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Immunohistochemical localization of lysyl oxidase with monoclonal antibodies.

Lysyl oxidase initiates the cross-linking of collagen and elastin by catalyzing the formation of the lysine-derived aldehyde. We cloned three hybridoma cell lines which secrete monoclonal antibodies to human lysyl oxidase. The localization of lysyl oxidase was investigated in various tissues and in cultured cells using an immunofluorescent antibody method. Antibodies showed a strong immunostaining in the aorta and dermal connective tissue suggesting a close relation to elastin and collagen. Fibroblasts, chondrocytes, and smooth muscle cells also yielded a marked positive immunoreaction as did a variety of nonfibroblastic cells such as endothelial cells, basal cells, biliary epithelial cells, and glomerular epithelial cells. In cultured cells, including human fibroblasts, an intense immunoreaction manifested as fine, filamentous structures in the cytoplasm. It is suggested that lysyl oxidase is associated with cytoskeletal protein.