Osteoadherin

Osteoadherin

Data
Mol mass: 85 kDa pI:
Mol weight (Human): Residues:
Isolation: Wendel et al (1998)
Sequence: Sommarin et al (1998)
Chromosome location: 9q
Swiss Protein Database OMIM Knockout PUBMED
Other LRR members: Asporin Decorin Biglycan PRELP Chondroadherin Fibromodulin Lumican Epiphycan Opticin
Osteoadherin Structure
Persons involved: Ahnders Franzen, Lisbet Camper, Patrik Önnerfjord, Dick Heinegård (see also Mikael Wendel)
Osteoadherin is a small cell-binding proteoglycan of Mr 85,000 as determined by SDS-PAGE. The protein is rich in aspartic acid, glutamic acid and leucine. Sequence determination has identified the protein as a LRR-protein closely related to e.g. fibromodulin [Sommarin et al., 1998]. The protein contains several N-glycosidically linked oligosaccharides, and in bovine bone some of these are elongated into a keratan sulphate chain [Wendel et al., 1998]. Osteoadherin contains up to 8 tyrosine sulphated residues primarily located in the N-terminal extension (Önnerfjord unpublished results). The protein and its message are primarily found along bone trabeculae.
Osteoadherin Interactions

Osteoadherin is a bone-specific protein that appears to have the capacity to bind cells via their αvβ3 integrin [Wendel et al., 1998]. It is isolated from bone in a disulphide bonded complex with Osteonectin. Osteoadherin-null mice are currently being characterized.

Osteoadherin in Disease
Not known.