ABSTRACT
This chapter examines what is known about the chemical and enzymatic properties of mammalian collagenases and their synthesis, secretion, activation, and inhibition. Collagenases are widely distributed in mammalian tissues. One basic dogma of mammalian collagenases states that the majority of collagen degradation in the extracellular matrix occurs through the action of these specific neutral pH metalloendoproteases. The human fibroblast collagenase is the most thoroughly described and will be used as a prototypic model of mammalian collagenases. The characteristic doublet of mammalian collagenases appears to arise from posttranslational glycosylation. Mammalian collagenases are clearly a family of metalloendoproteases with pH optima between seven and eight. It has appeared that a convenient way of classifying the mammalian collagenases lies in their respective substrate specificities. The extraordinary temperature dependence of mammalian collagenase was evident in the data of Harris and McCroskery and definitively quantitated by Welgus and Jeffrey.
