The role of small leucine-rich proteoglycans in collagen fibrillogenesis.
(2010) In Matrix Biology 29. p.248-253- Abstract
- Small leucine-rich proteoglycans/proteins (SLRPs) are associated with collagen fibril formation, and therefore important for the proper formation of extracellular matrices. SLRPs are differentially expressed in tissues and during pathological conditions, contributing to the development of connective tissue properties. The binding of SLRPs to collagens have recently been characterized, and may give some clues to the significance of these interactions. In this mini review, we summarize published work in this field, and propose several mechanisms for how SLRPs can control collagen matrix structure and function. SLRPs appear to influence collagen cross-linking patterns. We also propose that the SLRP-collagen interactions can assist in the... (More)
- Small leucine-rich proteoglycans/proteins (SLRPs) are associated with collagen fibril formation, and therefore important for the proper formation of extracellular matrices. SLRPs are differentially expressed in tissues and during pathological conditions, contributing to the development of connective tissue properties. The binding of SLRPs to collagens have recently been characterized, and may give some clues to the significance of these interactions. In this mini review, we summarize published work in this field, and propose several mechanisms for how SLRPs can control collagen matrix structure and function. SLRPs appear to influence collagen cross-linking patterns. We also propose that the SLRP-collagen interactions can assist in the process of juxtaposing the collagen monomers by steric hindrance or by directly connecting two collagen monomers during the fibril growth. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1541012
- author
- Kalamajski, Sebastian LU and Oldberg, Åke LU
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Matrix Biology
- volume
- 29
- pages
- 248 - 253
- publisher
- Elsevier
- external identifiers
-
- wos:000278307100002
- pmid:20080181
- scopus:77952550108
- pmid:20080181
- ISSN
- 1569-1802
- DOI
- 10.1016/j.matbio.2010.01.001
- language
- English
- LU publication?
- yes
- id
- efc21ecf-658d-4008-be2b-0e18368dac6c (old id 1541012)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/20080181?dopt=Abstract
- date added to LUP
- 2016-04-04 09:26:33
- date last changed
- 2022-04-23 20:34:32
@article{efc21ecf-658d-4008-be2b-0e18368dac6c,
abstract = {{Small leucine-rich proteoglycans/proteins (SLRPs) are associated with collagen fibril formation, and therefore important for the proper formation of extracellular matrices. SLRPs are differentially expressed in tissues and during pathological conditions, contributing to the development of connective tissue properties. The binding of SLRPs to collagens have recently been characterized, and may give some clues to the significance of these interactions. In this mini review, we summarize published work in this field, and propose several mechanisms for how SLRPs can control collagen matrix structure and function. SLRPs appear to influence collagen cross-linking patterns. We also propose that the SLRP-collagen interactions can assist in the process of juxtaposing the collagen monomers by steric hindrance or by directly connecting two collagen monomers during the fibril growth.}},
author = {{Kalamajski, Sebastian and Oldberg, Åke}},
issn = {{1569-1802}},
language = {{eng}},
pages = {{248--253}},
publisher = {{Elsevier}},
series = {{Matrix Biology}},
title = {{The role of small leucine-rich proteoglycans in collagen fibrillogenesis.}},
url = {{http://dx.doi.org/10.1016/j.matbio.2010.01.001}},
doi = {{10.1016/j.matbio.2010.01.001}},
volume = {{29}},
year = {{2010}},
}