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Synergistic interactions between mammalian antimicrobial defense peptides. Antimicrob. Agents Chemother
, 2001
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This article cites 13 articles, 5 of which can be accessed free at:
Bacteria in the intestine, helpful residents or enemies from within
- Infection and Immunity
, 2008
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Cited by 7 (0 self)
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This article cites 157 articles, 57 of which can be accessed free
Forecast Alert
- IT Spending, Worldwide, 2008-2015, 4Q11 Update. 2012 http://www.gartner.com: http://www.gartner.com/it/content/1870000/1870018/january_10_it_spending_forecast_4q11_update_rgordon.p df?userId=57517080
, 2011
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This article cites 42 articles, 15 of which can be accessed free
Human lipopolysaccharide-binding protein potentiates bactericidal activity of human bactericidal/permeability-increasing protein. Infect. Immun
, 1995
"... Human bactericidal/permeability-increasing protein (BPI) from neutrophils and a recombinant amino-terminal fragment, rBPI23, bind to and are cytotoxic for gram-negative bacteria both in vitro and ex vivo in plasma or whole blood. To function in vivo as an extracellular bactericidal agent, rBPI23 mus ..."
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Human bactericidal/permeability-increasing protein (BPI) from neutrophils and a recombinant amino-terminal fragment, rBPI23, bind to and are cytotoxic for gram-negative bacteria both in vitro and ex vivo in plasma or whole blood. To function in vivo as an extracellular bactericidal agent, rBPI23 must act in the presence of the lipopolysaccharide-binding protein (LBP), which also binds to but has no reported cytotoxicity for gram-negative bacteria. LBP, which is present at 5 to 10 mg/ml in healthy humans and at much higher levels in septic patients, mediates proinflammatory host responses to gram-negative infection. On the basis of these previous observations, we have examined the effect of recombinant LBP (rLBP) on the bactericidal activity of rBPI23 against Escherichia coli J5 in vitro. Physiological concentrations of rLBP (5 to 20 mg/ml) had little or no bactericidal activity but reduced by up to;10,000-fold the concentration of BPI required for bactericidal or related activities in assays which measure (i) cell viability as CFUs on solid media or growth in broth culture and (ii) protein synthesis following treatment with BPI. LBP also potentiated BPI-mediated permeabilization of the E. coli outer membrane to actinomycin D by about 100-fold but had no permeabilizing activity of its own. Under optimal conditions for potentiation, fewer than 100 BPI molecules were required to kill a single E. coli J5 bacterium. Bactericidal/permeability increasing protein (BPI) is a 55-
Brigham and Women’s Hospital
"... Copyright © 2005 by the American Physiological Society. G-00347-2005.R1 Epithelial cells of many mucosal organs have adapted to co-exist with microbes and microbial products. In general, most studies suggest that epithelial cell benefit from interactions with commensal microorganisms present at the ..."
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Copyright © 2005 by the American Physiological Society. G-00347-2005.R1 Epithelial cells of many mucosal organs have adapted to co-exist with microbes and microbial products. In general, most studies suggest that epithelial cell benefit from interactions with commensal microorganisms present at the lumenal surface. However, potentially injurious molecules found in this microenvironment also have the capacity to elicit local inflammatory responses and even systemic disease. We recently demonstrated that epithelia cells express the anti-infective molecule bactericidal/permeability-increasing protein (BPI). Here, we extend these findings to examine molecular mechanisms of intestinal epithelial cell (IEC) BPI expression and function. Initial experiments revealed a broad variance of BPI mRNA and protein expression among various intestinal epithelial cell lines. Studies of BPI promoter expression in IEC identified regulatory regions of the BPI promoter, and revealed a prominent role for C/EBP and especially Sp1/Sp3 in basal regulation of BPI. In order to assess the functional significance of this protein we generated an IEC line stably transfected with full-length BPI. We demonstrated
Induction of a Rat Enteric Defensin Gene by
, 1999
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ANTIMICROBIAL PEPTIDES—BACKGROUND AND DEFINITION
"... SYNOPSIS. Production of antimicrobial peptides and proteins is an important means of host defense in eukaryotes. The larger antimicrobial proteins, containing more than 100 amino acids, are often lytic en-zymes, nutrient-binding proteins or contain sites that target specific microbial macromolecules ..."
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SYNOPSIS. Production of antimicrobial peptides and proteins is an important means of host defense in eukaryotes. The larger antimicrobial proteins, containing more than 100 amino acids, are often lytic en-zymes, nutrient-binding proteins or contain sites that target specific microbial macromolecules. The smaller antimicrobial peptides act largely by disrupting the structure or function of microbial cell membranes. Hundreds of antimicrobial peptides have been found in the epithelial layers, phagocytic cells and body fluids of multicellular animals, from mollusks to humans. Some antimicrobial peptides are produced constitutively, others are induced in response to infection or inflammation. Studies of the regulation of antimicrobial peptide synthesis in Drosophila have been particularly fruitful, and have provided a new paradigm for the analysis of mammalian host defense responses. It now appears that the general patterns of antimicrobial responses of invertebrates have been preserved in vertebrates (‘‘innate immunity’’) where they contribute to host defense both independently and in complex interplay with adaptive immunity.
These include:
, 1996
"... group II phospholipase A2 acting against Determinants of activation by complement of ..."
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group II phospholipase A2 acting against Determinants of activation by complement of
Extracellular Accumulation of Potently Microbicidal Bactericidal/ Permeability-increasing Protein and pl5s in an Evolving Sterile Rabbit
"... To what extent the host defense role of granule-associated antibacterial proteins and peptides of PMN includes extra-cellular action has not been established. To address this question, we have analyzed the antibacterial activity of cell-free (ascitic) fluid (AF) obtained from glycogen-induced steril ..."
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To what extent the host defense role of granule-associated antibacterial proteins and peptides of PMN includes extra-cellular action has not been established. To address this question, we have analyzed the antibacterial activity of cell-free (ascitic) fluid (AF) obtained from glycogen-induced sterile inflammatory rabbit peritoneal exudates in which> 95 % of the accumulating cells are PMN. AF, but not plasma collected in parallel, exhibits potent activity toward serum-resistant Gram-negative and Gram-positive bacteria. Total and specific antibacterial activity ofAF increases dur-ing the first 12 h after injection of glycogen in parallel with the influx ofPMN. At maximum,> 99 % of 107 encapsulated Escherichia coli and Staphylococcus aureus are killed in 30 min/ml of AF. Neutralizing antibodies against the bacteri-cidal/permeability-increasing protein (BPI) of PMN abol-ishes activity of AF toward encapsulated E. coli but has no effect on activity vs staphylococci. However, BPI alone (- 1 jag/ml in AF) can only account for- 20 % of AF activity toward E. coli. AF also contains 15 kD PMN proteins (pl5s) that act in synergy with BPI. Purified BPI and pl5s, in amounts present in AF, reconstitute the growth-inhibitory activity of AF toward encapsulated E. coli. These findings show for the first time an extracellular function of endoge-nous BPI, providing, together with the pl5s, a potent micro-bicidal system toward Gram-negative bacteria resistant to plasma-derived proteins and phagocytes in inflammatory exudates. (J. Clin. Invest. 1995. 95:1916-1924.) Key words: polymorphonuclear leukocyte- inflammation * bacteria. ascites * synergy