AIM To evaluate the diagnostic and prognostic value of presepsin in cirrhosis-associated bacterial infections. METHODS Two hundred and sixteen patients with cirrhosis were enrolled. At admission, the presence of bacte...AIM To evaluate the diagnostic and prognostic value of presepsin in cirrhosis-associated bacterial infections. METHODS Two hundred and sixteen patients with cirrhosis were enrolled. At admission, the presence of bacterial infections and level of plasma presepsin, serum C-reactive protein(CRP) and procalcitonin(PCT) were evaluated. Patients were followed for three months to assess the possible association between presepsin level and short-term mortality.RESULTS Present 34.7 of patients had bacterial infection. Presepsin levels were significantly higher in patients with infection than without(median, 1002 pg/m L vs 477 pg/m L, P < 0.001), increasing with the severity of infection [organ failure(OF): Yes vs No, 2358 pg/m L vs 710 pg/m L, P < 0.001]. Diagnostic accuracy of presepsin for severe infections was similar to PCT and superior to CRP(AUC-ROC: 0.85, 0.85 and 0.66, respectively, P = NS for presepsin vs PCT and P < 0.01 for presepsin vs CRP). At the optimal cut-off value of presepsin > 1206 pg/m L sensitivity, specificity, positive predictive values and negative predictive values were as follows: 87.5%, 74.5%, 61.8% and 92.7%. The accuracy of presepsin, however, decreased in advanced stage of the disease or in the presence of renal failure, most probably because of the significantly elevated presepsin levels in non-infected patients. 28-d mortality rate was higher among patients with > 1277 pg/m L compared to those with ≤ 1277 pg/m L(46.9% vs 11.6%, P < 0.001). In a binary logistic regression analysis, however, only PCT(OR = 1.81, 95%CI: 1.09-3.01, P = 0.022) but neither presepsin nor CRP were independent risk factor for 28-d mortality after adjusting with MELD score and leukocyte count.CONCLUSION Presepsin is a valuable new biomarker for defining severe infections in cirrhosis, proving same efficacy as PCT. However, it is not a useful marker of short-term mortality.展开更多
This study is conducted to clone the cDNA encoding human TNF-related apoptosis-inducing ligand (hTRAIL) extracellular region (amino acids 41-281, hTRAIL41-281) and to express it in E.coli. The hTRAIL41-281 cDNA is amp...This study is conducted to clone the cDNA encoding human TNF-related apoptosis-inducing ligand (hTRAIL) extracellular region (amino acids 41-281, hTRAIL41-281) and to express it in E.coli. The hTRAIL41-281 cDNA is amplified by reverse transcription (RT) PCR from total RNA derived from human acute promyelocytic leukemia cell line HL-60. After sequenced, the cDNA is cloned into the vector pQE-80L and transformed into E.coli DH5 to express the recombinant hTRAIL41-281 (rhTRAIL41-281) induced by IPTG. The recombinant protein is analyzed by SDS-PAGE. The cloned cDNA is consistent with the cDNA sequence encoding hTRAIL41-281 reported in GenBankTM. After inducing, the hTRAIL41-281 protein is expressed, and the mass of the recombinant protein is about 30 % of total bacteria protein, which demonstrates that the cDNA encoding hTRAIL41-281 is successfully cloned and expressed in E.coli.展开更多
The effects of melittin on growth and bacteriostasis of four pathogens were extensively investigated using scanning electron microscopy(SEM) and transmission electron microscopy(TEM).The results indicated that the mel...The effects of melittin on growth and bacteriostasis of four pathogens were extensively investigated using scanning electron microscopy(SEM) and transmission electron microscopy(TEM).The results indicated that the melittin had a marked bacteriostatic effect on the four pathogenic bacteria.Among these,E.cacotowora was influenced most powerfully and quickly,the yeast and F.fulva were the second,and the S.aureus was inhibited by a low concentration but was killed by a high concentration.It was observed in the experiments that melittin killed pathogenic bacteria in three ways.One was by pore formation.After integrating melittin into the plasma membrane,a vacuole was formed then penetrated,resulting in bacterial content leakage.The vacuole also experienced plasmolysis and the growing cavity destroyed the membrane.A third effect was the formation of vacuoles in the cells which induced the pycnosis of the cytoplasm resulting in a cell death.The mechanism of melittin bacteriostasis was the result of integrating melittin with phospholipod double layers of the plasmalemma and the endomembranes.展开更多
基金Supported by János Bólyai Research Scholarship of Hungarian Academy of Sciences,No.BO/00426/11University of Debrecen and Research Grant of National Research,No.RH/885/2013Development and Innovation Office,No.K115818/2015/1
文摘AIM To evaluate the diagnostic and prognostic value of presepsin in cirrhosis-associated bacterial infections. METHODS Two hundred and sixteen patients with cirrhosis were enrolled. At admission, the presence of bacterial infections and level of plasma presepsin, serum C-reactive protein(CRP) and procalcitonin(PCT) were evaluated. Patients were followed for three months to assess the possible association between presepsin level and short-term mortality.RESULTS Present 34.7 of patients had bacterial infection. Presepsin levels were significantly higher in patients with infection than without(median, 1002 pg/m L vs 477 pg/m L, P < 0.001), increasing with the severity of infection [organ failure(OF): Yes vs No, 2358 pg/m L vs 710 pg/m L, P < 0.001]. Diagnostic accuracy of presepsin for severe infections was similar to PCT and superior to CRP(AUC-ROC: 0.85, 0.85 and 0.66, respectively, P = NS for presepsin vs PCT and P < 0.01 for presepsin vs CRP). At the optimal cut-off value of presepsin > 1206 pg/m L sensitivity, specificity, positive predictive values and negative predictive values were as follows: 87.5%, 74.5%, 61.8% and 92.7%. The accuracy of presepsin, however, decreased in advanced stage of the disease or in the presence of renal failure, most probably because of the significantly elevated presepsin levels in non-infected patients. 28-d mortality rate was higher among patients with > 1277 pg/m L compared to those with ≤ 1277 pg/m L(46.9% vs 11.6%, P < 0.001). In a binary logistic regression analysis, however, only PCT(OR = 1.81, 95%CI: 1.09-3.01, P = 0.022) but neither presepsin nor CRP were independent risk factor for 28-d mortality after adjusting with MELD score and leukocyte count.CONCLUSION Presepsin is a valuable new biomarker for defining severe infections in cirrhosis, proving same efficacy as PCT. However, it is not a useful marker of short-term mortality.
基金Funded by the Scientific Research Foundation of the Third Military Medical University.
文摘This study is conducted to clone the cDNA encoding human TNF-related apoptosis-inducing ligand (hTRAIL) extracellular region (amino acids 41-281, hTRAIL41-281) and to express it in E.coli. The hTRAIL41-281 cDNA is amplified by reverse transcription (RT) PCR from total RNA derived from human acute promyelocytic leukemia cell line HL-60. After sequenced, the cDNA is cloned into the vector pQE-80L and transformed into E.coli DH5 to express the recombinant hTRAIL41-281 (rhTRAIL41-281) induced by IPTG. The recombinant protein is analyzed by SDS-PAGE. The cloned cDNA is consistent with the cDNA sequence encoding hTRAIL41-281 reported in GenBankTM. After inducing, the hTRAIL41-281 protein is expressed, and the mass of the recombinant protein is about 30 % of total bacteria protein, which demonstrates that the cDNA encoding hTRAIL41-281 is successfully cloned and expressed in E.coli.
文摘The effects of melittin on growth and bacteriostasis of four pathogens were extensively investigated using scanning electron microscopy(SEM) and transmission electron microscopy(TEM).The results indicated that the melittin had a marked bacteriostatic effect on the four pathogenic bacteria.Among these,E.cacotowora was influenced most powerfully and quickly,the yeast and F.fulva were the second,and the S.aureus was inhibited by a low concentration but was killed by a high concentration.It was observed in the experiments that melittin killed pathogenic bacteria in three ways.One was by pore formation.After integrating melittin into the plasma membrane,a vacuole was formed then penetrated,resulting in bacterial content leakage.The vacuole also experienced plasmolysis and the growing cavity destroyed the membrane.A third effect was the formation of vacuoles in the cells which induced the pycnosis of the cytoplasm resulting in a cell death.The mechanism of melittin bacteriostasis was the result of integrating melittin with phospholipod double layers of the plasmalemma and the endomembranes.
