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The leucine-rich repeat protein PRELP binds fibroblast cell surface proteoglycans and enhances focal adhesion formation.

Bengtsson, Eva LU ; Lindblom, Karin LU ; Tillgren, Viveka LU and Aspberg, Anders LU (2016) In The Biochemical journal 473(9). p.1153-1164
Abstract
PRELP is a member of the leucine-rich repeat family of extracellular matrix proteins in connective tissue. In contrast to other members of the family, the amino-terminal domain of PRELP has a high content of proline and positively charged amino acids. This domain has previously been shown to bind chondrocytes and to inhibit osteoclast differentiation. Here we show that PRELP mediates cell adhesion by binding to cell surface glycosaminoglycans. Thus, rat skin fibroblasts bound to full-length PRELP and to the amino-terminal part of PRELP alone, but not to truncated PRELP lacking the positively charged amino-terminal region. Cell attachment to PRELP was inhibited by addition of soluble heparin or heparan sulfate, by blocking sulfation of the... (More)
PRELP is a member of the leucine-rich repeat family of extracellular matrix proteins in connective tissue. In contrast to other members of the family, the amino-terminal domain of PRELP has a high content of proline and positively charged amino acids. This domain has previously been shown to bind chondrocytes and to inhibit osteoclast differentiation. Here we show that PRELP mediates cell adhesion by binding to cell surface glycosaminoglycans. Thus, rat skin fibroblasts bound to full-length PRELP and to the amino-terminal part of PRELP alone, but not to truncated PRELP lacking the positively charged amino-terminal region. Cell attachment to PRELP was inhibited by addition of soluble heparin or heparan sulfate, by blocking sulfation of the fibroblasts, or by treating the cells with a combination of chondroitinase and heparinase. Using affinity chromatography, we identified syndecan-1, syndecan-4 and glypican-1 as cell surface proteoglycans binding to the amino-terminal part of PRELP. Finally, we show that the amino-terminal domain of PRELP in combination with the integrin-binding domain of fibronectin, but neither of the fragments alone, induced fibroblast focal adhesion formation. These findings provide support for a role of the amino-terminal region of PRELP as an important regulator of cell adhesion and behavior, which may be of importance in pathological conditions. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
The Biochemical journal
volume
473
issue
9
pages
1153 - 1164
publisher
Portland Press
external identifiers
  • PMID:26920026
  • Scopus:84975167004
ISSN
1470-8728
DOI
10.1042/BCJ20160095
language
English
LU publication?
yes
id
80490bab-2b2d-4019-9643-012b8642d725 (old id 8821500)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/26920026?dopt=Abstract
date added to LUP
2016-03-04 09:11:26
date last changed
2016-10-13 04:29:36
@misc{80490bab-2b2d-4019-9643-012b8642d725,
  abstract     = {PRELP is a member of the leucine-rich repeat family of extracellular matrix proteins in connective tissue. In contrast to other members of the family, the amino-terminal domain of PRELP has a high content of proline and positively charged amino acids. This domain has previously been shown to bind chondrocytes and to inhibit osteoclast differentiation. Here we show that PRELP mediates cell adhesion by binding to cell surface glycosaminoglycans. Thus, rat skin fibroblasts bound to full-length PRELP and to the amino-terminal part of PRELP alone, but not to truncated PRELP lacking the positively charged amino-terminal region. Cell attachment to PRELP was inhibited by addition of soluble heparin or heparan sulfate, by blocking sulfation of the fibroblasts, or by treating the cells with a combination of chondroitinase and heparinase. Using affinity chromatography, we identified syndecan-1, syndecan-4 and glypican-1 as cell surface proteoglycans binding to the amino-terminal part of PRELP. Finally, we show that the amino-terminal domain of PRELP in combination with the integrin-binding domain of fibronectin, but neither of the fragments alone, induced fibroblast focal adhesion formation. These findings provide support for a role of the amino-terminal region of PRELP as an important regulator of cell adhesion and behavior, which may be of importance in pathological conditions.},
  author       = {Bengtsson, Eva and Lindblom, Karin and Tillgren, Viveka and Aspberg, Anders},
  issn         = {1470-8728},
  language     = {eng},
  month        = {02},
  number       = {9},
  pages        = {1153--1164},
  publisher    = {ARRAY(0x8a409b0)},
  series       = {The Biochemical journal},
  title        = {The leucine-rich repeat protein PRELP binds fibroblast cell surface proteoglycans and enhances focal adhesion formation.},
  url          = {http://dx.doi.org/10.1042/BCJ20160095},
  volume       = {473},
  year         = {2016},
}