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Biotech / Medical : XOMA. Bull or Bear? -- Ignore unavailable to you. Want to Upgrade?

To: Pseudo Biologist who wrote (10791)	7/14/1999 7:55:00 PM
From: Robert K.	Read Replies (1) \| Respond to of 17367

PB. I will attempt to answer, but you can be assured its not as good a followup as cacaito will provide. According to the paper "many studies defining the therapeutic role for bpi during sepsis have been limited to acute studies or studies with very high bacterial load. In our study we used a less overwhelming bacteremia (2 logs less)" They used a hyperdynamic study approach I believe to more closely mimic clinical sepsis. Your other question , by what mechanism to reduce tnf etc.... IMO its prevention of lps-lbp from cd14 stimulation by bpi. cacatio.please correct me or add comments as need be. Thanks. BTW-the paper claims that ultimately it IS the reduced bacteria. IMO But think about what DOES actually get rid of LPS. (lbp probably) Also IMO.

To: Pseudo Biologist who wrote (10791)	7/15/1999 8:31:00 AM
From: Robert K.	Respond to of 17367

PB>more> The Three-Dimensional Structure of Human BPI: Implications for Protein-LPS Interactions Lesa J. Beamer, Stephen F. Carroll, David Eisenberg Biochemical Pharmacology, 57(3) (1999) pp. 225-229. ABSTRACT. Gram-negative bacterial infections are often complicated by the inflammatory properties of lipopolysaccharides (LPS) on or released from the bacterial outer membrane. When present in the mammalian bloodstream, LPS can trigger a series of pathological changes, sometimes resulting in septic shock. Two related mammalian proteins, bactericidal/permeability-increasing protein (BPI) and lipopolysaccharide-binding protein (LBP) are known to affect the LPS-induced inflammatory response and are therefore of clinical interest. The recently determined three-dimensional structure of human BPI provides information on the overall protein fold, domain organization, and conserved regions of these two proteins. In addition, the discovery of two apolar lipid binding pockets in BPI indicates a possible site of interaction with LPS. The BPI structure is an powerful tool for the design of site-directed mutants, peptide mimetics/inhibitors, and BPI/LBP chimeras. These studies should help further define the functions of BPI and LBP, and their mechanism of interaction with LPS.