Results from the Adverse Event Sedation Reporting Tool: A Global Anthology of 7952 Records Derived from >160,000 Procedural Sedation Encounters.

: The incidence of sedation-related adverse events, inclusive of both adults and children, administered by multiple specialty providers from different countries and venues, using standardized definitions, has never been reported on an international level. We are reporting the outcome data of the adverse event sedation reporting tool as an important step toward a more complete risk assessment of sedation-related morbidity, mortality, and etiology. The analysis of the AE sedation reporting data include descriptive measures to evaluate the characteristics of the provider, the patient, sedations performed, adverse events, interventions, and outcomes.

Mutation of conserved residues in transmembrane domains 4,6 and 8 causes loss of Ca2+ transport by the plasma membrane Ca2+ pump.

Mutants of the plasma membrane Ca2+ pump (PMCA), in which amino acids in transmembrane domains (TM) 4, 6, and 8 had been replaced, have been expressed in COS-7 cells. They were analyzed functionally by measuring the uptake of Ca2+ in microsomal preparations and by following the formation of the phosphorylated intermediate from ATP and from phosphate. The mutated residues corresponded to amino acids whose mutation in the sarcoplasmic reticulum pump (SERCA) caused loss of Ca2+ transport by the pump protein: however, only four of the six SERCA residues were conserved in the PMCA pump.

A signal for endoplasmic reticulum retention located at the carboxyl terminus of the plasma membrane Ca(2+)-ATPase isoform 4CI.

The plasma membrane Ca(2+)-ATPase isoform 4b (PMCA4CI) with truncations in the cytoplasmically exposed COOH-terminal tail was expressed in COS and HeLa cells and in Sf9 cells using the baculovirus system. The truncated protein terminating with the acidic sequence Glu1067-Arg1087 was retained within the endoplasmic reticulum (ER), whereas mutants lacking this sequence or having it at a distance from the COOH terminus were delivered to the plasma membrane. Although the truncated protein retained in the endoplasmic reticulum was still able to form a Ca(2+)-dependent phosphoenzyme, it underwent partial degradation.