Disease relevance of OMD

• The intergenic region between OMD and mimecan was shown to coincide with different patterns of DNAse I hypersensitivity sites in MG-63 and U937 cells [1].

High impact information on OMD

• The binding appears to be mediated by the integrin alphavbeta3, since this was the only integrin isolated by osteoadherin affinity chromatography of surface-iodinated osteoblast extracts [2].
• In immunohistochemical studies of the bovine fetal rib growth plate, osteoadherin was exclusively identified in the primary bone spongiosa [2].
• Bone matrix proteins: isolation and characterization of a novel cell-binding keratan sulfate proteoglycan (osteoadherin) from bovine bone [2].
• Osteoadherin binds to hydroxyapatite [2].
• These sequences are not previously described, and support the notion that osteoadherin belongs to the family of leucine-rich repeat proteins [2].

Biological context of OMD

• Tissue distribution of a novel cell binding protein, osteoadherin, in the rat [3].
• For studies of osteoadherin expression in rat tissues we isolated and sequenced a 1.3-kbp partial cDNA covering most of the coding region using a rat calvaria cDNA library [3].

Anatomical context of OMD

• We have identified OSAD in extracts of bovine dentin, and the identity was verified by N-terminal sequencing [4].
• Treatment of the tissue with a concentrated suspension of flagella or treatment of the bacteria with antisomatic serum (OMD) did not reduce the attachment of S. choleraesuis to tissues, indicating an absence of specific attachment sites for flagella or antigen O on the beef tissue surface [5].
• Ribonuclease protection assay showed osteoadherin mRNA to be expressed in femoral bone and calvaria tissues, while no expression was detected in cartilage, tendon or liver [3].
• To test these hypotheses in an in vivo model, the ultrastructural localization of OSAD in bone, tibial (metaphyses and diaphyses), and calvarial samples from normal 10 to 12-day-old rats were examined by immunohistochemical techniques at the ultrastructural level [6].

Associations of OMD with chemical compounds

• A small cell-binding proteoglycan for which we propose the name osteoadherin was extracted from bovine bone with guanidine hydrochloride-containing EDTA [2].
• Osteoadherin is a recently described bone proteoglycan containing keratan sulfate [7].
• Controlled-release chromic oxide boluses were used as an external marker to estimate fecal output, and acid insoluble ash was used as an internal marker to predict OM digestibility (OMD) [8].
• Additionally, sugars yielded a higher (P = .04) OMD than starch, and the monosaccharides yielded a higher (P = .02) OMD than sucrose [9].
• Osteoadherin contains two additional sulfated tyrosine residues close to its C terminus [10].

Physical interactions of OMD

• Osteoadherin is a cell binding keratan sulfate proteoglycan which was recently isolated from mineralized bovine bone and subsequently cloned and sequenced [3].

Analytical, diagnostic and therapeutic context of OMD

• An enzyme-linked immunosorbent assay was developed, and showed the osteoadherin content of bone extracts to be 0.4 mg/g of tissue wet weight, whereas none was found in extracts of various other bovine tissues [2].
• Northern blot analysis of RNA samples from various bovine tissues showed a 4.5-kilobase pair message for osteoadherin to be expressed in bone only [7].
• Osteoadherin mRNA was detected by in situ hybridization in mature osteoblasts located superficially on trabecular bone [7].
• An antiserum specific for the rat C-terminal region of osteoadherin was generated and used for studies of protein distribution by immunohistochemistry during femoral head development [3].

References