, and these molecules play an important role in regulating the diameter and interactions between the fibrils.
细胞外基质中的胶原纤维使肌腱、皮肤和骨骼等结缔组织能够承受拉力。这些纤维长度不定、不溶于水，并形成复杂的三维阵列，其延伸范围跨越许多细胞长度。对胶原纤维形成分子基础的研究，为前胶原（胶原蛋白的前体）通过细胞分泌途径的运输、前胶原金属蛋白酶将前胶原转化为胶原蛋白，以及涉及质膜和晚期分泌途径的纤维定向沉积提供了深入了解。纤维相关分子定位于胶原纤维表面，这些分子在调节纤维直径和纤维间相互作用方面发挥着重要作用。
