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

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Cystatin domains in alpha-2-HS-glycoprotein and fetuin.

We have found that chain A of alpha-2-HS-glycoprotein contains two cystatin domains that show closest similarity to those of kininogen. Most likely, the two proteins diverged after the primary duplication of a single cystatin domain as the two cystatin domains of alpha-2-HS-glycoprotein are more similar, especially in disulfide bonding, to the corresponding domains of kininogen than to each other. We also propose that the carboxyl-terminal (non-cystatin) parts of kininogen and alpha-2-HS-glycoprotein contain homologous segments. We suggest that alpha-2-HS-glycoprotein may act as an inhibitor of the cysteine proteinases responsible for bone resorption. We have also found that fetuin is closely related to alpha-2-HS-glycoprotein.[1]

References

  1. Cystatin domains in alpha-2-HS-glycoprotein and fetuin. Elzanowski, A., Barker, W.C., Hunt, L.T., Seibel-Ross, E. FEBS Lett. (1988) [Pubmed]
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