The use of automated real-time feedback devices to improve quality during CPR training and real CPR performance: a systematic review

High quality cardiopulmonary resuscitation (CPR) is imperative to improve patient outcome after a cardiac arrest. However, it has been demonstrated that CPR quality is normally of suboptimal quality in both real-life resuscitation attempts or simulated training. Automated real-time feedback (ARTF) devices have been considered a potential tool to improve the quality of CPR and maximise retention of the skills. Although previous studies have supported the usefulness of such devices during training, others have conflicting conclusions with regards to its efficacy during real-life CPR. This systematic review of the literature aims to assess the effectiveness of ARTF for improving CPR performance during simulated training and real-life resuscitation in the adult and paediatric population. Following PRISMA (Preferred Reporting Items for Systematic Reviews and Meta-Analyses) guidelines [1], articles published between January 2010 and November 2019 were searched from 7 electronic databases (SCIELO, LILACS, BVS, PubMed, Web of Science, Embase, Cochrane, Cinahl, Google Scholar) and reviewed according to the pre-defined eligibility criteria. CPR performance quality was assessed based on guideline compliance for chest compression rate, chest compression depth and complete chest recoil. 871 studies were found and 32 studies met inclusion criteria. 14 randomised controlled trials (RCTs), 08 randomised trials (RTs) and 10 randomised cross-over trials (RCOTs). Each study used ARTF devices during CPR training or real CPR to analyse the performance of healthcare professionals for paediatric or adult population. According to the studies, the use of ARTF devices enhances CPR performance in terms of achieving the recommended chest compression rate, depth and recoil. Based on the results of the studies analysed in this review, the use of ARTF can significantly help improve CPR performance during training of healthcare professionals. Further research is needed to reach the same conclusion for real-life CPR

A negative screen for mutations in calstabin 1 and 2 genes in patients with dilated cardiomyopathy

<p>Abstract</p> <p>Background</p> <p>Calstabins 1 and 2 bind to Ryanodine receptors regulating muscle excitation-contraction coupling. Mutations in Ryanodine receptors affecting their interaction with calstabins lead to different cardiac pathologies. Animal studies suggest the involvement of calstabins with dilated cardiomyopathy.</p> <p>Results</p> <p>We tested the hypothesis that calstabins mutations may cause dilated cardiomyopathy in humans screening 186 patients with idiopathic dilated cardiomyopathy for genetic alterations in calstabins 1 and 2 genes (<it>FKBP12 </it>and <it>FKBP12.6)</it>. No missense variant was found. Five no-coding variations were found but not related to the disease.</p> <p>Conclusions</p> <p>These data corroborate other studies suggesting that mutations in <it>FKBP12 </it>and <it>FKBP12.6 </it>genes are not commonly related to cardiac diseases.</p

The effects of over-expression of the FK506-binding protein FKBP12.6 on K+ currents in adult rabbit ventricular myocytes

This study examines the effects of the intracellular protein FKBP12.6 on action potential and associated K+ currents in isolated adult rabbit ventricular cardiomyocytes. FKBP12.6 was over-expressed by ~6 times using a recombinant adenovirus coding for human FKBP12.6. This over-expression caused prolongation of action potential duration (APD) by ~30%. The amplitude of the transient outward current (Ito) was unchanged, but rate of inactivation at potentials positive to +40 mV was increased. FKBP12.6 over-expression decreased the amplitude of the inward rectifier current (IK1) by ~25% in the voltage range −70 to −30 mV, an effect prevented by FK506 or lowering intracellular [Ca2+] below 1 nM. Over-expression of an FKBP12.6 mutant, which cannot bind calcineurin, prolonged APD and affected Ito and IK1 in a similar manner to wild-type protein. These data suggest that FKBP12.6 can modulate APD via changes in IK1 independently of calcineurin binding, suggesting that FKBP12.6 may affect APD by direct interaction with IK1