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J. Biol. Chem., Vol. 262, Issue 23, 10946-10950, 08, 1987

Internalization of serratial protease into cells as an enzyme-inhibitor complex with alpha 2-macroglobulin and regeneration of protease activity and cytotoxicity

H Maeda, A Molla, T Oda and T Katsuki

Extracellular serratial protease (56,000 Da) is known to be cytotoxic. Fluorescein isothiocyanate-labeled protease was found to form a complex with human alpha 2-macroglobulin (alpha 2M), and this enzyme-inhibitor complex was purified. The protease was found to be internalized by fibroblasts in culture as a complex with alpha 2M, which resulted in cell destruction. Regeneration of enzyme activity was confirmed in cells after 2-3 h of incubation. Chicken egg-white ovomacroglobulin, a homolog of human alpha 2M, formed a complex with this enzyme similarly and more tightly but failed to exhibit protease activity, cytotoxicity, and internalization into cells.
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