Subject(s)
Education, Nursing, Baccalaureate/methods , Empathy , Motion Pictures/standards , Nurse-Patient Relations , Students, Nursing/psychology , Teaching Materials/standards , Teaching/methods , Attitude of Health Personnel , Communication , Guillain-Barre Syndrome/nursing , Guillain-Barre Syndrome/psychology , Humans , Nursing Education ResearchABSTRACT
Two hematopoietic-specific adapters, src homology 2 domain-containing leukocyte phosphoprotein of 76 kD (SLP-76) and linker for activation of T cells (LAT), are critical for T cell development and T cell receptor (TCR) signaling. Several studies have suggested that SLP-76 and LAT function coordinately to promote downstream signaling. In support of this hypothesis, we find that a fraction of SLP-76 localizes to glycolipid-enriched membrane microdomains (GEMs) after TCR stimulation. This recruitment of SLP-76 requires amino acids 224-244. The functional consequences of targeting SLP-76 to GEMs for TCR signaling are demonstrated using a LAT/SLP-76 chimeric protein. Expression of this construct reconstitutes TCR-inducted phospholipase Cgamma1 phosphorylation, extracellular signal-regulated kinase activation, and nuclear factor of activated T cells (NFAT) promoter activity in LAT-deficient Jurkat T cells (J.CaM2). Mutation of the chimeric construct precluding its recruitment to GEMs diminishes but does not eliminate its ability to support TCR signaling. Expression of a chimera that lacks SLP-76 amino acids 224-244 restores NFAT promoter activity, suggesting that if localized, SLP-76 does not require an association with Gads to promote T cell activation. In contrast, mutation of the protein tyrosine kinase phosphorylation sites of SLP-76 in the context of the LAT/SLP-76 chimera abolishes reconstitution of TCR function. Collectively, these experiments show that optimal TCR signaling relies on the compartmentalization of SLP-76 and that one critical function of LAT is to bring SLP-76 and its associated proteins to the membrane.
Subject(s)
Adaptor Proteins, Signal Transducing , Carrier Proteins/metabolism , Glycolipids/metabolism , Membrane Proteins/metabolism , Phosphoproteins/metabolism , Receptors, Antigen, T-Cell/metabolism , Signal Transduction , T-Lymphocytes/metabolism , Binding Sites , Carrier Proteins/genetics , Cell Membrane/metabolism , Humans , Jurkat Cells , Membrane Proteins/genetics , Phosphoproteins/genetics , Phosphorylation , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , T-Lymphocytes/cytology , Tyrosine/metabolism , src Homology DomainsABSTRACT
This article describes the evaluation of a commercial device designed to assess the performance of phototimers on x-ray systems. The device consists of a digital readout meter that can be connected to a radiographic or mammographic test cassette. Results showed that the device provided reproducible results with different x-ray generators and processors. The device can be used in acceptance testing and routine quality control inspections, as well as to calibrate or adjust phototimers.
