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由α1(V)链(B链)组成的胶原蛋白分子:在外细胞骨架中的明显定位。

Collagen molecules comprised of alpha 1(V)-chains (B-chains): an apparent localization in the exocytoskeleton.

作者信息

Gay S, Rhodes R K, Gay R E, Miller E J

出版信息

Coll Relat Res. 1981;1(1):53-8. doi: 10.1016/s0174-173x(80)80007-0.

Abstract

Antibodies specific for alpha 1(V) chains and native collagen molecules containing the alpha 1(V) chain have been used to study the localization of alpha 1(V)-containing molecules in differentiating hyaline cartilage. Immunofluorescence data show that the undifferentiated mesenchyme contains significant quantities of these molecules throughout the cell-rich tissue matrix. Examination of fully differentiated hyaline cartilage reveals a unique staining pattern wherein the immunofluorescent material is restricted to the pericellular matrix within the chondrocyte lacunae. We conclude from these data in conjunction with other evidence that the Type V collagens function as components of an exocytoskeleton for connective tissue cells.

摘要

针对α1(V)链以及含有α1(V)链的天然胶原分子的抗体,已被用于研究含α1(V)分子在透明软骨分化过程中的定位。免疫荧光数据表明,未分化的间充质在富含细胞的组织基质中含有大量此类分子。对完全分化的透明软骨进行检查发现了一种独特的染色模式,其中免疫荧光物质局限于软骨细胞腔隙内的细胞周围基质。结合其他证据,我们从这些数据得出结论,V型胶原作为结缔组织细胞外细胞骨架的组成部分发挥作用。

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