THE LOW-MOLECULAR WEIGHT COLLAGEN SYNTHESIZED BY CHICK TIBIAL CHONDROCYTES IS DEPOSITED IN THE EXTRACELLULAR-MATRIX BOTH IN CULTURE AND INVIVO
THE LOW-MOLECULAR WEIGHT COLLAGEN SYNTHESIZED BY CHICK TIBIAL CHONDROCYTES IS DEPOSITED IN THE EXTRACELLULAR-MATRIX BOTH IN CULTURE AND INVIVO
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DOI：
10.1002/j.1460-2075.1984.tb01891.x
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发表时间：
1984-01-01
期刊：
影响因子：
11.4
通讯作者：
CANCEDDA, R
中科院分区：
文献类型：
--
作者：
CAPASSO, O;QUARTO, N;CANCEDDA, R
鸡胚软骨细胞在培养中合成的低分子量胶原蛋白（64 K）沉积在细胞外基质中;其沉积严格依赖于正确的羟基化。从17日龄鸡胚胫骨软骨中分离64 K胶原。这种胶原在细胞外基质中的周转非常迅速：在几个小时内，它成熟为释放在培养基中的30 K片段。这种成熟依赖于分子的正确羟基化。在不存在抗坏血酸或在α-抗坏血酸存在下合成的羟基化不足的形式。α的联吡啶不沉积在细胞外基质中，并在培养基中直接分泌为64 K胶原。
The low MW collagen (64 K) synthesized by chick embryo chondrocytes in culture is deposited in the extracellular matrix; its deposition is strictly dependent upon a correct hydroxylation. In vivo the 64 K collagen was isolated from the cartilage of tibiae obtained from 17-day-old chick embryos. The turnover of this collagen in the extracellular matrix is very rapid: within a few hours it is matured into a 30 K fragment released in the medium. This maturation is dependent upon a correct hydroxylation of the molecule. The underhydroxylated form, synthesized in the absence of ascorbic acid or in the presence of .alpha.-.alpha.'' dipyridyl, is not deposited in the extracellular matrix and is directly secreted as 64 K collagen in the culture medium.