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• W2892076817 abstract "After its uptake into the cytosol, intracellular glucose is phosphorylated to glucose-6-phosphate (G6P), trapping it within the cell and preparing it for metabolism. In glucose-exporting tissues, like liver, G6P is transported into the ER, where it is dephosphorylated by G6Pase-α. The glucose is then returned to the cytosol for export [1Bali D.S. Chen Y.-T. Austin S. Goldstein J.L. Glycogen storage disease type I.in: Adam M. Ardinger H. Pagon R.A. GeneReviews. University of Washington, 1993: 1-22Google Scholar, 2Csala M. Marcolongo P. Lizák B. Senesi S. Margittai E. Fulceri R. Magyar J.E. Benedetti A. Bánhegyi G. Transport and transporters in the endoplasmic reticulum.Biochim. Biophys. Acta. 2007; 1768: 1325-1341Crossref PubMed Scopus (41) Google Scholar]. Defects in these pathways cause glycogen storage diseases [1Bali D.S. Chen Y.-T. Austin S. Goldstein J.L. Glycogen storage disease type I.in: Adam M. Ardinger H. Pagon R.A. GeneReviews. University of Washington, 1993: 1-22Google Scholar]. G6Pase-β, an isozyme of G6Pase-α, is widely expressed [3Martin C.C. Oeser J.K. Svitek C.A. Hunter S.I. Hutton J.C. O’Brien R.M. Identification and characterization of a human cDNA and gene encoding a ubiquitously expressed glucose-6-phosphatase catalytic subunit-related protein.J. Mol. Endocrinol. 2002; 29: 205-222Crossref PubMed Scopus (72) Google Scholar, 4Guionie O. Clottes E. Stafford K. Burchell A. Identification and characterisation of a new human glucose-6-phosphatase isoform.FEBS Lett. 2003; 551: 159-164Crossref PubMed Scopus (60) Google Scholar]. Its role in cells that do not export glucose is unclear, although mutations in G6Pase-β cause severe and widespread abnormalities [5Boztug K. Appaswamy G. Ashikov A. Schäffer A.A. Salzer U. Diestelhorst J. Germeshausen M. Brandes G. Lee-Gossler J. Noyan F. et al.A syndrome with congenital neutropenia and mutations in G6PC3.N. Engl. J. Med. 2009; 360: 32-43Crossref PubMed Scopus (280) Google Scholar, 6Boztug K. Rosenberg P.S. Dorda M. Banka S. Moulton T. Curtin J. Rezaei N. Corns J. Innis J.W. Avci Z. et al.Extended spectrum of human glucose-6-phosphatase catalytic subunit 3 deficiency: Novel genotypes and phenotypic variability in severe congenital neutropenia.J. Pediatr. 2012; 160: 679-683.e2Abstract Full Text Full Text PDF PubMed Scopus (60) Google Scholar, 7Desplantes C. Fremond M.L. Beaupain B. Harousseau J.L. Buzyn A. Pellier I. Roques G. Morville P. Paillard C. Bruneau J. et al.Clinical spectrum and long-term follow-up of 14 cases with G6PC3 mutations from the French Severe Congenital Neutropenia Registry.Orphanet J. Rare Dis. 2014; 9: 183Crossref PubMed Scopus (38) Google Scholar]. Astrocytes, the most abundant cells in the brain, provide metabolic support to neurons, facilitated by astrocytic endfeet that contact blood capillaries or neurons [8Kacem K. Lacombe P. Seylaz J. Bonvento G. Structural organization of the perivascular astrocyte endfeet and their relationship with the endothelial glucose transporter: A confocal microscopy study.Glia. 1998; 23: 1-10Crossref PubMed Scopus (277) Google Scholar, 9Mathiisen T.M. Lehre K.P. Danbolt N.C. Ottersen O.P. The perivascular astroglial sheath provides a complete covering of the brain microvessels: An electron microscopic 3D reconstruction.Glia. 2010; 58: 1094-1103Crossref PubMed Scopus (556) Google Scholar, 10Dienel G.A. Fueling and imaging brain activation.ASN Neuro. 2012; 4: 267-321Crossref Scopus (119) Google Scholar, 11Díaz-García C.M. Mongeon R. Lahmann C. Koveal D. Zucker H. Yellen G. Neuronal stimulation triggers neuronal glycolysis and not lactate uptake.Cell Metab. 2017; 26: 361-374.e4Abstract Full Text Full Text PDF PubMed Scopus (229) Google Scholar, 12Dienel G.A. Lack of appropriate stoichiometry: Strong evidence against an energetically important astrocyte-neuron lactate shuttle in brain.J. Neurosci. Res. 2017; 95: 2103-2125Crossref PubMed Scopus (99) Google Scholar]. Perivascular endfeet are the main site of glucose uptake by astrocytes [13Morgello S. Uson R.R. Schwartz E.J. Haber R.S. The human blood-brain barrier glucose transporter (GLUT1) is a glucose transporter of gray matter astrocytes.Glia. 1995; 14: 43-54Crossref PubMed Scopus (177) Google Scholar], but in human brain they may be several millimeters away from the perineuronal processes [14Oberheim N.A. Takano T. Han X. He W. Lin J.H. Wang F. Xu Q. Wyatt J.D. Pilcher W. Ojemann J.G. et al.Uniquely hominid features of adult human astrocytes.J. Neurosci. 2009; 29: 3276-3287Crossref PubMed Scopus (865) Google Scholar]. We show that cultured human fetal astrocytes express G6Pase-β, but not G6Pase-α. ER-targeted glucose sensors [15Fehr M. Takanaga H. Ehrhardt D.W. Frommer W.B. Evidence for high-capacity bidirectional glucose transport across the endoplasmic reticulum membrane by genetically encoded fluorescence resonance energy transfer nanosensors.Mol. Cell. Biol. 2005; 25: 11102-11112Crossref PubMed Scopus (69) Google Scholar, 16Takanaga H. Frommer W.B. Facilitative plasma membrane transporters function during ER transit.FASEB J. 2010; 24: 2849-2858Crossref PubMed Scopus (52) Google Scholar] reveal that G6Pase-β allows the ER of human astrocytes to accumulate glucose by importing G6P from the cytosol. Glucose uptake by astrocytes, ATP production, and Ca2+ accumulation by the ER are attenuated after knockdown of G6Pase-β using lentivirus-delivered shRNA and substantially rescued by expression of G6Pase-α. We suggest that G6Pase-β activity allows effective uptake of glucose by astrocytes, and we speculate that it allows the ER to function as an intracellular “highway” delivering glucose from perivascular endfeet to the perisynaptic processes." @default.
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• W2892076817 date "2018-11-01" @default.
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• W2892076817 title "Effective Glucose Uptake by Human Astrocytes Requires Its Sequestration in the Endoplasmic Reticulum by Glucose-6-Phosphatase-β" @default.
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• W2892076817 doi "https://doi.org/10.1016/j.cub.2018.08.060" @default.
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