Heterologously overexpressed, affinity‐purified human meprin α is functionally active and cleaves components of the basement membrane in vitro

FEBS Letters

Stöcker, Walter¹  Sterchi, Erwin E.²  Köhler, Danny¹  Kruse, Markus-N.¹ 

[1] Institute of Zoophysiology, Hindenburgplatz 55, University of Münster, D-48143 Münster, Germany;Institute of Biochemistry and Molecular Biology, Bühlstrasse 28, University of Berne, CH-3012 Berne, Switzerland

关键词: Meprin;    Astacin family;    Expression;    Laminin cleavage;    Baculovirus;    EGF;    epidermal growth factor;    MAM;    meprin;    A5 protein;    receptor protein-tyrosine phosphatase μ;    MATH;    meprin and TRAF homology;    PAA;    polyacrylamide;    PABA-peptide;    N-benzoyl-tyrosyl-p-aminobenzoic acid;    PBS;    phosphate-buffered saline;    SF;    Spodoptera frugiperda;   

DOI  :  10.1016/S0014-5793(99)01712-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown