Matrix metalloproteinase matrilysin is constitutively expressed in adult human exocrine epithelium.

The proteolytic activity of matrix metalloproteinases is involved in normal and disease-related remodeling processes. One member of this family, matrilysin, can degrade a wide spectrum of connective tissue proteins, suggesting that this enzyme is involved in numerous and diverse biologic processes. In fact, recent studies have shown that matrilysin is expressed in developing hair follicles and glands. Using in situ hybridization and immunohistochemistry, we examined the sites of matrilysin expression in normal and diseased adult skin. In normal mature skin, matrilysin mRNA and protein was strongly and consistently expressed in ductal cells and in some secretory cells of all eccrine and apocrine glands and was not found in any other cell type. A similar tissue distribution was also found in numerous benign inflammatory skin lesions, and prominent expression of matrilysin mRNA and protein was also found in glandular disorders such as axillary hidradenitis and sweat gland tumors. These findings indicate that matrilysin is a constitutive product of the epithelium of dermal glands and that its expression may not be related to a disease-specific or remodeling process. Because of its extensive expression in dermal glands, we assessed whether matrilysin might be produced by all exocrine glands. Indeed, we detected matrilysin mRNA and immunoreactive protein in the ductal and glandular epithelium of mammary and parotid glands, pancreas, liver, prostate, and the serous acini of peribronchial glands of the lung. Thus, our findings indicate that matrilysin is constitutively produced by exocrine epithelial cells throughout the body. Because of its broad catalytic activity, we speculate matrilysin may participate in the normal function of exocrine glands by preventing glandular obstruction.