Literature DB >> 9363632

Collagen IX.

B R Olsen1.   

Abstract

Collagen IX was identified as a distinct component of cartilage about 10 years ago. Composed of three polypeptide chains, its heterotrimeric molecules are located on the surface of type II collagen fibrils in cartilage. The interaction between collagens II and IX is stabilized by covalent crosslinks. The location of collagen IX molecules on fibril surfaces suggests that they represent macromolecular bridges between fibrils and other matrix components in cartilage, and that collagen IX is important for the cohesive and compressive properties of cartilage. Transgenic mice with mutations in a type IX gene develop normally, but show degenerative changes in articular cartilage after birth. Additional evidence for the importance of collagen IX in human articular cartilage comes from the recent finding that a mutation in one of the collagen IX genes causes multiple epiphyseal dysplasia. The mild complaints in affected individuals with the mutation suggest that mutations in type IX collagen genes may represent genetic risk factors for late onset osteoarthritis.

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Year:  1997        PMID: 9363632     DOI: 10.1016/s1357-2725(96)00100-8

Source DB:  PubMed          Journal:  Int J Biochem Cell Biol        ISSN: 1357-2725            Impact factor:   5.085


  25 in total

1.  A mutation in the alpha 3 chain of type IX collagen causes autosomal dominant multiple epiphyseal dysplasia with mild myopathy.

Authors:  C G Bönnemann; G F Cox; F Shapiro; J J Wu; C A Feener; T G Thompson; D C Anthony; D R Eyre; B T Darras; L M Kunkel
Journal:  Proc Natl Acad Sci U S A       Date:  2000-02-01       Impact factor: 11.205

2.  Structural model of the amino propeptide of collagen XI alpha1 chain with similarity to the LNS domains.

Authors:  Arzhang Fallahi; Becky Kroll; Lisa R Warner; Rex J Oxford; Katey M Irwin; Linda M Mercer; Susan E Shadle; Julia Thom Oxford
Journal:  Protein Sci       Date:  2005-06       Impact factor: 6.725

3.  Characterization of an abundant COL9A1 transcript in the cochlea with a novel 3' UTR: Expression studies and detection of miRNA target sequence.

Authors:  Theru A Sivakumaran; Barbara L Resendes; Nahid G Robertson; Anne B S Giersch; Cynthia C Morton
Journal:  J Assoc Res Otolaryngol       Date:  2006-04-19

4.  Structural and functional characterization of recombinant matrilin-3 A-domain and implications for human genetic bone diseases.

Authors:  Maryline Fresquet; Thomas A Jowitt; Joni Ylöstalo; Paul Coffey; Roger S Meadows; Leena Ala-Kokko; David J Thornton; Michael D Briggs
Journal:  J Biol Chem       Date:  2007-09-18       Impact factor: 5.157

5.  An in-solution ultrasonication-assisted digestion method for improved extracellular matrix proteome coverage.

Authors:  Kirk C Hansen; Lauren Kiemele; Ori Maller; Jenean O'Brien; Aarthi Shankar; Jaime Fornetti; Pepper Schedin
Journal:  Mol Cell Proteomics       Date:  2009-04-07       Impact factor: 5.911

Review 6.  Extracellular matrix molecules: potential targets in pharmacotherapy.

Authors:  Hannu Järveläinen; Annele Sainio; Markku Koulu; Thomas N Wight; Risto Penttinen
Journal:  Pharmacol Rev       Date:  2009-06       Impact factor: 25.468

Review 7.  The collagen family.

Authors:  Sylvie Ricard-Blum
Journal:  Cold Spring Harb Perspect Biol       Date:  2011-01-01       Impact factor: 10.005

Review 8.  Cartilage diseases.

Authors:  Yamini Krishnan; Alan J Grodzinsky
Journal:  Matrix Biol       Date:  2018-05-24       Impact factor: 11.583

9.  Lifelong voluntary joint loading increases osteoarthritis in mice housing a deletion mutation in type II procollagen gene, and slightly also in non-transgenic mice.

Authors:  T Lapveteläinen; M M Hyttinen; A-M Säämänen; T Långsjö; J Sahlman; S Felszeghy; E Vuorio; H J Helminen
Journal:  Ann Rheum Dis       Date:  2002-09       Impact factor: 19.103

10.  Multiple epiphyseal dysplasia.

Authors:  Johanna Dahlqvist; Hanna Orlén; Hans Matsson; Niklas Dahl; Torsten Lönnerholm; Karl-Henrik Gustavson
Journal:  Acta Orthop       Date:  2009-12       Impact factor: 3.717

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