Titlebook: Glucose Transport; Methods and Protocol Karin Lindkvist-Petersson,Jesper S‘Hansen Book 2018 Springer Science+Business Media LLC 2018 GLUTs.

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Crystallization and Structural Determination of the Human Glucose Transporters GLUT1 and GLUT3,hapter, we present the detailed protocols of recombinant protein expression, purification, and crystallization of GLUT1 and GLUT3, which may help the pursuit of structural elucidation of other eukaryotic membrane proteins.

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Evaluating the Efficacy of GLUT Inhibitors Using a Seahorse Extracellular Flux Analyzer, Seahorse bioenergetics analyzer can measure both the oxygen consumption rate (OCR) and extracellular acidification rate (ECAR). The proposed methodology affords a robust, high-throughput method to screen for GLUT inhibition in cells engineered to express specific GLUTs, providing live cell read-outs upon GLUT inhibition.

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Design, Synthesis, and Evaluation of GLUT Inhibitors,estrogen receptor (ER) ligands, which were structurally optimized in order to direct their activity towards GLUT1 and to minimize their binding to the ERs, leading to the production of efficient and selective inhibitors of glucose uptake in cancer cells.

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GLUT4 Translocation in Single Muscle Cells in Culture: Epitope Detection by Immunofluorescence,ocal fluorescence microscopy to quantify cell surface GLUT4. or GLUT4.-GFP in cells co-transfected with diverse cDNA constructs, treated with siRNAs, or co-stained with antibodies for other proteins of interest. Herein, we describe the methodology to perform these experimental approaches in insulin-stimulated L6 muscle cells.

昏迷狀態(tài)

Proximity Ligation Assay to Study the GLUT4 Membrane Trafficking Machinery,lex and/or with the SNARE proteins individually. Studying the interactions that occur between SNARE proteins themselves and also with Munc18c in insulin-responsive cells is critical to further understand SNARE protein function and GLUT4 trafficking mechanism in general.

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Tracking GLUT2 Translocation by Live-Cell Imaging,uantify GLUT2 translocation, and its dynamics, by live imaging of a mCherry-hGLUT2 fusion protein in polarized epithelial cells. This system enables testing of putative modulators of GLUT2 translocation, which are potential drugs for conditions of impaired glucose homeostasis and associated nephropathy.

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https://doi.org/10.1007/978-1-349-07793-9itated by fluorescence-based screening approaches. We describe (1) the strategy and protocol of cloning by homologous recombination, (2) whole-cell and in-gel fluorescence measurements to estimate GLUT-GFP fusion protein yields, (3) use of size-exclusion chromatography monitored by fluorescence (FSE

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https://doi.org/10.1007/978-3-319-68072-9rovide a detailed protocol on oocyte extraction and preparation for GLUT9 protein expression. Furthermore, we describe the determination of GLUT9 overexpression level by biotinylation and Western blotting analysis. Finally, we also describe how GLUT9-expressing oocytes can be used to measure urate k