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Sökning: WFRF:(Pourhossein M)

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1.
  • Ah, Rebecka, et al. (författare)
  • Prognostic Value of P-POSSUM and Osteopenia for Predicting Mortality After Emergency Laparotomy in Geriatric Patients
  • 2019
  • Ingår i: Bulletin of emergency and trauma. - : Shiraz University of Medical Sciences. - 2322-2522 .- 2322-3960. ; 7:3, s. 223-231
  • Tidskriftsartikel (refereegranskat)abstract
    • Objective: To evaluate the Portsmouth-Physiological and Operative Severity Score for the enUmeration of Mortality and morbidity (P-POSSUM) in comparison with other risk factors for mortality including osteopenia as an indicator for frailty in geriatric patients subjected to emergency laparotomy.Methods: All geriatric patients (≥65 years) undergoing emergency laparotomy at a single university hospital between 1/2015 and 12/2016 were included in this cohort study. Demographics and outcomes were retrospectively collected from medical records. Association between prognostic markers and 30-day mortality was assessed using Poisson and backward stepwise regression models. Prognostic value was assessed using receiver operating characteristic (ROC) curves.Results: =0.004) while osteopenia was not. P-POSSUM had poor prognostic value for 30-day mortality with an area under the ROC curve (AUC) of 0.59. The prognostic value of P-POSSUM improved significantly when adjusting for patient covariates (AUC=0.83).Conclusion: P-POSSUM and osteopenia alone hardly predict 30-day mortality in geriatric patients following emergency laparotomy. P-POSSUM adjusted for other patient covariates improves the prediction.
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2.
  • Hodson, N, et al. (författare)
  • Identification that KfiA, a protein essential for the biosynthesis of the Escherichia coli K5 capsular polysaccharide, is an alpha -UDP-GlcNAcglycosyltransferase : The formation of a membrane-associated K5 biosynthetic complex requires KfiA, KfiB and KfiC.
  • 2000
  • Ingår i: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 275:35, s. 27311-27315
  • Tidskriftsartikel (refereegranskat)abstract
    • The Escherichia coli K5 capsular polysaccharide consists of the repeat structure -4)GlcA-beta(1,4)-GlcNAc-alpha(1-and requires the KfiA, KfiB, KfiC, and KfiD proteins for its synthesis, Previously, the KfiC protein was shown to be a beta-UDP-GlcA glycosyltransferase, and KfiD was shown to be a UDP-Glc dehydrogenase. Here, we demonstrate that KfiA is an alpha-UDP-GlcNAc glycosyltransferase and that biosynthesis of the K5 polysaccharide involves the concerted action of the KfiA and KfiC proteins. By site-directed mutagenesis, we determined that the acidic motif of DDD, which is conserved between the C family of glycosyltransferases, is essential for the enzymatic activity of KfiA III addition, by Western blot analysis, we determined that association of KfiA with the cytoplasmic membrane requires KfiC but not KfiB, whereas the interaction of KfiC with the cytoplasmic membrane was dependent on both KfiA and KfiB. Likewise, KfiB was only detectable in cytoplasmic membrane fractions when both KfiA and KfiC were present. These data suggest that the interaction between the KfiA, KfiB, and KfiC proteins is essential for the stable association of these proteins with the cytoplasmic membrane and the biosynthesis of the K5 polysaccharide.
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