| Osteoadherin | ||||||||||
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Osteoadherin |
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| Osteoadherin Structure | ||||||||||
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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 Osteoadherin contains up to 8 tyrosine sulphated residues primarily located in the N-terminal extension (Önnerfjord unpublished results).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. |
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| Osteoadherin Interactions | ||||||||||
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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. |
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Osteoadherin
in Disease
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| Not known. | ||||||||||
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