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. 2002 Feb:Chapter 21:21.7.1-21.7.14.
doi: 10.1002/0471140864.ps2107s26.

Serpins (serine protease inhibitors)

Susannah J Bauman  1 , Herbert C Whinna  1 , Frank C Church  1
Affiliations

Serpins (serine protease inhibitors)

Susannah J Bauman et al. Curr Protoc Protein Sci. 2002 Feb.

Abstract

Serpins are a class of proteins involved in the regulation of serine and other types of proteases. In humans, the majority of serpins regulate the functions of proteases involved in the body's response to injury. This includes roles in coagulation, fibrinolysis, inflammation, wound healing, and tissue repair. Serpins have been implicated in various animal and human pathologies by the loss of a functional serpin gene through deletion or mutation, which results in a defect in functional protein. Examples of sestorically called antithrombin III) are first described. Then, protocols to determine the second-order rate constant of AT inhibition of thrombin in the absence and presence of heparin are presented. Also provided is a partial list of other serpins and their purification methods.

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References

Literature Cited
    1. Carrell, R.W. and Travis, J. 1985. α1-Antitrypsin and the serpins: Variations and countervariations. Trends Biochem. Sci 10:20-24.
    1. Chang, W.-S.W. and Lomas, D.A. 1998. Latent α1-antichymotrypsin: A molecular explanation for the inactivation of α1-antichymotrypsin in chronic bronchitis and emphysema J. Biol. Chem. 273:3695-3701.
    1. Church, F.C. and Whinna, H.C. 1986. Rapid sulfopropyl-disk chromatographic purification of bovine and human thrombin. Anal. Biochem. 157:77-83.
    1. Church, F.C., Meade, J.B., and Pratt, C.W. 1987. Stucture-function relationships in heparin cofactor II: Spectral analysis of aromatic residues and absence of a role for sulfhydryl groups in thrombin inhibition. Arch. Biochem. Biophys. 259:331-340.
    1. Church, F.C., Cunningham, D.D., Ginsburg, D., Hoffman, M., Stone, S.R., and Tollefsen, D.M. 1997. Chemistry and biology of serpins. Adv. Exp. Med. Biol. 425:358.
Key References
    1. Church et al., 1997.
    1. Gettins and Olson, 1996.
    1. Griffith et al., 1985a.
    1. Silverman, G.A., Bird, P.I., Carrell, R.W., Church, F.C., Coughlin, P.B., Gettins, P.G., Irving, J.A., Lomas, D.A., Luke, C.J., Moyer, R.W., Pemberton, P.A., Remold-O'Donnell, E., Salvesen, G.S., Travis, J., and Whisstock, J.C. 2001. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. J. Biol. Chem. 276:33293-33296.

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