Association of prealbumin levels with contrast-induced acute kidney injury in elderly patients with elective percutaneous coronary intervention.

PURPOSE: Inflammatory factors play a critical role in contrast-induced acute kidney injury (CI-AKI). Prealbumin, a nutritional and inflammatory indicator, is a well-established predictor of short- and long-term outcomes in numerous clinical conditions. The current study investigated the association of pre-procedural prealbumin levels with CI-AKI and long-term outcomes in geriatric patients after elective percutaneous coronary intervention (PCI). PATIENTS AND METHODS: A total of 558 patients aged≥75 years, who underwent elective PCI between January 2012 and December 2015, were selected for the current study. Pre-procedural prealbumin levels were measured before PCI. Multivariable logistic regression and Cox proportional hazard regression analyses were performed to identify the independent risk factors for CI-AKI and long-term mortality. RESULTS: Out of 558 patients, 54 developed CI-AKI. The optimal cutoff value of prealbumin for detecting CI-AKI was 185.5 mg/L with 62.7% sensitivity and 70.4% specificity based on the receiver operating characteristic analysis (C-statistic=0.710; 95% confidence interval [CI] 0.673-0.751). Multivariable analysis demonstrated that prealbumin≤185.5 mg/L was significantly associated with CI-AKI (odds ratio [OR] 0.397; 95% CI 0.195-0.808; P=0.011). Cox regression analysis demonstrated that prealbumin≤185.5 mg/L was associated with long-term mortality (adjusted hazard ratio [HR] 0.525; 95% CI 0.289-0.952; P=0.034) during the follow-up. CONCLUSION: Pre-procedural levels of prealbumin were independently associated with an increased risk of CI-AKI and long-term mortality in elderly patients undergoing elective PCI.

[Screening for peptides of anti-rotavirus by phage-displayed technique].

In this study, a 15-mer phage display peptide library was employed to pan against human rotavirus immobilized on solid phase. 4 different peptides were selected and could bind with rotavirus particles specifically. Plaque reduction neutralization test and MTT analysis results indicated that 3 of the peptides can inhibit rotavirus infecting in vitro. A peptide which sequence is QSNPIHIITNTRNHP showed the best efficiency--93% neutralization infectivity. Two other peptides, A and B, showed 40% and 50% neutralization infectivity respectively. Amino sequence analysis results indicate the 3 peptides containing 2 conserved motifs: SNPIHII and NIP. No putative trypsin hydrolysis site was found in C peptide, however, 4 and 3 potential sites were found in A and B peptides respectively. Using trypsin inhibitor, both A and B peptides showed the similar antiviral effect as that of C peptide. It suggests that the intactness of the 2 conserved motifs play an important role in counteracting virus infection. According to the results of this study, peptide C is hopeful to be exploited as an antiviral peptide drug.