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Glycoconjugate Journal

, Volume 19, Issue 4–5, pp 269–273 | Cite as

Chondrodysplasia of gene knockout mice for aggrecan and link protein

Article

Abstract

The proteoglycan aggregate of the cartilage is composed of aggrecan, link protein, and hyaluronan and forms a unique gel-like moiety that provides resistance to compression in joints and a foundational cartilage structure critical for growth plate formation. Aggrecan, a large chondroitin sulfate proteoglycan, is one of the major structural macromolecules in cartilage and binds both hyaluronan and link protein through its N-terminal domain G1. Link protein, a small glycoprotein, is homologous to the G1 domain of aggrecan. Mouse cartilage matrix deficiency (cmd) is caused by a functional null mutation of the aggrecan gene and is characterized by perinatal lethal dwarfism and craniofacial abnormalities. Link protein knockout mice show chondrodysplasia similar to but milder than cmd mice, suggesting a supporting role of link protein for the aggregate structure. Analysis of these mice revealed that the proteoglycan aggregate plays an important role in cartilage development and maintenance of cartilage tissue and may provide a clue to the identification of human genetic disorders caused by mutations in these genes. Published in 2003.

aggrecan proteoglycan link protein gene defects knockout mouse 

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Copyright information

© Kluwer Academic Publishers 2002

Authors and Affiliations

  1. 1.Institute for Molecular Science of MedicineAichi Medical UniversityAichiJapan
  2. 2.Developmental Biology and Regeneration BranchNational Institute of Dental and Craniofacial Research, National Institutes of HealthBethesdaUSA

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