Evidence for procollagen, a biosynthetic precursors of collagen.

Abstract:

:Incubation of rat calvaria for short times in the presence of a labeled amino acid revealed the existence of a collagen fraction (procollagen) that functions as a biosynthetic precursor of collagen. Procollagen contains an alpha1-like chain (pre-alpha1) that elutes earlier from CM-cellulose than does rat-bone alpha1 and has a molecular weight, estimated by acrylamide gel electrophoresis, of 120,000. A time-dependent conversion of pre-alpha1 to alpha1 was demonstrated by incubation of calvaria for periods varying from 9 to 60 min and by a pulse-chase experiment. Limited cleavage of procollagen with pepsin resulted in a molecule with a chain resembling alpha1 in chromatographic properties, molecular weight, and relative hydroxyproline and proline contents. Thus, conversion of procollagen to collagen is likely to occur in vivo by a proteolytic mechanism. The additional peptide sequences in procollagen may serve to initiate chain association in triple-helix formation, to facilitate molecular transport, and to inhibit intracellular fibrogenesis.

authors

Bellamy G,Bornstein P

doi

10.1073/pnas.68.6.1138

subject

Has Abstract

pub_date

1971-06-01 00:00:00

pages

1138-42

issue

6

eissn

0027-8424

issn

1091-6490

journal_volume

68

pub_type

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