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J. Biol. Chem., Vol. 277, Issue 17, 15061-15068, April 26, 2002
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From the PRELP (proline arginine-rich end
leucine-rich repeat protein) 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.
The Leucine-rich Repeat Protein PRELP Binds Perlecan and
Collagens and May Function as a Basement Membrane Anchor*
§,,
, and
Department of Cell and Molecular Biology,
Section for Connective Tissue Biology, Lund University, SE-221 84 Lund, Sweden and the ¶ Max-Planck-Institute for Biochemistry,
D-82152 Martinsried, Germany
*
This work was supported by the Medical Faculty, Lund
University, the Swedish Medical Research Council,
Reumatikerförbundet, Greta och Johan Kock's Stiftelser, Konung
Gustaf V:s 80-års fond, Alfred Österlunds Stiftelse, and
Deutsche Forschungsgemeinschaft (Project Ti9518-1).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Cell and
Molecular Biology, Section for Connective Tissue Biology, Lund University, BMC, C12, SE-211 84 Lund, Sweden. Tel.: 46-46-2228571; Fax:
46-46-2113417; E-mail: dick.heinegard@medkem.lu.se.
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