Isolation and characterization of collagen A and B chains from chick embryos
Isolation and characterization of collagen A and B chains from chick embryos
复制标题
鸡胚胶原蛋白 A 和 B 链的分离和表征
DOI:
10.1016/0014-5793(79)80258-6
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发表时间:
1979
期刊:
影响因子:
3.5
通讯作者:
K. von der Mark
中科院分区:
文献类型:
--
作者:
H. von der Mark;K. von der Mark
From human fetal membranes two new collagen chains, called A and B chains, have been isolated which are genetically different to the a-chains of types I, II, III and IV collagen [I]. These collagen chains were also found in human skin and in vessel walls [2], in skeletal bovine muscle [3] and in bone and cartilage [4]; in vitro A and B chains are produced by cultures of smooth muscle cells [51. From most tissues and cell cultures twice as much B chains as A chains were obtained which is consistent with the existence of a collagen molecule of the subunit composition AB2 (1.6) similar to type I collagen (~ rl (I))~ ct2. However, another study suggests that A and B chains are subunits of two different triple-helical molecules A3 and Ba [4]. The similarity of A, B-collagen to basement membrane collagen in terms of amino acid composition [1, 4, 6] and its localization in the endomysium [3] suggest the possibility that A, B-collagen may be a constituent of the muscle basal lamina. To answer this question, we attempted to localize this collagen type in chick muscle cell cultures immunohistologically using specific antibodies to chick A, B-collagen. The existence of A, B-collagen-like molecules in non-mammalian species was suggested recently by two in vitro studies.In suspension cultures of freshly-isolated chick tendon fibroblasts [8] and in cultures of embryonic chick neural retina cells [9] two chains were observed which migrated in the positions corresponding to human A and B chains. However, no conclusive data were available as to whether a collagen which is