GLUT4 glucose transporter expression in rodent brain: effect of diabetes

Vannucci, Susan J.; Koehler-Stec, Ellen M.; Li, Kang; Reynolds, Thomas H.; Clark, Rebekah R.; Simpson, Ian A.

doi:10.1016/s0006-8993(98)00103-6

Cited by 174 publications

(121 citation statements)

References 24 publications

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“…GLUT1 can be readily detected in cultured neurons and is detected in vivo under conditions of stress such as following a hypoxic-ischemic insult (45,70,78,129,131). The presence of GLUT2 has been reported in neurons in the hypothalamus (7,8), and GLUT4 has been found in several subsets of neurons, including Purkinje and granule cells in cerebellum, principle and nonprinciple cells in the hippocampus, and isolated cells in the cortex and hypothalamus (5,7,12,67,72,106,126). Both GLUT6 and -8 have been reported to be present in neurons; however, as with GLUT4, both proteins contain a dileucine motif in their COOH termini and would appear to reside in intracellular membranes; GLUT8 may be recruited to the ER in the presence of insulin (see Ref.…”

Section: Neuronal Glut3 and Cerebral Glucose Utilizationmentioning

confidence: 99%

The facilitative glucose transporter GLUT3: 20 years of distinction

Simpson

Dwyer

Malide

et al. 2008

American Journal of Physiology-Endocrinology and Metabolism

395

322

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Glucose metabolism is vital to most mammalian cells, and the passage of glucose across cell membranes is facilitated by a family of integral membrane transporter proteins, the GLUTs. There are currently 14 members of the SLC2 family of GLUTs, several of which have been the focus of this series of reviews. The subject of the present review is GLUT3, which, as implied by its name, was the third glucose transporter to be cloned (Kayano T, Fukumoto H, Eddy RL, Fan YS, Byers MG, Shows TB, Bell GI. J Biol Chem 263: [15245][15246][15247][15248] 1988) and was originally designated as the neuronal GLUT. The overriding question that drove the early work on GLUT3 was why would neurons need a separate glucose transporter isoform? What is it about GLUT3 that specifically suits the needs of the highly metabolic and oxidative neuron with its high glucose demand? More recently, GLUT3 has been studied in other cell types with quite specific requirements for glucose, including sperm, preimplantation embryos, circulating white blood cells, and an array of carcinoma cell lines. The last are sufficiently varied and numerous to warrant a review of their own and will not be discussed here. However, for each of these cases, the same questions apply. Thus, the objective of this review is to discuss the properties and tissue and cellular localization of GLUT3 as well as the features of expression, function, and regulation that distinguish it from the rest of its family and make it uniquely suited as the mediator of glucose delivery to these specific cells.neurons; sperm; preimplantation embryo; white blood cells GLUCOSE METABOLISM IS VITAL to most mammalian cells, and the passage of glucose across cell membranes is facilitated by a family of integral membrane transporter proteins, the GLUTs. There are currently 14 members of the SLC2 family of GLUTs, several of which have been the focus of this series of reviews. The subject of the present review is GLUT3 which, as implied by its name, was the third glucose transporter to be cloned (62) and was originally designated as the neuronal glucose transporter. Together with GLUT1, -2, and -4, it comprises the Class 1 group of transporters (For review see Refs. 15,81,121). With the cloning of GLUT3, it became apparent that the brain did not rely exclusively on GLUT1 and that GLUT3 was highly and specifically expressed by neurons. Thus, GLUT3 became the third facilitative glucose transporter isoform with unique characteristics suited for cell-specific expression and function. GLUT2 is ideally suited for expression in liver and pancreas due to its high K m for glucose; GLUT4 and its translocation from intracellular vesicles to the cell surface facilitates insulin-stimulated glucose uptake in insulin-sensitive cells: muscle and fat. The overriding question that drove the early work in GLUT3 in the brain was: why would neurons need a separate glucose transporter isoform; what is it about GLUT3 that specifically suits the needs of the highly metabolic and oxidative neuron with its high glucose demand?...

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Section: Neuronal Glut3 and Cerebral Glucose Utilizationmentioning

confidence: 99%

The facilitative glucose transporter GLUT3: 20 years of distinction

Simpson

Dwyer

Malide

et al. 2008

American Journal of Physiology-Endocrinology and Metabolism

395

322

View full text Add to dashboard Cite

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“…35 S-labeled riboprobes for IGF-1 were synthesized from a linearized plasmid containing a partial cDNA insert to rat IGF-1 (17). Following the initial autoradiographic exposure, cell-specific expression was analyzed by immunohistochemistry (18) with mouse monoclonal glial fibrillary acidic protein (GFAP) for astrocytes or neuron-specific TG2 antibody (provided by Steven Levison, Penn State Milton S. Hershey Medical Center, Hershey, Pennsylvania, USA, and Peter Davies, Albert Einstein Medical College, New York, New York, USA, respectively) using the ABC Elite kit (Vector Laboratories Inc., Burlingame, California, USA) with diaminobenzidine (Sigma-Aldrich). Lectin staining was performed using GSA I-B 4 Griffonia lectin (SigmaAldrich) as previously described (19).…”

Section: Figurementioning

confidence: 99%

Estrogen stimulates microglia and brain recovery from hypoxia-ischemia in normoglycemic but not diabetic female mice

et al. 2004

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Diabetic hyperglycemia increases ischemic brain damage in experimental animals and humans. The mechanisms are unclear but may involve enhanced apoptosis in penumbral regions. Estrogen is an established neuroprotectant in experimental stroke. Our previous study demonstrated that female diabetic db/db mice suffered less damage following cerebral hypoxia-ischemia (H/I) than male db/db mice. Here we investigated the effects of diabetes and estrogen apoptotic gene expression following H/I. Female db/db and nondiabetic (+/?) mice were ovariectomized (OVX) and treated with estrogen or vehicle prior to H/I; brains were analyzed for damage and bcl-2 family gene expression. OVX increased ischemic damage in +/? mice; estrogen reduced tissue injury and enhanced antiapoptotic gene expression (bcl-2 and bfl-1). db/db mice demonstrated more damage, without increased bcl-2 mRNA; bfl-1 expression appeared at 48 hours of recovery associated with infarction. To our knowledge, this is the first description of bfl-1 in the brain with localization to microglia and macrophages. Early induction of bfl-1 expression in +/? mouse brain was associated with microglia; delayed bfl-1 expression in diabetic brain was in macrophages bordering the infarct. Furthermore, estrogen replacement stimulated early postischemic expression of bcl-2 and bfl-1 and reduced damage in normoglycemic animals but failed to protect the diabetic brain.

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“…Это может служить объясне-нием того, что снижение уровня IRAP вызывает уменьшение ýкспрессии GLUT4 [28].…”

Section: Discussionunclassified