Drains did not prevent seroma formation, and were associated with a longer postoperative stay and higher pain scores after surgery for breast cancer. In patients who had mastectomy the use of fibrin sealant reduced the rate of seroma formation.

No abstract

BT is associated with postoperative sepsis. Emergency surgery and TPN are independently associated with an increased prevalence of BT.

A number of pathogenic bacteria target mitochondria to modulate the host's apoptotic machinery. Studies here revealed that infection with the human gastric pathogen Helicobacter pylori disrupts the morphological dynamics of mitochondria as a mechanism to induce host cell death. The vacuolating cytotoxin A (VacA) is both essential and sufficient for inducing mitochondrial network fragmentation through the mitochondrial recruitment and activation of dynamin-related protein 1 (Drp1), which is a critical regulator of mitochondrial fission within cells. Inhibition of Drp1-induced mitochondrial fission within VacA-intoxicated cells inhibited the activation of the proapoptotic Bcl-2-associated X (Bax) protein, permeabilization of the mitochondrial outer membrane, and cell death. Our data reveal a heretofore unrecognized strategy by which a pathogenic microbe engages the host's apoptotic machinery.cytochrome c | mitochondrial dynamics | gastric cancer | gastric ulcer | toxin

Background: It is possible to manipulate the composition of the gastrointestinal microflora by administration of pre-and probiotics. This may help to preserve gut barrier function and reduce the incidence of septic morbidity. Aims: To assess the effects of a combination of pre-and probiotics (synbiotic) on bacterial translocation, gastric colonisation, systemic inflammation, and septic morbidity in elective surgical patients. Patients: Patients were enrolled two weeks prior to elective abdominal surgery. Seventy two patients were randomised to the synbiotic group and 65 to the placebo group. Patients were well matched regarding age and sex distribution, diagnoses, and POSSUM scores. Methods: Patients in the synbiotic group received a two week preoperative course of Lactobacillus acidophilus La5, Bifidobacterium lactis Bb-12, Streptococcus thermophilus, and Lactobacillus bulgaricus, together with the prebiotic oligofructose. Patients in the placebo group received placebo capsules and sucrose powder. At surgery, a nasogastric aspirate, mesenteric lymph node, and scrapings of the terminal ileum were harvested for microbiological analysis. Serum was collected preoperatively and on postoperative days 1 and 7 for measurement of C reactive protein, interleukin 6, and antiendotoxin antibodies. Septic morbidity and mortality were recorded. Results: There were no significant differences between the synbiotic and control groups in bacterial translocation (12.1% v 10.7%; p = 0.808, x 2 ), gastric colonisation (41% v 44%; p = 0.719), systemic inflammation, or septic complications (32% v 31%; p = 0.882). Conclusions: In this study, synbiotics had no measurable effect on gut barrier function in elective surgical patients. Further studies investigating the place of pre-and probiotics in clinical practice are required.

Both sucralose and 51Cr-EDTA underwent significant colonic absorption. A significant amount of lactulose also appeared to be absorbed in the colon. This unexpected finding requires further study.

No abstract

Modification of eukaryotic proteins is a powerful strategy used by pathogenic bacteria to modulate host cells during infection. Previously, we demonstrated that Helicobacter pylori modify an unidentified protein within mammalian cell lysates in a manner consistent with the action of a bacterial ADP-ribosylating toxin. Here, we identified the modified eukaryotic factor as the abundant nuclear factor poly(ADP-ribose) polymerase-1 (PARP-1), which is important in the pathologies of several disease states typically associated with chronic H. pylori infection. However, rather than being ADP-ribosylated by an H. pylori toxin, the intrinsic poly(ADPribosyl) polymerase activity of PARP-1 is activated by a heat-and protease-sensitive H. pylori factor, resulting in automodification of PARP-1 with polymers of poly(ADP-ribose) (PAR). Moreover, during infection of gastric epithelial cells, H. pylori induce intracellular PAR-production by a PARP-1-dependent mechanism. Activation of PARP-1 by a pathogenic bacterium represents a previously unrecognized strategy for modulating host cell signaling during infection.apoptosis ͉ infection ͉ PARP-1 ͉ toxin C hronic infection with Helicobacter pylori is a significant risk for the development of peptic ulcer disease and gastric cancer in humans (1-3). During infection, H. pylori generate several protein factors that modulate host cells and tissues in a manner that contributes to pathogen colonization and persistence, as well as the pathophysiological changes associated with gastric disease (4). Previous work indicated that a soluble factor within mammalian cell lysates was modified in the presence of NAD and H. pylori culture filtrate (HPCF) (5). Initial characterization suggested that the eukaryotic factor was ADPribosylated (5). Notably, the ADP-ribosylation of eukaryotic targets has been identified as the action of multiple protein toxins and effectors important for bacterial virulence (6). Because the modified eukaryotic factor demonstrated an apparent molecular weight greater than any of the currently identified ADP-ribose acceptors, we hypothesized that this factor is a member of the growing list of eukaryotic proteins targeted for ADP-ribosylation by pathogens (5).The objective of this study was to identify the mammalian protein previously demonstrated to be modified in an H. pyloridependent manner (5). Here, we demonstrate that the modified protein is the nuclear factor poly(ADP-ribose) polymerase-1 (PARP-1), which is involved in the pathogenesis of several cancers and inflammatory disorders (7,8). Unexpectedly, rather than being modified by a bacterial ADP-ribosylating toxin, the intrinsic catalytic activity of PARP-1 is activated by a heat-and protease-sensitive factor(s) within the HPCF, resulting in automodification with polymers of poly(ADP-ribose) (PAR). Moreover, we demonstrated that PARP-1-dependent PAR production occurs in gastric epithelial cells infected with H. pylori. H. pylori activation of PARP-1 may represent a strategy for pathogen modulation of host signaling. ...