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Gene Review

OMD  -  osteomodulin

Bos taurus

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Disease relevance of OMD


High impact information on OMD


Biological context of OMD


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


Analytical, diagnostic and therapeutic context of OMD


  1. Analysis of transcriptional regulation of the small leucine rich proteoglycans. Tasheva, E.S., Klocke, B., Conrad, G.W. Mol. Vis. (2004) [Pubmed]
  2. Bone matrix proteins: isolation and characterization of a novel cell-binding keratan sulfate proteoglycan (osteoadherin) from bovine bone. Wendel, M., Sommarin, Y., Heinegård, D. J. Cell Biol. (1998) [Pubmed]
  3. Tissue distribution of a novel cell binding protein, osteoadherin, in the rat. Shen, Z., Gantcheva, S., Sommarin, Y., Heinegård, D. Matrix Biol. (1999) [Pubmed]
  4. Identification, distribution and expression of osteoadherin during tooth formation. Petersson, U., Hultenby, K., Wendel, M. Eur. J. Oral Sci. (2003) [Pubmed]
  5. Attachment of Salmonella choleraesuis choleraesuis to beef muscle and adipose tissues. Bouttier, S., Linxe, C., Ntsama, C., Morgant, G., Bellon-Fontaine, M.N., Fourniat, J. J. Food Prot. (1997) [Pubmed]
  6. Ultrastructural distribution of osteoadherin in rat bone shows a pattern similar to that of bone sialoprotein. Ramstad, V.E., Franzén, A., Heinegård, D., Wendel, M., Reinholt, F.P. Calcif. Tissue Int. (2003) [Pubmed]
  7. Osteoadherin, a cell-binding keratan sulfate proteoglycan in bone, belongs to the family of leucine-rich repeat proteins of the extracellular matrix. Sommarin, Y., Wendel, M., Shen, Z., Hellman, U., Heinegârd, D. J. Biol. Chem. (1998) [Pubmed]
  8. Effect of methionine addition to a urea-grain supplement on intake and digestibility of mature, dormant grasses and performance of cows grazing winter range. Momont, P.A., Pruitt, R.J., Johnson, P.S. J. Anim. Sci. (1993) [Pubmed]
  9. Effects of different supplemental sugars and starch fed in combination with degradable intake protein on low-quality forage use by beef steers. Heldt, J.S., Cochran, R.C., Stokka, G.L., Farmer, C.G., Mathis, C.P., Titgemeyer, E.C., Nagaraja, T.G. J. Anim. Sci. (1999) [Pubmed]
  10. Identification of tyrosine sulfation in extracellular leucine-rich repeat proteins using mass spectrometry. Onnerfjord, P., Heathfield, T.F., Heinegård, D. J. Biol. Chem. (2004) [Pubmed]
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