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不同软骨组织中胶原蛋白的生物合成与加工

Biosynthesis and processing of collagens in different cartilaginous tissues.

作者信息

Sussman M D, Ogle R C, Balian G

出版信息

J Orthop Res. 1984;2(2):134-42. doi: 10.1002/jor.1100020204.

Abstract

The distribution, structure, and biosynthesis of various collagen types have been studied in growth and structural cartilage from young rabbits. The major collagen of cartilage is alpha 1(II); however, all cartilage matrix also contains 1 alpha, 2 alpha, 3 alpha (Type Cm), as well as a high molecular weight disulfide-linked collagen (Type M). Cartilage fragments in organ culture demonstrate synthesis of precursors of collagen alpha chains and processing to their final forms. Although Type Cm collagen is present in the same proportion in the matrix of growth and structural cartilage, in vitro radiolabeling of rabbit cartilage showed that only growth cartilage is capable of actively synthesizing Type Cm, except in the newborn period when synthesis of Type Cm does occur in structural cartilage. A low molecular weight collagen (designated G collagen) is synthesized in vitro by growth cartilage but not by structural or articular cartilage. Preferential distribution of these minor collagens in growth cartilage suggests a role in development during normal cartilage growth.

摘要

已对幼兔生长软骨和结构软骨中各种胶原类型的分布、结构及生物合成进行了研究。软骨的主要胶原是α1(II);然而,所有软骨基质还含有1α、2α、3α(Cm型),以及一种高分子量的二硫键连接的胶原(M型)。器官培养中的软骨碎片显示出胶原α链前体的合成及其向最终形式的加工过程。尽管Cm型胶原在生长软骨和结构软骨的基质中所占比例相同,但对兔软骨进行的体外放射性标记显示,只有生长软骨能够活跃地合成Cm型,新生期除外,此时结构软骨中确实会发生Cm型的合成。一种低分子量的胶原(称为G胶原)可由生长软骨在体外合成,但结构软骨或关节软骨则不能。这些次要胶原在生长软骨中的优先分布表明它们在正常软骨生长发育过程中发挥作用。

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