Long-term care provision, hospital bed blocking, and discharge destination for hip fracture and stroke patients

We examine the relationship between long-term care supply (care-home beds and prices) and (i) the probability of being discharged to a care home and (ii) length of stay in hospital for patients admitted to hospital for hip fracture or stroke. Using patient level data from all English hospitals and allowing for a rich set of demographic and clinical factors, we find no association between discharge destination and long term care beds supply or prices. We do, however, find evidence of bed blocking: hospital length of stay for hip fracture patients discharged to a care home is shorter in areas with more long-term care beds and lower prices. Length of stay is over 30% shorter in areas in the highest quintile of care home beds supply compared to those in the lowest quintile

Amyloid-beta-induced degeneration of human brain pericytes is dependent on the apolipoprotein E genotype

Item does not contain fulltex

Role of Secretory Carrier Membrane Protein SCAMP2 in Granule Exocytosis

In secretory carrier membrane proteins (SCAMPs), the most conserved structural segment is between transmembrane spans 2 and 3, facing the cytosol. A synthetic peptide, CWYRPIYKAFR (E peptide), from this segment of SCAMP2 potently inhibits exocytosis in permeabilized neuroendocrine (PC12) cells. E peptide blocked discharge of (35)S-labeled secretogranin with the same structural selectivity and potency as observed for hexosaminidase secretion in mast cells. SCAMPs 1 and 2 are concentrated primarily on intracellular membranes in PC12 cells. Both, however, are found on plasma membranes, but neither is present on large dense-core vesicles. Yet, large dense-core vesicles marked by secretogranin attach to plasma membranes at foci containing SCAMP2 along with syntaxin1 and complexin at putative cell-surface docking/fusion sites. Regulated overexpression of SCAMP2 with point mutations in its E peptide but not of normal SCAMP2 caused dose-dependent inhibition of depolarization-induced secretion. The SCAMP2 mutants also inhibited secretion stimulated by elevated calcium. Inhibition was largely overcome by adding lysophosphatidylcholine to the medium at concentrations that do not otherwise affect secretion. Although overexpression of normal or mutant SCAMP2 slightly inhibits endocytosis, this effect does not appear to be related to the specific effect of the mutant SCAMP on stimulated exocytosis. Thus, SCAMP2 not only colocalizes with fusion sites but also appears to have an essential function in granule exocytosis through actions mediated by its E peptide–containing domain