Hite, M.C. Pro-apoptotic Bid induces membrane perturbation by inserting selected lysolipids into the bilayer. Induction of autolysis of staphylococci by the basic peptide antibiotics Pep 5 and nisin and their influence on the activity of autolytic enzymes, A rapid method of total lipid extraction and purification, Detection and partial characterization of antibacterial factor(s) in alveolar lining material of rats, 2-Acylglycerolphosphoethanolamine acyltransferase/acyl-acyl carrier protein synthetase is a membrane-associated acyl carrier protein binding protein, Characterization of a bactericidal lipid developing within staphylococcal abscesses, Oxygen-independent antimicrobial systems of phagocytes, Cell-wall determinants of the bactericidal action of group IIA phospholipase A2 against gram-positive bacteria, Structural and functional properties of a phospholipase A2 purified from an inflammatory exudate, Metabolism of phosphatidylglycerol and lysyl phosphatidylglycerol in, Alteration of the phospholipid composition of, Mechanism of bactericidal activity of lysolecithin and its biological implication, Inhalation of cold air increases the number of inflammatory cells in the lungs in healthy subjects, Antibiotic proteins of polymorphonuclear leukocytes, Isolation and characterization of autolysis-defective mutants of, Inflammatory cytokines in the BAL of patients with ARDS. The fate of PLA2-treated S. aureus therefore appears to depend on the relative rates of phospholipid degradation and synthesis. These metrics are regularly updated to reflect usage leading up to the last few days. Phosphatidylglycerol (PG), the major phospholipid of S. aureus (14, 28), is degraded and resynthesized up to three times during one bacterial doubling (9). Michael C Seeds Department of Internal Medicine, Section on Pulmonary, Critical Care, Allergy and Immunologic Diseases, Wake Forest University School of Medicine, Medical Center Boulevard, Winston-Salem, NC 27157, USA. PLA2 degradation of extracted S. aureusphospholipids in the presence and absence of BSA. PLA2-treated bacteria also continue to incorporate sodium [2-14C]acetate into phospholipids, suggesting that the bacteria are attempting to repair the damaged membranes by de novo synthesis of phospholipids. l and resuspended in 30 μl of chloroform-methanol (2:1, vol/vol). It has been shown previously that killing of S. aureusby mammalian group IIA PLA2 is accompanied by degradation of nearly all bacterial phospholipids (10, 32). TLC analysis of bacterial (phospho)lipids.To identify the degradation products formed during treatment of [1-14C]oleate-labeled S. aureus with PLA2 or the lantibiotic nisin (1) (Sigma Chemical Co., St. Louis, Mo. A sample of 106S. In the absence of albumin, the bacteria retain and substantially reutilize the phospholipid breakdown products and survive an otherwise lethal dose of PLA2.

In both the Lyt+ and Lyt− strains, the control and PLA2-treated bacteria incorporated a comparable amount of acetate into the phospholipids, despite the lack of growth by the PLA2-treated bacteria. Phospholipase A2 hydrolyzed ... phosphatidylglycerol, whereas phospholipase C preferentially degraded phosphatidylethanolamine.

Enter multiple addresses on separate lines or separate them with commas. The results represent the mean and standard error of the mean of three independent determinations. L618-L624 There is no increase in diglycerides or phosphatidic acid, indicating that PLA2 does not trigger a PLC-like or PLD-like activity. In the salvage pathway, lyso compounds are either directly reacylated or further degraded by endogenous (bacterial) enzymes before reutilization (5). aureus RN450 Lyt+ (A) and Lyt− (B) (4 × 107/ml) were resuspended by sonication in RPMI 1640 supplemented with 10 mM HEPES (pH 7.4) and 1 mM CaCl2 and incubated at 37°C for 60 min with 300 ng of PLA2 per ml with and without 1% BSA. Taken together, these results indicate that bacterial PLC or PLD enzymes do not contribute to PLA2-mediated phospholipid degradation. After addition of acidified physiological saline, pH 2.0 (8.3 sample volumes), the sample was vortexed for 30 s and briefly centrifuged (70 × g for 5 min) to facilitate separation of the phases. Ileana M. Cristea, Mauro Degli Esposti. Membrane lipids and cell death: an overview. 3A). Interactions of two structurally related anionic phospholipids cardiolipin and phosphatidylglycerol with phospholipase A2. Some error bars are masked by the symbols. All samples were run with the appropriate standards to aid in the identification of the lipid species, using one of the following solvent systems: (i) chloroform-methanol-H2O-glacial acetic acid (65:25:4:1, by volume) (To separate PG, lysyl-PG, lyso-PG, and phosphatidic acid, Silica Gel G plates [Analtech] were developed for 90 to 100 min in this solvent; to further separate lysyl-PG from the degradation product lyso-PG, the plates were dried and developed a second time.) Activation of isoforms of PLA 2, cyclooxygenase-2, and lipoxygenase contribute to the production of eicosanoids and other nonenzymic arachidonic acid–derived products, such as 4-hydroxynonenal and isoprotane (Farooqui and Horrocks, 2009). Purification of rabbit AF PLA2.Rabbit group IIA PLA2 was purified from ascitic fluid (AF) by ion exchange chromatography and reversed-phase high-pressure liquid chromatography as previously described (11, 32, 35). In other bacteria (e.g., E. coli), there are two pathways by which lyso-PG is reused. It is unlikely that there are sites in the mammalian host that are completely free of albumin during a bacterial infection.

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