Advanced

The Different Roles of Aggrecan Interaction Domains

Aspberg, Anders LU (2012) In Journal of Histochemistry and Cytochemistry 60(12). p.987-996
Abstract

The aggregating proteoglycans of the lectican family are important components of extracellular matrices. Aggrecan is the most well studied of these and is central to cartilage biomechanical properties and skeletal development. Key to its biological function is the fixed charge of the many glycosaminoglycan chains, that provide the basis for the viscoelastic properties necessary for load distribution over the articular surface. This review is focused on the globular domains of aggrecan and their role in anchoring the proteoglycans to other extracellular matrix components. The N-terminal G1 domain is vital in that it binds the proteoglycan to hyaluronan in ternary complex with link protein, retaining the proteoglycan in the tissue. The... (More)

The aggregating proteoglycans of the lectican family are important components of extracellular matrices. Aggrecan is the most well studied of these and is central to cartilage biomechanical properties and skeletal development. Key to its biological function is the fixed charge of the many glycosaminoglycan chains, that provide the basis for the viscoelastic properties necessary for load distribution over the articular surface. This review is focused on the globular domains of aggrecan and their role in anchoring the proteoglycans to other extracellular matrix components. The N-terminal G1 domain is vital in that it binds the proteoglycan to hyaluronan in ternary complex with link protein, retaining the proteoglycan in the tissue. The importance of the C-terminal G3 domain interactions has recently been emphasized by two different human hereditary disorders: autosomal recessive aggrecan-type spondyloepimetaphyseal dysplasia and autosomal dominant familial osteochondritis dissecans. In these two conditions, different missense mutations in the aggrecan C-type lectin repeat have been described. The resulting amino acid replacements affect the ligand interactions of the G3 domain, albeit with widely different phenotypic outcomes.

(Less)
Please use this url to cite or link to this publication:
author
publishing date
type
Contribution to journal
publication status
published
keywords
aggrecan, cartilage, chondrodysplasia, extracellular matrix, osteochondritis dissecans, protein interactions
in
Journal of Histochemistry and Cytochemistry
volume
60
issue
12
pages
10 pages
publisher
Histochemical Society
external identifiers
  • scopus:84873030415
ISSN
0022-1554
DOI
10.1369/0022155412464376
language
English
LU publication?
no
id
042bf38f-2667-47fa-b29c-22e824bdd010
date added to LUP
2016-12-06 10:02:04
date last changed
2017-10-01 05:27:05
@article{042bf38f-2667-47fa-b29c-22e824bdd010,
  abstract     = {<p>The aggregating proteoglycans of the lectican family are important components of extracellular matrices. Aggrecan is the most well studied of these and is central to cartilage biomechanical properties and skeletal development. Key to its biological function is the fixed charge of the many glycosaminoglycan chains, that provide the basis for the viscoelastic properties necessary for load distribution over the articular surface. This review is focused on the globular domains of aggrecan and their role in anchoring the proteoglycans to other extracellular matrix components. The N-terminal G1 domain is vital in that it binds the proteoglycan to hyaluronan in ternary complex with link protein, retaining the proteoglycan in the tissue. The importance of the C-terminal G3 domain interactions has recently been emphasized by two different human hereditary disorders: autosomal recessive aggrecan-type spondyloepimetaphyseal dysplasia and autosomal dominant familial osteochondritis dissecans. In these two conditions, different missense mutations in the aggrecan C-type lectin repeat have been described. The resulting amino acid replacements affect the ligand interactions of the G3 domain, albeit with widely different phenotypic outcomes.</p>},
  author       = {Aspberg, Anders},
  issn         = {0022-1554},
  keyword      = {aggrecan,cartilage,chondrodysplasia,extracellular matrix,osteochondritis dissecans,protein interactions},
  language     = {eng},
  number       = {12},
  pages        = {987--996},
  publisher    = {Histochemical Society},
  series       = {Journal of Histochemistry and Cytochemistry},
  title        = {The Different Roles of Aggrecan Interaction Domains},
  url          = {http://dx.doi.org/10.1369/0022155412464376},
  volume       = {60},
  year         = {2012},
}