Underhydroxylated Minor Cartilage Collagen Precursors Cannot Form Stable Triple Helices

Overview

Journal Biochem J

Specialty Biochemistry

Date 1988 Feb 15

PMID 3355524

Citations 2

Authors

C C Clark

C F RICHARDS

Affiliations

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Abstract

Matrix-free cells from chick-embryo sterna were incubated with various concentrations of 2,2'-bipyridyl, an iron chelator that inhibits prolyl hydroxylase and lysyl hydroxylase. At concentrations in the region of 0.1 mM, significant effects on cartilage collagen hydroxylation and secretion were observed. When the underhydroxylated collagens were subsequently digested with chymotrypsin or chymotrypsin plus trypsin at 4 degrees C for 15 min, the minor cartilage collagen precursors (namely types IX and XI) were extensively degraded; type II procollagen was only partially susceptible and was converted into underhydroxylated collagen. The results demonstrate that there were significant differences in triple-helix stability among cartilage collagens such that the underhydroxylated minor collagen precursors were unable to attain a native structure under conditions where type II procollagen was successful.

Citing Articles

Reconstitution of the folding pathway of collagen in a cell-free system: formation of correctly aligned and hydroxylated triple helices.

Middleton R, Bulleid N Biochem J. 1993; 296 ( Pt 2):511-7.

PMID: 8257444 PMC: 1137724. DOI: 10.1042/bj2960511.

Inhibition of prolyl hydroxylation and procollagen processing in chick-embryo calvaria by a derivative of pyridine-2,4-dicarboxylate. Characterization of the diethyl ester as a proinhibitor.

Tschank G, Brocks D, ENGELBART K, Mohr J, Baader E, Gunzler V Biochem J. 1991; 275 ( Pt 2):469-76.

PMID: 1850989 PMC: 1150076. DOI: 10.1042/bj2750469.

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