Search PubMed⌕ Search

Biomedical subjects

E A Bauer

Publications and source records attributed to E A Bauer.

117 records · Page 7Linked to original sources
PubMed1971

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.

Alpha-Globulins↗
PubMed1971

Studies on purified rheumatoid synovial collagenase in vitro and in vivo.

Rheumatoid synovial collagenase obtained from culture medium can be separated by Sephadex gel filtration into two peaks of enzyme activity. These have been designated as fast-moving and slow-moving rheumatoid synovial collagenases on the basis of their electrophoretic mobility on polyacrylamide gels. The slow-moving rheumatoid synovial collagenase has been highly purified by affinity chromatography on collagen conjugated to Sepharose and used to prepare a monospecific anti-synovial collagenase antiserum. The antiserum against rheumatoid synovial collagenase has permitted the demonstration of immunoreactive collagenase in extracts of rheumatoid synovial tissue that have no detectable enzymatic activity. Collagenase has also been detected immunologically in enzymatically inactive culture medium from the first 24 hr of culture. Recovery of collagenase activity appears to be related to the chromatographic separation of the enzyme from serum antiproteases. The demonstration of collagenase in vivo in rheumatoid synovium adds further support for the concept that the enzyme is present in tissue at levels that are of significance in the pathogenesis of rheumatoid arthritis. In addition, rheumatoid synovial collagenase and human skin collagenase show complete immunologic identity when reacted with monospecific antiserum prepared against either of these purified enzymes, indicating that organ specificity between these two human collagenases is unlikely.

Alpha-Globulins↗