ENZYMES CONVERTING PROCOLLAGENS TO COLLAGENS
ENZYMES CONVERTING PROCOLLAGENS TO COLLAGENS
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DOI:
10.1002/jcb.240280104
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发表时间:
1985-01-01
影响因子:
4
通讯作者:
RYHANEN, L
中科院分区:
文献类型:
--
作者:
PELTONEN, L;HALILA, R;RYHANEN, L
Conversion from [human] procollagen to collagen is a specific process that is a requirement for proper alignment of collagen molecules to form functional fibers. This process is catalyzed by at least 3 structurally and functionally distinct enzymes cleaving collagen types I-III. The cleavage processes possibly taking place in the more recently discovered collagen types are not known to any extent at this time. Two amino-terminal proteinases, one cleaving type I and type II procollagens and the other cleaving type III procollagen, were purified close to homogeneity, and the more unspecific activity of carboxy-terminal proteinase was isolated from several tissues. In the experimental model cleavage of the carboxy-terminal propeptides of types I and III procollagen is differently affected by Lys. This suggests the presence of at least 2 distinct enzymes for the removal of carboxyl-terminal propeptides. The regulation of the reaction process from procollagen to collagen is not well known at present. The importance of the phenomenon in terms of fibril formation is demonstrated by several elegant studies in vitro; and certain genetic disorders in which this process is defective demonstrate the significance in vivo. The factors shown to effect the cleavage process may be potentially beneficial in the treatment of the pathological processes with abnormal collagen accumulation such as fibrosis. The current knowledge of the converting enzymes is reviewed, including some very recent findings of this laboratory as well as the evidence presented for the biological significance of the conversion process.