Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Mohsen Lachaal"'
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1466(1-2):379-389
GLUT2, the major facilitative glucose transporter isoform expressed in hepatocytes, pancreatic β-cells, and absorptive epithelial cells, is unique not only with its low affinity and broad substrate specificity as a glucose transporter, but also with
Publikováno v:
Journal of Biological Chemistry. 271:5225-5230
We synthesized a transportable diazirine derivative of D-glucose, 3-deoxy-3,3-azi-D-glucopyranose (3-DAG), and studied its interaction with purified human erythrocyte facilitative glucose transporter, GLUT1. 3-DAG was rapidly transported into human e
Publikováno v:
Experimental & Molecular Medicine. 28:33-40
Effects of cadmium on glucose transport in rat adipocytes and human erythrocytes: stimulation of GLUT1 catalytic activity
Publikováno v:
Biochemistry. 35:14958-14962
Cadmium stimulates glucose transport in fibroblasts, apparently by increasing the intrinsic activity of GLUT1 [Harrison, S.A., Buxton, J.M., Clancy, B.M.,Czech, M.P. (1991) J. Biol. Chem. 266, 19438-19449]. In the present study, we examined whether c
Publikováno v:
Journal of Biological Chemistry. 270:7869-7875
We have identified a 70-kDa cytosolic protein (GTBP70) in rat adipocytes that binds to glutathione S-transferase fusion proteins corresponding to the cytoplasmic domains of the facilitative glucose transporter isoforms Glut1, Glut2, and Glut4. GTBP70
Publikováno v:
Journal of Biological Chemistry. 269:23689-23693
GLUT4, the major insulin-responsive glucose transporter isoform in rat adipocytes, rapidly recycles between an intracellular pool and the plasma membrane in the basal and insulin-stimulated states. To gain insight into the route of this GLUT4 recycli
Publikováno v:
Journal of Biological Chemistry. 267:17710-17715
We labeled rat adipocyte cell surface glucose transporters with an impermeable, photoreactive glucose analogue, 1,3-bis-(3-deoxy-D-glucopyranose-3-yloxy)-2-propyl 4-benzoylbenzoate (B3GL) and its radioactive tracer [3H]B3GL. The labeling did not affe
Publikováno v:
Journal of Biological Chemistry. 265:15449-15454
Glyceraldehyde-3-phosphate dehydrogenase was found to bind in vitro to purified, human erythrocyte glucose transporter reconstituted into vesicles. Mild tryptic digestion of the glucose transporter totally inactivated the binding, suggesting that the
Publikováno v:
Biochimica et biophysica acta. 1511(1)
Evidence indicates that a large portion of the facilitative glucose transporter isoform GLUT1 in certain animal cells is kept inactive and activated in response to acute metabolic stresses. A reversible interaction of a certain inhibitor molecule wit
Publikováno v:
Archives of biochemistry and biophysics. 363(2)
Evidence indicates that the carboxy-terminal cytoplasmic domain of glucose transporter 4 (GLUT4) is important for the regulation of GLUT4 in muscle and adipocytes. We cloned from a human skeletal muscle cDNA library a 34-kDa protein which interacts w