Procollagen processing. Limited proteolysis of COOH-terminal extension peptides by a cathepsin-like protease secreted by tendon fibroblasts.

J M Davidson; L S McEneany; P Bornstein

doi:10.1111/j.1432-1033.1979.tb04201.x

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Procollagen processing. Limited proteolysis of COOH-terminal extension peptides by a cathepsin-like protease secreted by tendon fibroblasts.

J M Davidson·L S McEneany·P Bornstein

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Abstract

An enzymatic activity, capable of removing the COOH-terminal extensions of type I chick procollagen, has been demonstrated in embryonic chick tendons and in cultured tendon fibroblasts utilizing two new methods of analysis. The protease was purified by a combination of ultrafiltration concanavalin A affinity chromatography and gel filtration. The isolated protein has an apparent Mr of 43,000 by gel filtration and sodium dodecyl sulfate gel electrophoresis. The enzyme shows a major pH optimum at 4.2 and is susceptible to inhibitors such as pepstatin and leupeptin; it therefore seems related to the cathepsins. The possibility that this enzyme plays a role in the limited proteolytic processing of procollagen is discussed.

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Animals Cathepsins Cells, Cultured Chick Embryo Fibroblasts Hydrogen-Ion Concentration Kinetics Molecular Weight Peptide Hydrolases Procollagen Protease Inhibitors Tendons Journal Article Research Support, U.S. Gov't, P.H.S.

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J M Davidson, L S McEneany, P Bornstein. 1979-10-15. Procollagen processing. Limited proteolysis of COOH-terminal extension peptides by a cathepsin-like protease secreted by tendon fibroblasts.. https://doi.org/10.1111/j.1432-1033.1979.tb04201.x

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