Title: Bactericidal Permeability-Increasing Protein
Additional Names: BPI
Literature References: Antibacterial protein found in azurophilic granules of mammalian neutrophils; plays a predominant role during phagocytosis. Selectively cytotoxic for gram negative bacteria; binds to both soluble and membrane lipopolysaccharide (LPS) and neutralizes endotoxin activity. Cationic protein containing 456 amino acid residues having a characteristic "boomerang" shape; mol wt ~55 kDa. Antibacterial activity resides in the amino terminal half while the C-terminal domain facilitates phagocytosis. Isoln from human polymorphonuclear leukocytes: J. Weiss et al., J. Biol. Chem. 253, 2664 (1978). Cloning and primary structure: P. W. Gray et al., ibid. 264, 9505 (1989). Crystal structure: L. J. Beamer et al., Science 276, 1861 (1997); eidem, Biochem. Pharmacol. 57, 225 (1999). ELISA determn in body fluids: M. L. White et al., J. Immunol. Methods 167, 227 (1994). Review of role in host defense: P. Elsbach, J. Leukocyte Biol. 64, 14-18 (1998); P. Elsbach, J. Weiss, Curr. Opin. Immunol. 10, 45-49 (1998).
Derivative Type: Opebacan
CAS Registry Number: 158113-60-1
CAS Name: 1-193-Bactericidal/permeability-increasing protein [132-alanine] (human reduced)
Additional Names: rBPI21
Trademarks: Neuprex (Xoma)
Literature References: Amino-terminal fragment of human BPI produced by recombinant DNA technology in Chinese hamster ovary cells. Biologically active mutein in which the cysteine at position 132 has been replaced with alanine; mol wt 25 kDa. Prepn: G. Theofan et al., WO 9418323; eidem, US 5420019 (1994, 1995 both to Xoma); A. H. Horwitz et al., Protein Expression Purif. 8, 28 (1996). Clinical trial in meningococcal sepsis: M. Levin et al., Lancet 356, 961 (2000). Review of development and clinical potential in meningococcemia and hemorrhagic trauma: P. J. Scannon, J. Endotoxin Res. 5, 209-212 (1999); O. Levy, Expert Opin. Invest. Drugs 11, 159-167 (2002).
Therap-Cat: Antisepsis; in treatment of meningococcemia. |