Heterologously overexpressed, affinity-purified human meprin α is functionally active and cleaves components of the basement membrane in vitro
Heterologously overexpressed, affinity-purified human meprin α is functionally active and cleaves components of the basement membrane in vitro
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DOI：
10.1016/s0014-5793(99)01712-3
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发表时间：
2000-01-07
期刊：
影响因子：
3.5
通讯作者：
Sterchi, EE
中科院分区：
文献类型：
--
作者：
Köhler, D;Kruse, MN;Sterchi, EE
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 a hydrolyzes the synthetic substrate N-benzoyl-tyrosyl-p-amino-benzoic 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. (C) 2000 Federation of European Biochemical Societies.
