Evidence of two mechanisms for the activation of the glucose transporter GLUT1 by anisomycin: p38(MAP kinase) activation and protein synthesis inhibition in mammalian cells
Author
dc.contributor.author
Barros, Luis Felipe
Author
dc.contributor.author
Young, Michelle
Author
dc.contributor.author
Saklatvala, Jeremy
Author
dc.contributor.author
Baldwin, Stephen A.
Admission date
dc.date.accessioned
2019-01-29T15:54:58Z
Available date
dc.date.available
2019-01-29T15:54:58Z
Publication date
dc.date.issued
1997
Cita de ítem
dc.identifier.citation
Journal of Physiology, Volumen 504, Issue 3, 2018, Pages 517-525
Identifier
dc.identifier.issn
00223751
Identifier
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10.1111/j.1469-7793.1997.517bd.x
Identifier
dc.identifier.uri
https://repositorio.uchile.cl/handle/2250/162748
Abstract
dc.description.abstract
1. Inhibitors of protein synthesis stimulate sugar transport in mammalian cells through activation of plasma membrane GLUT1, the housekeeping isoform of the glucose transporter. However, it has been reported that some of these compounds, in addition to their effect on protein synthesis, also activate protein kinases. 2. In the present study we have explored the role of these two effects on GLUT1 activation. In 3T3-L1 adipocytes and Clone 9 cells, stimulation of sugar transport by puromycin, a translational inhibitor that does not activate kinases, was not detectable until 90 min after exposure. In contrast, stimulation by anisomycin, a potent Jun-NH2-terminal kinase (JNK) agonist, exhibited no lag phase. An intermediate response was observed to emetine and cycloheximide, weak activators of JNK. 3. The potency of anisomycin to stimulate transport acutely (30 min of exposure) was 5- to 10-fold greater than for its chronic stimulation of transport, measured after 4 h of exposure. The stim
Evidence of two mechanisms for the activation of the glucose transporter GLUT1 by anisomycin: p38(MAP kinase) activation and protein synthesis inhibition in mammalian cells