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Hemopexin domains as multifunctional liganding modules in matrix metalloproteinases and other proteins
Author(s) -
Piccard Helene,
Van den Steen Philippe E.,
Opdenakker Ghislain
Publication year - 2007
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1189/jlb.1006629
Subject(s) - hemopexin , matrix metalloproteinase , biology , matrix (chemical analysis) , microbiology and biotechnology , biochemistry , computational biology , enzyme , chemistry , chromatography , heme
The heme‐binding hemopexin consists of two, four‐bladed propeller domains connected by a linker region. Hemopexin domains are found in different species on the phylogenetic tree and in the human species represented in hemopexin, matrix metalloproteinases (MMPs), vitronectin, and products of the proteoglycan 4 gene. Hemopexin and hemopexin domains of human proteins fulfill functions in activation of MMPs, inhibition of MMPs, dimerization, binding of substrates or ligands, cleavage of substrates, and endocytosis by low‐density lipoprotein receptor‐related protein‐1 (LRP‐1; CD91) and LRP‐2 (megalin, GP330). Insights into the structures and functions of hemopexin (domains) form the basis for positive or negative interference with the formation of molecular complexes and hence, might be exploited therapeutically in inflammation, cancer, and wound healing.