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. 1985 Apr 15;227(2):491–502. doi: 10.1042/bj2270491

Characterization of a type VI collagen-related Mr-140 000 protein from cutis-laxa fibroblasts in culture.

S W Crawford, J A Featherstone, K Holbrook, S L Yong, P Bornstein, H Sage
PMCID: PMC1144868  PMID: 4004777

Abstract

The precise biochemical defects in connective-tissue metabolism that are responsible for the laxity of skin seen in the syndrome of cutis laxa are largely unknown. We have studied fibroblasts cultured from skin explants of a 2-year-old male with the syndrome. Electron-microscopic examination of this skin revealed decreased amounts of amorphous elastin and an increase in elastin-associated microfibrils. Although the cultured fibroblasts were similar to control skin fibroblasts in morphology, growth rate and total protein synthesis, there was a 4-6-fold increase in accumulation of a collagenous protein of Mr 140 000 in both the culture medium and in the cell layer. This protein was structurally distinct from collagen types I, III, IV, V and VIII. It was found to be related to a cell-surface-associated glycoprotein, GP140, by both antigenic cross-reactivity and peptide mapping. Our data support observations that GP140 is a precursor of at least one form of pepsin-extracted type VI collagen.

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