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

OVOS  -  ovostatin

Homo sapiens

Synonyms: OVOS1, Ovostatin homolog 1
 
 
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High impact information on OVOS

  • A stretch of 34 amino acid residues of the ovostatin bait region sequence was determined and the matrix metalloproteinase cleavage sites identified [1].
  • Thus, proteinase-bound ovostatin has a uniform structure with a 2-fold axis of symmetry [2].
  • Both free and thermolysin-bound ovostatin preparations were negatively stained with uranyl acetate, a series of three pictures were taken at 10 degrees specimen tilt intervals (+10 degrees, 0 degrees, and -10 degrees), and images of the inhibitor molecules were observed in three dimensions [2].
  • The results support the unique mechanism of inhibition of proteinases by alpha 2-macroglobulin and ovostatin postulated from biochemical observations (Barrett, A. J., and Starkey, P. M. (1973) Biochem. J. 133, 709-724; Nagase, H., and Harris, E. D., Jr. (1983) J. Biol. Chem. 258, 7490-7498) [2].
  • 9. The protease activity is inhibited by chelators, Z-phenylalanine, ovostatin, and tissue inhibitor of metalloproteinase from human articular cartilage [3].
 

Biological context of OVOS

 

Associations of OVOS with chemical compounds

  • The results indicate that ovostatin is a close relative to plasma alpha-macroglobulins and may share a common ancestor with C3 and C4 [5].
  • The Cys-to-Asn substitution forms the chemical basis for the lack of thiol esters in hen egg-white ovostatin [6].
 

Other interactions of OVOS

  • From these electron microscopic studies we propose that a proteinase reaches to the center of the free ovostatin molecule and attacks the bait region [2].
 

Analytical, diagnostic and therapeutic context of OVOS

References

  1. Interaction of human rheumatoid synovial collagenase (matrix metalloproteinase 1) and stromelysin (matrix metalloproteinase 3) with human alpha 2-macroglobulin and chicken ovostatin. Binding kinetics and identification of matrix metalloproteinase cleavage sites. Enghild, J.J., Salvesen, G., Brew, K., Nagase, H. J. Biol. Chem. (1989)
  2. Electron microscopic studies of free and proteinase-bound duck ovostatins (ovomacroglobulins). Model of ovostatin structure and its transformation upon proteolysis. Ruben, G.C., Harris, E.D., Nagase, H. J. Biol. Chem. (1988)
  3. Purification and characterization of an acid metalloproteinase from human articular cartilage. Azzo, W., Woessner, J.F. J. Biol. Chem. (1986)
  4. Ovostatin: a novel proteinase inhibitor from chicken egg white. I. Purification, physicochemical properties, and tissue distribution of ovostatin. Nagase, H., Harris, E.D., Woessner, J.F., Brew, K. J. Biol. Chem. (1983)
  5. Amino acid sequence of a 32-residue region around the thiol ester site in duck ovostatin. Nagase, H., Brew, K. FEBS Lett. (1987)
  6. Evidence from sequence analysis that hen egg-white ovomacroglobulin (ovostatin) is devoid of an internal beta-Cys-gamma-Glu thiol ester. Nielsen, K.L., Sottrup-Jensen, L. Biochim. Biophys. Acta (1993)
  7. Amino acid sequence of hen ovomacroglobulin (ovostatin) deduced from cloned cDNA. Nielsen, K.L., Sottrup-Jensen, L., Nagase, H., Thøgersen, H.C., Etzerodt, M. DNA Seq. (1994)
 

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