Zobrazeno 1 - 10
of 235
pro vyhledávání: '"M, Mueckler"'
Autor:
Mike M. Mueckler
Publikováno v:
Red Blood Cell Membranes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5f9b42a85909a7b37cb349b0a2f6eb3
https://doi.org/10.1201/9781003066118-2
https://doi.org/10.1201/9781003066118-2
Akademický článek
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Autor:
K H Moley, M M Mueckler
Publikováno v:
APOPTOSIS. 5:99-105
The transport and metabolism of glucose modify programmed cell death in a number of different cell types. This review presents three cell death paradigms that link a decrease in glucose transport to apoptosis. Although these pathways overlap, the glu
Autor:
David W. Rose, M. Mueckler, Tetsuro Haruta, Aaron J. Morris, James G. Nelson, Jerrold M. Olefsky, Peter Vollenweider
Publikováno v:
Endocrinology. 139:358-364
To delineate the signaling pathway leading to glucose transport protein (GLUT4) translocation, we examined the effect of microinjection of the nonhydrolyzable GTP analog, guanosine 5′-O-(3-thiotriphosphate) (GTPγS), into 3T3-L1 adipocytes. Thirty
Publikováno v:
The Journal of Cell Biology
The GLUT4 glucose transporter appears to be targeted to a unique insulin-sensitive intracellular membrane compartment in fat and muscle cells. Insulin stimulates glucose transport in these cell types by mediating the partial redistribution of GLUT4 f
Publikováno v:
Journal of Clinical Investigation. 95:429-432
The effect of increased Glut4 protein expression in muscle and fat on the whole body glucose metabolism has been evaluated by the euglycemic hyperinsulinemic clamp technique in conscious mice. Fed and fasting plasma glucose concentrations were 172 +/
Publikováno v:
Journal of Biological Chemistry. 269:32110-32119
The rate of movement of the glucose transporter isoforms Glut1 and Glut4 from the endoplasmic reticulum (ER) to the Golgi apparatus was investigated by pulse labeling and monitoring endoglycosidase H resistance in mRNA-injected Xenopus oocytes and in
Publikováno v:
Journal of Biological Chemistry. 269:20533-20538
The possible role of 5 transmembrane amino acid residues in the function of the Glut1 glucose transporter was investigated by site-directed mutagenesis. The residues were chosen based on their containing hydroxyl or amide side chains capable of hydro
Publikováno v:
Journal of Biological Chemistry. 269:20482-20488
The erythrocyte glucose transporter (Glut 1) is predicted to contain 12 membrane-spanning domains based on the hydropathy plot of its deduced amino acid sequence. The membrane topology of Glut 1 was analyzed by a scanning mutagenesis procedure in whi
Autor:
E. A. Gulve, M. Mueckler, Jian-Ming Ren, Bess A. Marshall, Jiaping Gao, John O. Holloszy, Polly A. Hansen
Publikováno v:
Journal of Biological Chemistry. 269:18366-18370
Glucose transport activity was examined in transgenic mice overexpressing the human GLUT1 glucose transporter in skeletal muscles. Basal transport activity measured in vitro with the glucose analog 2-deoxy-D-glucose (1 mM) was increased 2-8-fold in f