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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1994-6-30
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pubmed:abstractText |
Human neutrophil azurophilic granules contain an approximately 55-kDa protein, known as bactericidal/permeability-increasing protein (BPI), which possesses a high-affinity binding domain for the lipid A component of lipopolysaccharide (LPS). The in vivo LPS neutralizing activity of exogenous BPI was studied in a model of lethal Escherichia coli bacteremia. Five baboons were treated with BPI (5 mg/kg bolus injection followed by a 95 micrograms/kg/min BPI infusion over 4 hr), while four additional animals received a genetically engineered variant of BPI (NCY103). Five animals received a placebo treatment and served as controls. Both wild-type rhBPI and NCY103 significantly (P < 0.05) decreased blood levels of LPS throughout an 8-hr evaluation period following live bacterial challenge. Two hours following E. coli administration, LPS levels peaked in the controls, at 6.86 +/- 3.22 ng/ml, whereas LPS levels were 3.39 +/- 2.1 ng/ml in the BPI group and 2.04 +/- 1.18 ng/ml in the NCY103 group. Tumor necrosis factor-alpha (TNF-alpha) and interleukin-6 levels likewise were attenuated in the treatment groups, whereas circulating sTNFR I was significantly (P < 0.05) reduced only in the BPI group. Leukocytopenia and granulocytopenia were significantly (P < 0.02) lessened in the BPI group, by an average of 59% leukocytopenia and 65% granulocytopenia, respectively. This study supports the concept of E. coli LPS neutralization by BPI in vivo and demonstrates that a moderate (70%) reduction in peak LPS-LAL activity is sufficient to alter some hematologic and cytokine manifestations of bacteremia.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Infective Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Antimicrobial Cationic Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-6,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Tumor Necrosis Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/bactericidal permeability...
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0271-9142
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
N
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pubmed:pagination |
120-33
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8195314-Animals,
pubmed-meshheading:8195314-Anti-Infective Agents,
pubmed-meshheading:8195314-Antimicrobial Cationic Peptides,
pubmed-meshheading:8195314-Bacteremia,
pubmed-meshheading:8195314-Blood Proteins,
pubmed-meshheading:8195314-Escherichia coli Infections,
pubmed-meshheading:8195314-Interleukin-6,
pubmed-meshheading:8195314-Membrane Proteins,
pubmed-meshheading:8195314-Neutrophils,
pubmed-meshheading:8195314-Papio,
pubmed-meshheading:8195314-Receptors, Tumor Necrosis Factor,
pubmed-meshheading:8195314-Recombinant Proteins,
pubmed-meshheading:8195314-Shock, Septic,
pubmed-meshheading:8195314-Tumor Necrosis Factor-alpha
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pubmed:year |
1994
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pubmed:articleTitle |
The role of bactericidal/permeability-increasing protein in the treatment of primate bacteremia and septic shock.
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pubmed:affiliation |
Department of Surgery, Cornell University Medical College, New York, New York 10021.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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