Fibromodulin binds collagen type I via Glu-353 and Lys-355 in leucine-rich repeat 11
(2007) In Journal of Biological Chemistry 282(37). p.26740-26745- Abstract
- Fibromodulin belongs to the small leucine-rich repeat proteoglycan family, interacts with collagen type I, and controls collagen fibrillogenesis and assembly. Here, we show that a major fibromodulin-binding site for collagen type I is located in leucine-rich repeat 11 in the C terminus of the leucine-rich repeat domain. We identified Glu-353 and Lys-355 in repeat 11 as essential for binding, and the synthetic peptide RLDGNEIKR, including Glu-353 and Lys-355, inhibits the binding of fibromodulin to collagen in vitro. Fibromodulin and lumican compete for the same binding region on collagen, and fibromodulin can inhibit the binding of lumican to collagen type I. However, the peptide RLDGNEIKR does not inhibit the binding of lumican to... (More)
- Fibromodulin belongs to the small leucine-rich repeat proteoglycan family, interacts with collagen type I, and controls collagen fibrillogenesis and assembly. Here, we show that a major fibromodulin-binding site for collagen type I is located in leucine-rich repeat 11 in the C terminus of the leucine-rich repeat domain. We identified Glu-353 and Lys-355 in repeat 11 as essential for binding, and the synthetic peptide RLDGNEIKR, including Glu-353 and Lys-355, inhibits the binding of fibromodulin to collagen in vitro. Fibromodulin and lumican compete for the same binding region on collagen, and fibromodulin can inhibit the binding of lumican to collagen type I. However, the peptide RLDGNEIKR does not inhibit the binding of lumican to collagen, suggesting separate but closely situated fibromodulin- and lumican-binding sites in collagen. The collagen-binding Glu-353 and Lys-355 residues in fibromodulin are exposed on the exterior of the beta-sheet-loop structure of the leucine-rich repeat, which resembles the location of interacting residues in other leucine-rich repeat proteins, e. g. decorin. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/657284
- author
- Kalamajski, Sebastian LU and Oldberg, Åke LU
- organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Fibromodulin, collagen, Glu353, repeat 11, Lys355, type I, leucine-rich
- in
- Journal of Biological Chemistry
- volume
- 282
- issue
- 37
- pages
- 26740 - 26745
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- wos:000249304900012
- scopus:34848851981
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M704026200
- language
- English
- LU publication?
- yes
- id
- 5ef78189-ec01-47e8-9d1b-6801154bb647 (old id 657284)
- alternative location
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=17623650&dopt=Abstract
- date added to LUP
- 2016-04-01 11:40:57
- date last changed
- 2022-04-28 18:22:37
@article{5ef78189-ec01-47e8-9d1b-6801154bb647,
abstract = {{Fibromodulin belongs to the small leucine-rich repeat proteoglycan family, interacts with collagen type I, and controls collagen fibrillogenesis and assembly. Here, we show that a major fibromodulin-binding site for collagen type I is located in leucine-rich repeat 11 in the C terminus of the leucine-rich repeat domain. We identified Glu-353 and Lys-355 in repeat 11 as essential for binding, and the synthetic peptide RLDGNEIKR, including Glu-353 and Lys-355, inhibits the binding of fibromodulin to collagen in vitro. Fibromodulin and lumican compete for the same binding region on collagen, and fibromodulin can inhibit the binding of lumican to collagen type I. However, the peptide RLDGNEIKR does not inhibit the binding of lumican to collagen, suggesting separate but closely situated fibromodulin- and lumican-binding sites in collagen. The collagen-binding Glu-353 and Lys-355 residues in fibromodulin are exposed on the exterior of the beta-sheet-loop structure of the leucine-rich repeat, which resembles the location of interacting residues in other leucine-rich repeat proteins, e. g. decorin.}},
author = {{Kalamajski, Sebastian and Oldberg, Åke}},
issn = {{1083-351X}},
keywords = {{Fibromodulin; collagen; Glu353; repeat 11; Lys355; type I; leucine-rich}},
language = {{eng}},
number = {{37}},
pages = {{26740--26745}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{Fibromodulin binds collagen type I via Glu-353 and Lys-355 in leucine-rich repeat 11}},
url = {{http://dx.doi.org/10.1074/jbc.M704026200}},
doi = {{10.1074/jbc.M704026200}},
volume = {{282}},
year = {{2007}},
}