Journal of Leukocyte Biology
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Originally published online as doi:10.1189/jlb.1006629 on December 21, 2006

Published online before print December 21, 2006
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(Journal of Leukocyte Biology. 2007;81:870-892.)
© 2007 by Society for Leukocyte Biology

Hemopexin domains as multifunctional liganding modules in matrix metalloproteinases and other proteins

Helene Piccard, Philippe E. Van den Steen and Ghislain Opdenakker1

Rega Institute for Medical Research, Laboratory of Immunobiology, University of Leuven, Leuven, Belgium

1 Correspondence: Rega Institute for Medical Research, Laboratory of Immunobiology, University of Leuven, Minderbroedersstraat 10, 3000 Leuven, Belgium. E-mail: ghislain.opdenakker{at}rega.kuleuven.be

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.

Key Words: vitronectin • endocytosis • heme metabolism • chemokine • collagenolysis • pericellular proteolysis






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