Human skin collagenase: isolation of precursor and active forms from both fibroblast and organ cultures

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Abstract
Human skin procollagenase was isolated, in pure form, from the medium of fibroblasts cultured in the presence or absence of added serum. Purification was achieved using a combination of cation-exchange (phosphocellulose or carboxymethylcellulose) and gel-filtration chromatography. Two forms (60,000 and 55,000 daltons) of the procollagenase were detected by electrophoresis in sodium dodecyl sulfate-polyacrylamide gels and could be separated by chromatography on Ultrogel AcA-44. Each form was converted to active enzyme by trypsin, producing species of 50,000 and 45,000 daltons, respectively. An autoactivation process also occurred, which yielded active enzyme without a detectable change in MW. Procollagenase also was found in organ cultures of human skin but only when serum was added to the medium. This suggests that a serum-inhibitable proteolytic system is present in these cultures which, like trypsin, converts procollagenase to the active enzyme forms that can be isolated from serum-free organ culture medium. The collagenase species obtained from either fibroblast or organ culture medium were chromatographically and electrophoretically identical.

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