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Research Article |
1 School of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2
9JT, UK
2 Centro de Estudios Científicos CECS, Casilla 1469, Valdivia,
Chile
3 Biochemistry Department, Dundee University, Dundee DD1 5EH, Scotland, UK
4 Cellular Stress Group, MRC Clinical Sciences Centre, Imperial College School
of Medicine, Hammersmith Hospital, London W12 0NN, UK
5 U465 INSERM, Centre de Recherches Biomédical des Cordeliers, 75270
Paris Cedex 06, France
* Author for correspondence (e-mail: K.Barnes{at}leeds.ac.uk )
Accepted 18 March 2002
In the rat liver epithelial cell line Clone 9, the Vmax for
glucose uptake is actuely increased by inhibition of oxidative phosphorylation
and by osmotic stress. By using a membrane-impermeant photoaffinity labelling
reagent together with an isoform-specific antibody, we have, for the first
time, provided direct evidence for the involvement of the GLUT1 glucose
transporter isoform in this response. Transport stimulation was found to be
associated with enhanced accessibility of GLUT1 to its substrate and with
photolabelling of formerly `cryptic' exofacial substrate binding sites in
GLUT1 molecules. The total amount of cell surface GLUT1 remained constant. The
precise mechanism for this binding site `unmasking' is unclear but appears to
involve AMP-activated protein kinase: in the current study, osmotic and
metabolic stresses were found to result in activation of the 
1 isoform
of AMP-activated protein kinase, and transport stimulation could be mimicked
both by 5-aminoimidazole-4-carboxamide ribonucleoside and by infection of
cells with a recombinant adenovirus encoding constitutively active
AMP-activated protein kinase. The effect of 5-aminoimidazole-4-carboxamide
ribonucleoside, as for metabolic stress, was on the Vmax rather
than on the Km for transport and did not affect the cell-surface
concentration of GLUT1. The relevant downstream target(s) of AMP-activated
protein kinase have not yet been identified, but stimulation of transport by
inhibition of oxidative phosphorylation or by 5-aminoimidazole-4-carboxamide
ribonucleoside was not prevented by either inhibitors of conventional and
novel protein kinase C isoforms or inhibitors of nitric oxide synthase. These
enzymes, which have been implicated in stress-regulated pathways in other cell
types, are therefore unlikely to play a role in transport regulation by stress
in Clone 9 cells.
Key words: Glucose, Transport, GLUT1, Stress, AMP-activated protein kinase
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