 |
|
EGFP-conjugated GLUT1 ligand
|
Description:
The only detection of extra facial domain of GLUT1 on mammalian cells.
Glucose transport, as mediated by the members of the closely related glucose transporters (GLUT), plays an essential role in normal and pathological cellular metabolism. GLUT1 is the most widely expressed isoform of the known glucose transporters and the primary glucose transporter across the blood-brain barrier (1). High levels of GLUT1 expression on tumors have been associated with worse prognosis in different types of cancers, including breast and gastric carcinoma (2,3). Also, recent investigations have shown that GLUT1 mediates the transport of some glycosylated neuroactive peptidic drugs designed to cross the blood-brain barrier (4).
The recent identification of the receptor binding domain of the human T cell leukemia virus (HTLV) envelope glycoprotein (HRBD) that is necessary and sufficient to bind GLUT1 (5,6) has allowed the development of an HRBD derived peptide coupled with EGFP (EGFP-GLUT1 ligand).
EGFP-GLUT1 ligand has been shown to bind the carboxy terminal extracellular loop of GLUT1 (7) and has allowed GLUT1 expression to be monitored at the plasma membrane of all mammalian cell lines by FACS analyses or fluorescence staining (8). EGFP-GLUT1 ligand has facilitated studies of GLUT1 expression during T cell activation (9) and has been critical for the successful identification of an immature CD4+CD8+ human thymocyte population with high metabolic activity (10). Assessment of GLUT1 expression via binding of EGFP-GLUT1 ligand correlates with increased glucose uptake, as observed in malignant cancer cells or metabolically active cells (see fig 3). EGFP-GLUT1 ligand can provide insights, as a qualitative and quantitative marker, into the molecular bases of both normal and disordered glucose homeostasis.
 |  |  |  |
References :
1. Hruz PW, Mueckler MM. (2001), Mol Membr Biol., 18:183-93.
2. Kang SS et al. (2002), Jpn J Cancer Res., 93:1123-8.
3. Kawamura et al. (2001), Cancer 92:634-41.
4. Guo X, Geng M, Du G. (2005), Biochem Genet., 43:175-87.
5. Manel N, Kim FJ, Kinet S, Taylor N, Sitbon M, Battini JL. (2003), Cell., 115:449-59.
6. Kim FJ, Manel N, Garrido EN, Valle C, Sitbon M, Battini JL. (2004), Retrovirology, 1:41
7. Manel N, Battini JL, Sitbon M. (2005), J Biol Chem (280):29025-9
8. Manel N, Battini JL, Taylor N, Sitbon M. (2005), Oncogene, (39):6016-25.
9. Manel N, Kinet S, Battini JL, Kim FJ,Taylor N, Sitbon M. (2003), Blood., 101:1913-18.
10. Swainson L, Kinet S, Manel N, Battini JL, Sitbon M, Taylor N. (2005), Proc Natl Acad Sci U S A., 102: 12867-72.
|  |  |  |  | |  |