The inhibition of mouse bone collagenase by lysozyme.

Abstract

Egg white lysozyme, as well as basic proteins such as histone and protamine-free base, were found to inhibit mouse bone collagenase. The inhibition of mouse bone collagenase by lysozyme was detected when the activity of the collagenase was assayed using collagen as the substrate in the solid state, but not when the collagenase activity was assayed using collagen in solution as the substrate. On the other hand, the inhibition of collagenase activity by histone and protamine-free base was observed in both assay systems. The inhibition of mouse bone collagenase by polycationic molecules is interesting in light of previous findings that several polyanionic molecules, such as heparin, dextran sulfate and polyethylenesulphonic acid, enhance the activity of mouse bone collagenase under the same experimental conditions. Since lysozyme is widely distributed in connective tissues and its concentration varies with the rate of tissue remodeling, the inhibition of mouse bone collagenase by lysozyme suggests its possible role in the regulation of collagen degradation during the remodeling of collagenous tissuesin vivo during normal and pathological states.