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Matthew Beard

Publications and source records attributed to Matthew Beard.

4 recordsLinked to original sources

Cell-based assays using primary endothelial cells to study multiple steps in inflammation.

Cell-based assays are powerful tools for drug discovery and provide insight into complex signal transduction pathways in higher eukaryotic cells. Information gleaned from assays that monitor a cellular phenotype can be used to elucidate the details of a single pathway and to establish patterns of cross talk between pathways. By selecting the appropriate cell model, cell-based assays can be used to understand the function of a specific cell type in a complex disease process such as inflammation. We have used human umbilical vein endothelial cells to establish three cell-based, phenotypic assays that query different stages of a major signaling pathway activated in inflammation. One assay analyzes the tumor necrosis factor alpha (TNFalpha)-induced translocation of the transcription factor NF-kappaB from the cytoplasm into the nucleus 20 min after stimulation with TNFalpha. Two more assays monitor the expression of E-selectin and VCAM-1, 4 and 24 h after stimulation with TNFalpha. Indirect immunofluorescence and high-throughput automated microscopy were used to analyze cells. Imaging was performed with the IN Cell Analyzer 3000. All assays proved to be highly robust. Z' values between 0.7 and 0.8 make each of the three assays well suited for use in high-throughput screening for drug or probe discovery.

Animals↗

A cryptic Rab1-binding site in the p115 tethering protein.

Small GTPases and coiled-coil proteins of the golgin family help to tether COPI vesicles to Golgi membranes. At the cis-side of the Golgi, the Rab1 GTPase binds directly to each of three coiled-coil proteins: p115, GM130, and as now shown, Giantin. Rab1 binds to a coiled-coil region within the tail domain of p115 and this binding is inhibited by the C-terminal, acidic domain of p115. Furthermore, GM130 and Giantin bind to the acidic domain of p115 and stimulate p115 binding to Rab1, suggesting that p115 binding to Rab1 is regulated. Regulation of this interaction by proteins such as GM130 and Giantin may control the membrane recruitment of p115 by Rab1.

Animals↗

Preparation and characterization of recombinant golgin tethers.

Golgin tethers are integral or peripheral Golgi proteins with predicted coiled-coil domains and many are known to interact directly with small GTPases of the Ypt/Rab or Arl families. Here we describe the preparation of recombinant golgins: GM130, p115 (and truncations thereof), the N-terminal fragment of giantin, CASP, and golgin-84.

Animals↗

On the constructs of quality physiotherapy.

The quality of physiotherapy services invites evaluation using a range of constructs. These must reflect the needs of different stakeholders and the different elements of the "package" of physiotherapy. Measurement of quality can consider organisation of the service, the way in which care is provided, the way in which information about care is recorded and used for evaluation purposes, and the outcome of care. A clear understanding of the elements of quality is essential for physiotherapists to be competitive by providing consistently effective services.

Journal Article↗