Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro.

Meprins are astacin-like metalloproteases of renal and intestinal epithelia and embryonic neuroepithelial cells. The full length cDNA of the human meprin alpha subunit has been overexpressed in baculovirus-infected insect cells yielding the tetrameric proprotein which could be proteolytically activated and affinity-purified to homogeneity. Recombinant meprin alpha hydrolyzes the synthetic substrate ...
N-benzoyl-tyrosyl-p-aminobenzoic acid (PABA-peptide) and cleaves by limited proteolysis the basement membrane constituents laminin 1 and laminin 5. This supports a concept that meprin alpha, when basolaterally secreted by human colon carcinoma epithelial cells, increases the proteolytic capacity for tumor progression in the stroma.
Mesh Terms:
Animals, Baculoviridae, Basement Membrane, Cell Line, Chromatography, Affinity, DNA, Complementary, Enzyme Activation, Enzyme Precursors, Gene Expression, Insects, Laminin, Metalloendopeptidases, Transfection
FEBS Lett.
Date: Jan. 07, 2000
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