title: Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro.
abstract: 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.
authors.affiliation: Institute of Zoophysiology, Hindenburgplatz 55, University of M]unster, D-48143, M]unster, Germany.
authors.forename: D
authors.initials: D
authors.lastname: Köhler
authors.forename: M
authors.initials: M
authors.lastname: Kruse
authors.forename: W
authors.initials: W
authors.lastname: Stöcker
authors.forename: E E
authors.initials: EE
authors.lastname: Sterchi
mesh_terms: D000818:Animals; D016367:Baculoviridae / Q000235:genetics; D001485:Basement Membrane / Q000378:metabolism; D002460:Cell Line; D002846:Chromatography, Affinity; D018076:DNA, Complementary / Q000302:isolation & purification; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism; D015870:Gene Expression; D007313:Insecta; D007797:Laminin / Q000378:metabolism; D008666:Metalloendopeptidases / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism; D014162:Transfection
chemical_list: D018076:DNA, Complementary; D004792:Enzyme Precursors; D007797:Laminin; C121346:laminin 1; D008666:Metalloendopeptidases; C053833:meprin A