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M108285200v1
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Papers In Press, published online ahead of print February 14, 2002
J. Biol. Chem, 10.1074/jbc.M108285200
Submitted on August 28, 2001
Revised on February 13, 2002
Accepted on February 14, 2002

The leucine-rich repeat protein PRELP binds perlecan and collagens and may function as a basement anchor

Eva Bengtsson, Matthias Mörgelin, Takako Sasaki, Rupert Timpl, Dick Heinegård, and Anders Aspberg

Department of Cell & Molecular Biology, University of Lund, SE-221 84 Lund

Corresponding Author: dick.heinegard{at}medkem.lu.se

PRELP is a heparin-binding leucine-rich repeat protein in connective tissue extracellular matrix. In search of natural ligands and biological functions of this molecule, we found that PRELP binds the basement membrane heparan sulfate proteoglycan perlecan. Also recombinant perlecan domains I and V carrying heparan sulfate bound PRELP, whereas other domains without glycosaminoglycan substitution did not. Heparin, but not chondroitin sulfate, inhibited the interactions. Glycosaminoglycan-free recombinant perlecan domain V and mutated domain I did not bind PRELP. The dissociation constants of the PRELP-perlecan interactions were in the range of 3-18 nM as determined by surface plasmon resonance. As expected, truncated PRELP, without the heparin-binding domain, did not bind perlecan. Confocal immunohistochemistry showed that PRELP outlines basement membranes with a location adjacent to perlecan. We also found that PRELP binds collagen type I and type II through its leucine-rich repeat domain. Electron microscopy visualized a complex with PRELP binding simultaneously to the triple helical region of procollagen I and the heparan sulfate chains of perlecan. Based on the location of PRELP and its interaction with perlecan heparan sulfate chains and collagen, we propose a function of PRELP as a molecule anchoring basement membranes to the underlying connective tissue.


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