The role of small leucine-rich proteoglycans in collagen fibrillogenesis
- PMID: 20080181
- DOI: 10.1016/j.matbio.2010.01.001
The role of small leucine-rich proteoglycans in collagen fibrillogenesis
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.
Copyright 2010 International Society of Matrix Biology. Published by Elsevier B.V. All rights reserved.
Similar articles
-
Structural correlations in the family of small leucine-rich repeat proteins and proteoglycans.J Struct Biol. 2006 Aug;155(2):294-305. doi: 10.1016/j.jsb.2006.01.016. Epub 2006 May 19. J Struct Biol. 2006. PMID: 16884925 Review.
-
Fibrillogenesis of collagen types I, II, and III with small leucine-rich proteoglycans decorin and biglycan.Biomacromolecules. 2006 Aug;7(8):2388-93. doi: 10.1021/bm0603746. Biomacromolecules. 2006. PMID: 16903686
-
Phenotypic effects of biglycan deficiency are linked to collagen fibril abnormalities, are synergized by decorin deficiency, and mimic Ehlers-Danlos-like changes in bone and other connective tissues.J Bone Miner Res. 2002 Jul;17(7):1180-9. doi: 10.1359/jbmr.2002.17.7.1180. J Bone Miner Res. 2002. PMID: 12102052
-
[Proteoglycan knock-out mice and osteoarthritis].Clin Calcium. 2004 Jul;14(7):58-63. Clin Calcium. 2004. PMID: 15577077 Review. Japanese.
-
Development of tendon structure and function: regulation of collagen fibrillogenesis.J Musculoskelet Neuronal Interact. 2005 Mar;5(1):5-21. J Musculoskelet Neuronal Interact. 2005. PMID: 15788867 Review.
Cited by
-
Mesenchymal condensation-dependent accumulation of collagen VI stabilizes organ-specific cell fates during embryonic tooth formation.Dev Dyn. 2015 Jun;244(6):713-23. doi: 10.1002/dvdy.24264. Epub 2015 Apr 24. Dev Dyn. 2015. PMID: 25715693 Free PMC article.
-
Distinguishing tendon and ligament fibroblasts based on 1H nuclear magnetic resonance spectroscopy.Tissue Eng Regen Med. 2016 Dec 17;13(6):677-683. doi: 10.1007/s13770-016-0128-5. eCollection 2016 Dec. Tissue Eng Regen Med. 2016. PMID: 30603448 Free PMC article.
-
Comprehensive quantitative characterization of the human term amnion proteome.Matrix Biol Plus. 2021 Sep 21;12:100084. doi: 10.1016/j.mbplus.2021.100084. eCollection 2021 Dec. Matrix Biol Plus. 2021. PMID: 34765964 Free PMC article.
-
Dermatopontin in Skeletal Muscle Extracellular Matrix Regulates Myogenesis.Cells. 2019 Apr 9;8(4):332. doi: 10.3390/cells8040332. Cells. 2019. PMID: 30970625 Free PMC article.
-
The extracellular matrix proteoglycan lumican improves survival and counteracts cardiac dilatation and failure in mice subjected to pressure overload.Sci Rep. 2019 Jun 24;9(1):9206. doi: 10.1038/s41598-019-45651-9. Sci Rep. 2019. PMID: 31235849 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases