29 research outputs found
National adoption of video-assisted thoracoscopic surgery (VATS) lobectomy: The Italian VATS register evaluation
Conversion due to vascular injury during video-assisted thoracic surgery lobectomy: A multicentre retrospective analysis from the Italian video-assisted thoracic surgery group registry
Are antifibrinolytic drugs equivalent in reducing blood loss and transfusion in cardiac surgery? A meta-analysis of randomized head-to-head trials
BACKGROUND: Aprotinin has been shown to be effective in reducing peri-operative blood loss and the need for re-operation due to continued bleeding in cardiac surgery. The lysine analogues tranexamic acid (TXA) and epsilon aminocaproic acid (EACA) are cheaper, but it is not known if they are as effective as aprotinin. METHODS: Studies were identified by searching electronic databases and bibliographies of published articles. Data from head-to-head trials were pooled using a conventional (Cochrane) meta-analytic approach and a Bayesian approach which estimated the posterior probability of TXA and EACA being equivalent to aprotinin; we used as a non-inferiority boundary a 20% increase in the rates of transfusion or re-operation because of bleeding. RESULTS: Peri-operative blood loss was significantly greater with TXA and EACA than with aprotinin: weighted mean differences were 106 mls (95% CI 37 to 227 mls) and 185 mls (95% CI 134 to 235 mls) respectively. The pooled relative risks (RR) of receiving an allogeneic red blood cell (RBC) transfusion with TXA and EACA, compared with aprotinin, were 1.08 (95% CI 0.88 to 1.32) and 1.14 (95% CI 0.84 to 1.55) respectively. The equivalent Bayesian posterior mean relative risks were 1.15 (95% Bayesian Credible Interval [BCI] 0.90 to 1.68) and 1.21 (95% BCI 0.79 to 1.82) respectively. For transfusion, using a 20% non-inferiority boundary, the posterior probabilities of TXA and EACA being non-inferior to aprotinin were 0.82 and 0.76 respectively. For re-operation the Cochrane RR for TXA vs. aprotinin was 0.98 (95% CI 0.51 to 1.88), compared with a posterior mean Bayesian RR of 0.63 (95% BCI 0.16 to 1.46). The posterior probability of TXA being non-inferior to aprotinin was 0.92, but this was sensitive to the inclusion of one small trial. CONCLUSION: The available data are conflicting regarding the equivalence of lysine analogues and aprotinin in reducing peri-operative bleeding, transfusion and the need for re-operation. Decisions are sensitive to the choice of clinical outcome and non-inferiority boundary. The data are an uncertain basis for replacing aprotinin with the cheaper lysine analogues in clinical practice. Progress has been hampered by small trials and failure to study clinically relevant outcomes
Effects of n-acetyl-cysteine, taurine, and oxerutin on the glomerular lesions of long-term experimental diabetes Mellitus
La formazione di addotti tra aldeidi lipoperossidative e proteine può causare danno ossidativo
Giornale di Gerontologia, Vol LII, Numero S5, p A68, Ottobre 200
Malondialdehyde, a lipoperoxidation-derived aldehyde, can bring about secondary oxidative damage to proteins
Lipoperoxidation-derived aldehydes, for example malondialdehyde (MDA), can damage
proteins by generating covalent adducts whose accumulation probably participates
in tissue damage during aging. However, the mechanisms of adduct formation and
their stability are scarcely known. This article investigates whether oxidative
steps are involved in the process. As a model of the process, the interaction
between MDA and bovine serum albumin (BSA) was analyzed. Incubation of BSA with
MDA resulted in rapid quenching of tryptophan fluorescence and appearance of MDA
protein adduct fluorescence; transition metal ion traces interfered with the
latter process. MDA induced generation of peroxides in BSA, which was preventable
with the antioxidant 2,6,-di-tert-butyl-4-methylphenol (BHT). MDA-exposed BSA
underwent aggregation, degradation, and BHT-sensitive "gel retardation" effects.
Phycoerythrin fluorescence disappearance, a marker of damage mediated by reactive
oxygen species, indicated synergism between MDA and metal ions. The interaction
between reactive aldehydes and proteins is likely to occur in several steps, some
of them oxidative in nature, giving rise to advanced lipoperoxidation
end-products, which could participate, with advanced glycation end-products, in
the generation of tissue damage during aging