Biochemical and functional characterization of aminopeptidase N expressed by human melanoma cells.
A cell surface protein expressed on melanoma cells, but not on normal melanocytes, was biochemically and functionally characterized. Microsequencing of the M(r) 143,000 affinity-purified protein revealed amino acid sequence identity to aminopeptidase N (EC 3.4.11.2). In situ expression, indirect immunofluorescence, and Western blotting demonstrated that aminopeptidase N is tightly associated with extracellular matrix components. A specific polyclonal antiserum and the competitive inhibitors of aminopeptidase N, bestatin and amastatin, inhibited invasion of an aminopeptidase N-expressing metastatic melanoma cell line through the reconstituted basement membrane Matrigel in a dose-dependent manner. In vitro digestion of Matrigel with affinity-purified aminopeptidase N revealed an enzyme-sensitive M(r) 160,000 protein. These experiments suggest a role for aminopeptidase N in melanoma invasion of basement membranes.[1]References
- Biochemical and functional characterization of aminopeptidase N expressed by human melanoma cells. Menrad, A., Speicher, D., Wacker, J., Herlyn, M. Cancer Res. (1993) [Pubmed]
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