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Encyclopedia > GLUT4

Glucose transporters (GLUT or SLC2A family) are a family of membrane proteins found in most mammalian cells. A membrane protein is a protein molecule (or assembly of molecules) that is either embedded in or weakly attached to a biological membrane, especially the plasma membrane. ...

  • GLUT1 is used by erythrocytes to transport glucose
  • GLUT2 by liver and pancreatic β cells
  • GLUT3 by brain and nerve tissue (it may operate in concert with GLUT1 to maximise glucose uptake)
  • GLUT4 by only muscle and adipose tissue
  • Other families exist

Glucose is an essential substrate for the metabolism of most cells. Because glucose is a polar molecule, its transport through biological membranes requires specific transporter proteins. Transport of glucose through the apical membrane of intestinal and kidney epithelial cells depends on the presence of active Na+/glucose symporters, SGLT-1 and SGLT-2, which concentrate glucose inside the cells, using the energy provided by cotransportof Na+ ions down their electrochemical gradient (Hediger and Rhoads 1994). Facilitated diffusion of glucose through the cellular membrane is otherwise catalyzed by glucose carriers (protein symbol GLUT, gene symbol SLC2 for Solute Carrier Family 2) that belong to a superfamily of transport facilitators (major facilitator superfamily) which comprises organic anion and cation transporters, yeast hexose transporter, plant hexose/proton symporters, and bacterial sugar/proton symporters (Henderson 1993). Human red blood cells Red blood cells are the most common type of blood cell and are the vertebrate bodys principal means of delivering oxygen to body tissues via the blood. ... Glucose (Glc), a monosaccharide, is one of the most important carbohydrates. ... Electrochemical gradients in cellular biology refers to the electrical and chemical properties across a membrane. ...


GLUTs are integral membrane proteins which contain 12 membrane-spanning helices with both the amino- and carboxyl-termini exposed on the cytoplasmic side of the plasma membrane. GLUT proteins transport glucose and related hexoses according to a model of alternate conformation (Oka et al. 1990; Hebert and Carruthers 1992; Cloherty et al. 1995), which predicts that the transporter exposes a single substrate binding site toward either the outside or the inside of the cell. Binding of glucose to one site provokes a conformational change associated with transport and releases glucoses to the other side of the membrane. The inner and outer glucose-binding sites are probably located in transmembrane segments 9, 10, 11 (Hruz and Mueckler 2001); also, the QLS motif located in the seventh transmembrane segment could be involved in the selection and affinity of transported substrate (Seatter et al. 1998; Hruz and Mueckler 1999).


Each glucose transporter isoform plays a specific role in glucose metabolism which is determined by its pattern of tissue expression, substrate specificity, transport kinetics, and regulated expression in different physiological conditions (Thorens 1996).


To date, 13 members of the GLUT/SLC2 have been identified (Joost and Thorens 2001). On the basis of sequence similarities, the GLUT family has been divided into three subclasses. Class I comprises the well-characterized glucose transporters GLUT1-GLUT4 (Bell et al. 1990). GLUT1 was the first glucose transporters to be characterized (Mueckler et al. 1985). It is widely distributed in fetal tissues. In the adult it is expressed at highest levels in erythrocytes and also in the endothelial cells of barrier tissues such as the blood-brain barrier. Mutations in the GLUT1 gene are responsible for GLUT1 deficiency or De Vivo syndrome (OMIM 606777), which is a rare autosomal dominant disorder (Seidner et al. 1998). This disease is characterized by a low cerebrospinal fluid glucose concentration (hypoglycorrhachia) which results from impaired glucose transport across the blood-brain barrier. GLUT3 is an isoform expressed mostly in neurons where it is believed to be the main glucose transporter isoform. GLUT4 is the insulin-regulated glucose transporter found in adipose tissues and muscles that is responsible for insulin-regulated glucose disposal. Class II comprises the fructose transporter GLUT5 and GLUT7, 9, 11. Class III comprises GLUT6, 8, 10, and 12 and the H+/myoinositol transporter HMIT (Uldry et al. 2000). Most members of classes II and III have been idenitified recently in homology searches of EST databases and the sequence information provided by the various genome projects. The blood-brain barrier is a physical barrier between the blood vessels in the central nervous system, and most parts of the central nervous system itself. ... EST may stand for: Eastern Standard Time - There are three time zones known as Eastern Standard Time (Australian time zone UTC+10, Brazilian Eastern time zone UTC-3 and North American time zone, UTC-5) EST.. - New Zealand Graffiti-influenced Art Label Electron Spiral Toroid (Energy technology) Erhard Seminars Training...


Most of cells are unable to produce free glucose because they lack expression of glucose-6-phosphatase and thus are only involved in glucose uptake and catabolism. Only hepatocytes and, in more severe fasting conditions, intestine and kidney are able to produce glucose following activation of gluconeogenesis and glycogenolysis.


  Results from FactBites:
 
The Endosomal Compartment Is an Insulin-Sensitive Recruitment Site for GLUT4 and GLUT1 Glucose Transporters in Cardiac ... (6050 words)
GLUT4 vesicle populations in cardiomyocytes in response to insulin
Immunotitration of GLUT4, GLUT1, and SCAMPs in intracellular membranes from nonstimulated cardiomyocytes.
GLUT4 and GLUT1 in the plasma membrane; Fig.
Characterization of Two Distinct Intracellular GLUT4 Membrane Populations in Muscle Fiber. Differential Protein ... (6601 words)
The abundance of GLUT4 was assayed in 1) surface membrane fraction 23F1 enriched in sarcolemmal markers and in membrane fraction 23F2 enriched in sarcolemmal markers and in T-tubule markers; and 2) in intracellular membranes 26F1, 29F1, 35F1, 26F2, 29F2, and 35F2 from control and insulin-stimulated muscles.
The abundance of GLUT4 and cellubrevin was assayed in plasma membranes (PM) and intracellular membrane fractions (LDM) from unstimulated and insulin-treated cardiomyocytes (A).
that cellubrevin and VAMP2 colocalize with GLUT4 in intracellular
  More results at FactBites »


 

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