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. 1989 Nov 20;210(2):337-45.
doi: 10.1016/0022-2836(89)90335-5.

Pleomorphism in type I collagen fibrils produced by persistence of the procollagen N-propeptide

D J Hulmes  1 , K E Kadler, A P Mould, Y Hojima, D F Holmes, C Cummings, J A Chapman, D J Prockop
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Pleomorphism in type I collagen fibrils produced by persistence of the procollagen N-propeptide

D J Hulmes et al. J Mol Biol. .

Abstract

The assembly of type I collagen and type I pN-collagen was studied in vitro using a system for generating these molecules enzymatically from their immediate biosynthetic precursors. Collagen generated by C-proteinase digestion of pC-collagen formed D-periodically banded fibrils that were essentially cylindrical (i.e. circular in cross-section). In contrast, pN-collagen generated by C-proteinase digestion of procollagen formed thin, sheet-like structures that were axially D-periodic in longitudinal section, of varying lateral widths (up to several microns) and uniform in thickness (approximately 8 nm). Mixtures of collagen and pN-collagen assembled to form a variety of pleomorphic fibrils. With increasing pN-collagen content, fibril cross-sections were progressively distorted from circular to lobulated to thin and branched structures. Some of these structures were similar to fibrils observed in certain heritable disorders of connective tissue where N-terminal procollagen processing is defective. The observations are considered in terms of the hypothesis that the N-propeptides are preferentially located on the surface of a growing assembly. The implications for normal diameter control of collagen fibrils in vivo are discussed.

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