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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

OGN  -  osteoglycin

Bos taurus

 
 
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High impact information on OGN

  • Osteoglycin (OGN), a small leucine-rich proteoglycan with unclear functions, is found in cornea, bone, and other tissues, and appears to undergo proteolytic processing in vivo [1].
  • Moreover, whereas wild-type mouse embryo fibroblasts (MEFs) produce primarily the processed, mature form of OGN, MEFs homozygous null for genes encoding three of the four mammalian BMP-1/Tolloid-related proteinases produce only unprocessed pro-OGN [1].
  • Biglycan, a proteoglycan that is structurally closely related to decorin contains a similar high affinity Zn2+-binding segment, whereas the structurally more distantly related proteoglycans, epiphycan and osteoglycin, do not bind Zn2+ with high affinity [2].
  • We conclude that the full-length translation product of the gene producing osteoglycin is a corneal keratan sulfate proteoglycan, also present in many non-corneal tissues without keratan sulfate chains [3].
  • This study examined the relationship between the KSPG25 protein and the gene for osteoglycin, a 12-kDa bone glycoprotein [3].
 

Biological context of OGN

References

  1. Bone morphogenetic protein-1/tolloid-related metalloproteinases process osteoglycin and enhance its ability to regulate collagen fibrillogenesis. Ge, G., Seo, N.S., Liang, X., Hopkins, D.R., Höök, M., Greenspan, D.S. J. Biol. Chem. (2004) [Pubmed]
  2. Decorin is a Zn2+ metalloprotein. Yang, V.W., LaBrenz, S.R., Rosenberg, L.C., McQuillan, D., Höök, M. J. Biol. Chem. (1999) [Pubmed]
  3. Mimecan, the 25-kDa corneal keratan sulfate proteoglycan, is a product of the gene producing osteoglycin. Funderburgh, J.L., Corpuz, L.M., Roth, M.R., Funderburgh, M.L., Tasheva, E.S., Conrad, G.W. J. Biol. Chem. (1997) [Pubmed]
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