Human skin collagenase. The role of serum alpha-globulins in the control of activity in vivo and in vitro.

An antibody against human skin collagenase obtained from tissue culture has been used to demonstrate the presence of immunoreactive collagenase in human skin extracts that have no detectable enzyme activity. Gel filtration of these skin extracts permits the separation of collagenase in its active form from the other proteins in the crude mixture. The recovery of enzymatically active collagenase appears to be due to the chromatographic separation of the enzyme from the serum antiproteases, alpha(1)-antitrypsin and alpha(2)-macroglobulin, suggesting that collagenase activity in fresh tissue extracts is masked by these known collagenase inhibitors. These findings are supported by in vitro studies untilizing human skin explants in tissue culture. The demonstration of collagenase in vivo in human skin indicates that the enzyme is present at concentrations that are of physiologic significance in collagen remodeling. Evidence is also presented that these findings are not unique to human skin.