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Heterologously overexpressed, affinity‐purified human meprin α is functionally active and cleaves components of the basement membrane in vitro
Author(s) -
Köhler Danny,
Kruse Markus-N.,
Stöcker Walter,
Sterchi Erwin E.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01712-3
Subject(s) - metalloproteinase , basement membrane , laminin , proteolysis , biochemistry , recombinant dna , matrix metalloproteinase , in vitro , microbiology and biotechnology , chemistry , biology , type iv collagen , extracellular matrix , enzyme , gene
Meprins are astacin‐like metalloproteases of renal and intestinal epithelia and embryonic neuroepithelial cells. The full length cDNA of the human meprin α 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 α 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 α, when basolaterally secreted by human colon carcinoma epithelial cells, increases the proteolytic capacity for tumor progression in the stroma.