Collagen fibril biosynthesis in tendon: a review and recent insights

被引：86

作者：

Canty, EG ^{[1
]}

Kadler, KE ^{[1
]}

机构：

[1] Univ Manchester, Sch Biol Sci, Wellcome Trust Ctr Cell Matrix Res, Manchester M13 9PT, Lancs, England

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-MOLECULAR AND INTEGRATIVE PHYSIOLOGY | 2002年 / 133卷 / 04期

关键词：

collagen; fibrils; procollagen; extracellular matrix; electron microscopy;

D O I：

10.1016/S1095-6433(02)00212-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The development and evolution of multicellular animals relies on the ability of certain cell types to synthesise an extracellular matrix (ECM) comprising very long collagen fibrils that are arranged in very ordered 3-dimensional scaffolds. Tendon is a good example of a highly ordered ECM, in which tens of millions of collagen fibrils, each hundreds of microns long, are synthesised parallel to the tendon long axis. This review highlights recent discoveries showing that the assembly of collagen fibrils in tendon is hierarchical, and involves the formation of fairly short 'collagen early fibrils' that are the fusion precursors of the very long fibrils that occur in mature tendon. (C) 2002 Elsevier Science Inc. All rights reserved.

引用

页码：979 / 985

页数：7

共 49 条

[1]

AUBERTFOUCHER E, 1992, J BIOL CHEM, V267, P15759

[2]

BACHINGER HP, 1987, J BIOL CHEM, V262, P17144

[3] ROLE OF CIS-TRANS ISOMERIZATION OF PEPTIDE-BONDS IN COIL REVERSIBLE TRIPLE HELIX CONVERSION OF COLLAGEN [J].