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The amino-terminal part of PRELP binds to heparin and heparan sulfate

Bengtsson, Eva; Aspberg, Anders LU ; Heinegård, Dick LU ; Sommarin, Y and Spillmann, D (2000) In Journal of Biological Chemistry 275(52). p.40695-40702
Abstract
PRELP (proline, arginine-rich end leucine-rich repeat protein) is an extracellular matrix leucine-rich repeat protein. The amino-terminal region of PRELP differs from that of other leucine-rich repeat proteins in containing a high number of proline and arginine residues. The clustered proline and basic residues are conserved in rat, bovine, and human PRELP. Although the function of PRELP is not yet known, the clustered arginine residues suggest a heparan sulfate/heparin-binding capacity. We show here that PRELP indeed binds heparin and heparan sulfate. Truncated PRELP without the amino-terminal region does not bind heparin. The dissociation constant for the interaction of PRELP with heparin was determined by an in solution binding assay... (More)
PRELP (proline, arginine-rich end leucine-rich repeat protein) is an extracellular matrix leucine-rich repeat protein. The amino-terminal region of PRELP differs from that of other leucine-rich repeat proteins in containing a high number of proline and arginine residues. The clustered proline and basic residues are conserved in rat, bovine, and human PRELP. Although the function of PRELP is not yet known, the clustered arginine residues suggest a heparan sulfate/heparin-binding capacity. We show here that PRELP indeed binds heparin and heparan sulfate. Truncated PRELP without the amino-terminal region does not bind heparin. The dissociation constant for the interaction of PRELP with heparin was determined by an in solution binding assay and by surface plasmon resonance analysis to be in the range of 10-30 nm. A 6-mer heparin oligosaccharide was the smallest size showing binding to PRELP. The binding increased with increasing length up to an 18-mer and depended on the degree of sulfation of heparin as well as heparan sulfate. Sulfate groups at all positions were shown to be of importance for the binding. Fibroblasts bind PRELP, and this interaction is inhibited with heparin, suggesting a function for PRELP as a linker between the matrix and cell surface proteoglycans. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
275
issue
52
pages
40695 - 40702
publisher
ASBMB
external identifiers
  • pmid:11007795
  • scopus:0034731438
ISSN
1083-351X
DOI
10.1074/jbc.M007917200
language
English
LU publication?
yes
id
f2a912cc-7459-49dd-a4e8-d844e3969352 (old id 1118185)
date added to LUP
2008-06-18 12:48:03
date last changed
2017-01-01 05:07:33
@article{f2a912cc-7459-49dd-a4e8-d844e3969352,
  abstract     = {PRELP (proline, arginine-rich end leucine-rich repeat protein) is an extracellular matrix leucine-rich repeat protein. The amino-terminal region of PRELP differs from that of other leucine-rich repeat proteins in containing a high number of proline and arginine residues. The clustered proline and basic residues are conserved in rat, bovine, and human PRELP. Although the function of PRELP is not yet known, the clustered arginine residues suggest a heparan sulfate/heparin-binding capacity. We show here that PRELP indeed binds heparin and heparan sulfate. Truncated PRELP without the amino-terminal region does not bind heparin. The dissociation constant for the interaction of PRELP with heparin was determined by an in solution binding assay and by surface plasmon resonance analysis to be in the range of 10-30 nm. A 6-mer heparin oligosaccharide was the smallest size showing binding to PRELP. The binding increased with increasing length up to an 18-mer and depended on the degree of sulfation of heparin as well as heparan sulfate. Sulfate groups at all positions were shown to be of importance for the binding. Fibroblasts bind PRELP, and this interaction is inhibited with heparin, suggesting a function for PRELP as a linker between the matrix and cell surface proteoglycans.},
  author       = {Bengtsson, Eva and Aspberg, Anders and Heinegård, Dick and Sommarin, Y and Spillmann, D},
  issn         = {1083-351X},
  language     = {eng},
  number       = {52},
  pages        = {40695--40702},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {The amino-terminal part of PRELP binds to heparin and heparan sulfate},
  url          = {http://dx.doi.org/10.1074/jbc.M007917200},
  volume       = {275},
  year         = {2000},
}