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Cartilage oligomeric matrix protein-deficient mice have normal skeletal development.

Svensson, Liz; Aszodi, Attila LU ; Heinegård, Dick LU ; Hunziker, Ernst B; Reinholt, Finn P; Fässler, Reinhard and Oldberg, Åke LU (2002) In Molecular and Cellular Biology 22(12). p.4366-4371
Abstract
Cartilage oligomeric matrix protein (COMP) belongs to the thrombospondin family and is a homopentamer primarily expressed in cartilage. Mutations in the COMP gene result in the autosomal dominant chondrodysplasias pseudoachondroplasia (PSACH) and some types of multiple epiphyseal dysplasia (MED), which are characterized by mild to severe short-limb dwarfism and early-onset osteoarthritis. We have generated COMP-null mice to study the role of COMP in vivo. These mice show no anatomical, histological, or ultrastructural abnormalities and show none of the clinical signs of PSACH or MED. Northern blot analysis and immunohistochemical analysis of cartilage indicate that the lack of COMP is not compensated for by any other member of the... (More)
Cartilage oligomeric matrix protein (COMP) belongs to the thrombospondin family and is a homopentamer primarily expressed in cartilage. Mutations in the COMP gene result in the autosomal dominant chondrodysplasias pseudoachondroplasia (PSACH) and some types of multiple epiphyseal dysplasia (MED), which are characterized by mild to severe short-limb dwarfism and early-onset osteoarthritis. We have generated COMP-null mice to study the role of COMP in vivo. These mice show no anatomical, histological, or ultrastructural abnormalities and show none of the clinical signs of PSACH or MED. Northern blot analysis and immunohistochemical analysis of cartilage indicate that the lack of COMP is not compensated for by any other member of the thrombospondin family. The results also show that the phenotype in PSACH/MED cartilage disorders is not caused by the reduced amount of COMP. (Less)
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keywords
Extracellular Matrix Proteins : metabolism, Glycoproteins : deficiency, Female, Glycoproteins : genetics, Glycoproteins : metabolism, Male, Mice, Inbred Strains, Mutant Strains, Reference Values, Skeleton, Reverse Transcriptase Polymerase Chain Reaction, Support, Non-U.S. Gov't, Tibia : growth & development, Tibia : anatomy & histology, Extracellular Matrix Proteins : genetics, Extracellular Matrix Proteins : deficiency, Cartilage : ultrastructure, Cartilage : growth & development, Cartilage : anatomy & histology, Animal
in
Molecular and Cellular Biology
volume
22
issue
12
pages
4366 - 4371
publisher
American Society for Microbiology
external identifiers
  • wos:000175866400037
  • pmid:12024046
  • scopus:0036264997
ISSN
0270-7306
DOI
10.1128/MCB.22.12.4366-4371.2002
language
English
LU publication?
yes
id
5b4a5259-e6ed-4a7b-a565-3e9ec3140b57 (old id 108431)
alternative location
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12024046&dopt=Abstract
http://mcb.asm.org/cgi/content/full/22/12/4366?view=full&pmid=12024046
date added to LUP
2007-07-19 15:26:52
date last changed
2017-10-29 03:30:15
@article{5b4a5259-e6ed-4a7b-a565-3e9ec3140b57,
  abstract     = {Cartilage oligomeric matrix protein (COMP) belongs to the thrombospondin family and is a homopentamer primarily expressed in cartilage. Mutations in the COMP gene result in the autosomal dominant chondrodysplasias pseudoachondroplasia (PSACH) and some types of multiple epiphyseal dysplasia (MED), which are characterized by mild to severe short-limb dwarfism and early-onset osteoarthritis. We have generated COMP-null mice to study the role of COMP in vivo. These mice show no anatomical, histological, or ultrastructural abnormalities and show none of the clinical signs of PSACH or MED. Northern blot analysis and immunohistochemical analysis of cartilage indicate that the lack of COMP is not compensated for by any other member of the thrombospondin family. The results also show that the phenotype in PSACH/MED cartilage disorders is not caused by the reduced amount of COMP.},
  author       = {Svensson, Liz and Aszodi, Attila and Heinegård, Dick and Hunziker, Ernst B and Reinholt, Finn P and Fässler, Reinhard and Oldberg, Åke},
  issn         = {0270-7306},
  keyword      = {Extracellular Matrix Proteins : metabolism,Glycoproteins : deficiency,Female,Glycoproteins : genetics,Glycoproteins : metabolism,Male,Mice,Inbred Strains,Mutant Strains,Reference Values,Skeleton,Reverse Transcriptase Polymerase Chain Reaction,Support,Non-U.S. Gov't,Tibia : growth & development,Tibia : anatomy & histology,Extracellular Matrix Proteins : genetics,Extracellular Matrix Proteins : deficiency,Cartilage : ultrastructure,Cartilage : growth & development,Cartilage : anatomy & histology,Animal},
  language     = {eng},
  number       = {12},
  pages        = {4366--4371},
  publisher    = {American Society for Microbiology},
  series       = {Molecular and Cellular Biology},
  title        = {Cartilage oligomeric matrix protein-deficient mice have normal skeletal development.},
  url          = {http://dx.doi.org/10.1128/MCB.22.12.4366-4371.2002},
  volume       = {22},
  year         = {2002},
}