Mammalian glucose transporters: intracellular signalling and transporter translocation

Arbuckle, Margaret I.; Brant, Alison M.; Campbell, Ian W; Jess, Thomas J.; Kane, Susan E.; Livingstone, Callum; Martin, Sally; Merrall, Nicola W.; Porter, Lisa M.; Reid, Andrea L.; Seatter, Michael J.; Plevin, Robin; Gould, Gwyn W.

doi:10.1042/bst0220664

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“…The rapid activation of glucose transport by IGF-I implied a n enhanced uptake due to transporter activation or recruitment of transporters, rather than to synthesis of new transporter molecules. Previous studies in various cell types have shown that activation of the IGF type 1 receptor leads to translocation of GLUT4 as well as GLUTl (Yang et al, 1992;Arbuckle et al, 1994). The present observation that IGF-I caused a small but significant redistribution of GLUTl from the light microsomes to a plasma membrane-enriched fraction suggested that translocation of GLUTl a t least partially accounted for the hormone-induced doubling in transport of glucose also in BCC.…”

Section: Discussionsupporting

confidence: 48%

“…GLUTl, first identified in erythrocytes, appears on the other hand to be widely distributed and probably accounts for basal uptake of glucose in most tissues. Insulin as well as IGF-I have also been reported to enhance glucose transport in various cell lines by a similar translocation of GLUT1, although the effect is far less striking than for GLUT4 (Yang et al, 1992;Arbuckle et al, 1994).…”

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confidence: 99%

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GLUT1-mediated glucose transport and its regulation by IGF-I in cultured bovine chromaffin cells

1996

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Regulation of glucose transport was studied in primary cultures of bovine chromaffin cells (BCC) using the glucose analogue 2-deoxyglucose (DOG) as a model substrate. The glucose transporter in freshly isolated and cultured BCC was identified as GLUT1 by Western immunoblots. The level of GLUT1 increased by time in culture and was followed by an enhancement in uptake of DOG. The DOG uptake was stimulated by insulin-like growth factor I (IGF-I) with an EC50 of 1 nM and a maximal response (approximately 2-fold) was obtained at 10-100 nM IGF-I. Insulin was at least 100-fold less potent than IGF-I. Exposure to 10(-8) M IGF-I also caused a redistribution of GLUT1 from an intracellular compartment to a plasma membrane-enriched fraction. Our results demonstrate a GLUT1-mediated glucose uptake in adrenomedullary cells. An enhanced glucose transport in response to IGF-I appears to be coupled to activation of IGF receptor type 1 and GLUT1 translocation.

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Section: Discussionsupporting

confidence: 48%

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confidence: 99%