Cartilage oligomeric matrix protein-deficient mice have normal skeletal development.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/108431
- author
- Svensson, Liz ; Aszodi, Attila LU ; Heinegård, Dick LU ; Hunziker, Ernst B ; Reinholt, Finn P ; Fässler, Reinhard and Oldberg, Åke LU
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- 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
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Experimental Pathology (013031100), Cell and Matrix Biology (LUR000002), Åke Oldberg´s group (013212049), Pathology, (Lund) (013030000), Connective Tissue Biology (013230151)
- 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
- 2016-04-01 11:52:00
- date last changed
- 2022-03-20 20:01:01
@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}}, 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}}, 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 = {{https://lup.lub.lu.se/search/files/2678013/623613.pdf}}, doi = {{10.1128/MCB.22.12.4366-4371.2002}}, volume = {{22}}, year = {{2002}}, }