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Influence of the telopeptides on type I collagen fibrillogenesis

✍ Scribed by Maureen Brennan; Peter F. Davison

Publisher
Wiley (John Wiley & Sons)
Year
1981
Tongue
English
Weight
529 KB
Volume
20
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

Preparations have been made of acid‐soluble collagens whose telopeptides have suffered different levels of proteolytic attack. The collagens with more intact telopeptides form fibrils more rapidly than those with degraded telopeptides. In addition, we have shown that a high molecular weight aggregate rich in the carboxyterminal CNBr peptide, α1CB6, can be found in cyanogen bromide digests of fibrils formed from intact collagen. A similar aggregate is found in CNBr digests of native tendons. The aggregate formed in fibrils assembled in vitro can be stabilized by reduction, and its generation is strongly dependent on the presence of intact telopeptides. The latter point is the most objective evidence that to reproduce the characteristics of native fibrils in vitro, the collagen telopeptides must be preserved from proteolysis.

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