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Blood, Vol. 89 No. 11 (June 1), 1997: pp.

4190-4195

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Human Erythrocytes Express GLUT5 and Transport Fructose By Ilona I. Concha, Fernando V. Velásquez, Juan M. Martínez, Constanza Angulo, Andrea Droppelmann, Alejandro M. Reyes, Juan Carlos Slebe, Juan Carlos Vera, and David W. Golde From the Instituto de Bioquímica, Facultad de Ciencias, Universidad Austral de Chile, Valdivia, Chile; and the Program in Molecular Pharmacology and Therapeutics, Memorial Sloan-Kettering Cancer Center, New York, NY.

ABSTRACT Abstract Introduction Methods

We present evidence indicating that human erythrocytes express the fructose transporter GLUT5.1-4 The sodium-glucose cotransporters correspond to a transport system that is restricted in expression to the small intestine and kidney and consist of a family of proteins with the capacity to transport glucose against a concentration gradient. the sodium-glucose cotransporters and the facilitative glucose transporters. Similarly. which is the major means for transporting fructose into the cell. did not affect the transport of fructose in human erythrocytes. Immunoblotting and immunolocalization experiments identified the presence of GLUT1 and GLUT5 as the main facilitative hexose transporters expressed in human erythrocytes.000 per cell.Results Discussion References Although erythrocytes readily metabolize fructose. a glucose analog that is transported by GLUT1 and GLUT2. Functional studies allowed the identification of two transporters with different kinetic properties involved in the transport of fructose in human erythrocytes. the transport of glucose is mediated by the glucose transporter isoform GLUT1. is restricted in expression to the internal membranes of the endoplasmic reticulum. are mainly expressed on the cell membrane.5 Each glucose transporter has a characteristic tissue distribution and mammalian cells generally express more than one transporter isoform concomitantly. cytochalasin B. GLUT1 through GLUT5. of which there are about 300. Two glucose transporter families have been identified in mammalian cells that differ both in structure and function. a potent inhibitor of the functional activity of GLUT1 and GLUT2. The facilitative glucose transporters (GLUTs) allow the transport of glucose down a concentration gradient (facilitated transport) and are present in all cells and tissues. with GLUT2 present in lower amounts.6 As a consequence of this high level of expression. The predominant transporter (GLUT5) showed an apparent Km for fructose of approximately 10 mmol/L.1-3 Six facilitative glucose transporter isoforms have been characterized in mammalian cells.4 The transport of glucose is coupled to the simultaneous transport of sodium ions down a concentration gradient. of which five. the initial studies that led to the functional characterization of the facilitative glucose transporters were performed using human erythrocytes and later . INTRODUCTION Abstract Introduction Methods Results Discussion References CELLULAR GLUCOSE uptake is mediated by specific transporters that transfer it through the lipid barrier. and one. Transport of low concentrations of fructose was not affected by 2-deoxy-D-glucose. The functional properties of the fructose transporter present in human erythrocytes are consistent with a central role for GLUT5 as the physiological transporter of fructose in these cells. GLUT7. In human erythrocytes. it has not been known how this sugar gains entry to the red blood cell.

Two facilitative hexose transporter isoforms have the capacity to transport fructose. The high glucose transport capacity of the human erythrocyte is consistent with its dependence on glucose for generating energy.7 Fructose is phosphorylated to fructose-6phosphate by hexokinase. a phosphorylated sugar that is not a known intermediary of glucose metabolism.using highly purified preparations of GLUT1 reconstituted in lipid vesicles. The erythrocyte is also capable of metabolizing fructose by at least two routes. GLUT2 is a low affinity transporter of glucose that also transports fructose with lower affinity. our results indicate that GLUT5 is the primary physiological transporter of fructose in these cells. Outdated human blood was obtained from the Blood Bank at Hospital Regional. Erythrocytes were used within 2 weeks of preparation. and because the transport of fructose is minimally affected by compounds known to block the function of GLUT1 and GLUT2. this isoform is still known as the "erythrocyte" glucose transporter.8. GLUT2. The final pellet was resuspended in PBS and stored at 4°C until use. Although current evidence suggests that GLUT1 is universally expressed in mammalian cells. . generation of fructose-3-phosphate in vitro in erythrocytes incubated in the presence of extracellular fructose is compatible with the existence of fructose transporters operating in the erythrocyte plasma membrane. Blood samples were washed three times in phosphate-buffered saline (PBS) pH 7. The kinetic characteristics of the transport of fructose by human erythrocytes show that they express a high affinity transporter of fructose. Valdivia. Fructose-3-phosphate. we12 and others13 have noted that erythrocytes in blood vessels show strong immunohistochemical reactivity for GLUT5. and GLUT5.10 Although the physiological source of the intracellular fructose was not identified in these studies. MATERIALS AND METHODS Abstract Introduction Methods Results Discussion References Erythrocytes.4 by centrifugation at 2.000g for 5 minutes. has also been identified in human erythrocytes. The immunolocalization studies indicated the presence of GLUT2 and GLUT5 in human erythrocytes.11 In the course of studies of the expression of facilitative hexose transporters in human breast tumors.9 an enzyme that has an important role in the metabolism of glucose. The hexose transporter GLUT5 is unable to transport glucose and is instead a high affinity transporter of fructose with a Km approximately 10 times lower than GLUT2. We have studied in detail the expression of facilitative hexose transporters on human erythrocytes and kinetically and functionally characterized the transport and uptake of fructose.

The smears were incubated with 5% skim milk.14 Membrane proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). and incubated with antibodies to the glucose transporters or preimmune sera diluted 1:500. Erythrocytes were spread onto gelatin-coated slides and fixed with Histochoice (Amresco. Immunolocalization of hexose transporters in blood vessel erythrocytes.3% Triton X-100 in PBS (pH 7. OH). Fig 2. The specificity of the antibodies was tested using human and rat tissues.4) for 1 hour. Erythrocyte membranes were isolated as previously described. Inc. and . and color developed with 4-nitroblue tetrazolium chloride and 5-bromo-4-chloro-3-indolyl phosphate. For immunofluorescence.Fig 1. followed by alkaline phosphatase-antirabbit IgG treatment. The fructose transporter GLUT5 is expressed in human erythrocytes. tissue sections were reacted with GLUT antibodies or with preimmune serum (PI) and visualized using fluorescein-coupled secondary antibodies. erythrocyte smears were reacted with GLUT antibodies or with antibodies preabsorbed with the corresponding peptide (P) and visualized using fluorescein-coupled secondary antibodies. View larger version (58K): [in this window] [in a new window] Immunocytochemistry. MA). Solon. View larger version (139K): [in this window] [in a new window] Western blot analysis. 1% bovine serum albumin (BSA). The glucose transporter antibodies were from East Acres Biologicals (Southbridge. 0. For immunofluorescence. transferred to nitrocellulose membranes.

All cells within an observation field reacted with the three antibodies. the immunoreactivity was abolished by preincubating the antibodies with the respective peptides used to generate them (Fig 1). Gaithersburg. The cells were dissolved in 0. Uptake was stopped with ice-cold PBS containing HgCl2 and KI. The erythrocytes were washed with PBS (pH 7.4]. and observed by fluorescence microscopy. Immunofluorescent detection of the glucose transporters in blood vessels was studied in normal human tissue sections prepared from paraffin-archived tissue blocks. Uptake assays. 0. Erythrocytes were diluted in incubation buffer (15 mmol/L HEPES [pH 7. and the reaction was distributed in patches across the cell. 5 mmol/L KCl. For both GLUT1 and GLUT5. and the incorporated radioactivity was assayed by liquid scintillation spectroscopy. competitors and inhibitors were added to the uptake assays or preincubated with the cells. Thus. For GLUT2.0.4). with a clear rim of fluorescence observed at the cell external border. DuPont NEN). No immunoreactivity was observed using preimmune serum. Boston. DuPont/NEN. GLUT2. washed with PBS (pH 7. RESULTS Abstract Introduction Methods Results Discussion References We used a panel of antibodies for each of the five members of the family of glucose transporters (GLUT1 through GLUT5) to identify the isoforms expressed in human erythrocytes.4). we analyzed the reactivity of the erythrocytes present in blood vessels of samples of human tissue fixed for routine pathological analysis. incubated with goat antirabbit IgG (H-L)-fluorescein isothiocyanate (FITC) conjugate (GIBCO-BRL. and GLUT5 in human erythrocytes (Fig 1). 0. or 0. 135 mmol/L NaCl. Immunolocalization using immunofluorescence showed the presence of the transporters GLUT1. MD) at a dilution of 1:30 for 1 hour. No positive reaction was observed in the case of GLUT3 and GLUT4 antibodies. Similar to erythrocytes present in the blood smears.8 mmol/L MgCl2 ). the immunocytologic data are compatible with the expression of high levels of the transporters GLUT1 and GLUT5 in human erythrocytes and low levels of the transporter GLUT2.8 mmol/L CaCl2 .5 mmol/L 2-deoxy-D-glucose and 1 µCi of 3Hdeoxyglucose (5 mCi/mmol. the level of fluorescence was consistently lower than that observed with GLUT1 and GLUT5 antibodies. Unless otherwise indicated. GLUT2. Where appropiate. mounted.then with the glucose transporter antibodies or preimmune rabbit serum diluted 1:100 in the same solution for 1 hour. the immune reaction was homogeneously distributed across the cell. uptake assays were performed at 4°C in 200 µL of incubation buffer containing 0. To confirm the results obtained with blood smears. erythrocytes in . 1. Control experiments showed that GLUT3 and GLUT4 antibodies gave positive reactions in tissues that express the respective transporters.2% SDS). In the cases of GLUT1.5 mmol/L fructose and 2 µCi of D-[U-14C]fructose (6 Ci/mmol. Data represent means ± standard deviation (SD) of four samples. and GLUT5. MA).5 mL lysis buffer (10 mmol/L Tris-HCl pH 8.

000 was observed in membranes reacted with GLUT2 antibodies. and GLUT5 in the human erythrocytes was confirmed by immunoblotting. No immunoreactivity was observed in control experiments in which the GLUT1. followed by a second. Sizes on the left are kD. was observed in membranes tested with GLUT5 antibodies (Fig 3). GLUT2. slower uptake component that lasted for the length of the uptake assay (Fig 4A). On the other hand.blood vessels were strongly positive for GLUT1 and GLUT5 and reacted only weakly with GLUT2 antibodies (Fig 2). using different detection methods (immunofluorescence. For immunoblotting. was observed in total membrane proteins of erythrocytes probed with anti-GLUT1 (Fig 3). fructose uptake proceeded in a linear fashion for the first 3 minutes.000. GLUT2. immunoperoxidase. Overall. Deoxyglucose uptake proceeded rapidly. Bouin). Expression of hexose transport proteins in erythrocytes. Similar results were observed when using archival tissue (paraffin-embedded) or fresh samples (frozen tissue). reacted with the different anti-GLUT antibodies. and visualized using horseradish peroxidase antirabbit IgG and enhanced chemiluminescence. We observed anti-GLUT5 immunoreactivity in erythrocytes of blood vessels from different tissues (testis. Considering an intracellular exchange volume for the erythrocytes of approximately 0. Fig 3. breast. with an estimated Mr of 45. electrophoresed.000. Total fructose uptake accounted for only about 5% of the uptake of deoxyglucose under . the immunolocalization and the immunoblotting data are consistent with the expression of three different facilitative hexose transporters in human erythrocytes. brain. the glucose transporter GLUT1. alkaline phosphatase) and different fixation protocols (formalin. and the highaffinity fructose transporter GLUT5. the deoxyglucose uptake data indicated that half the expected equilibrium concentration of deoxyglucose was reached in about 2 minutes. Time-course experiments showed that the transport of fructose by the erythrocytes occurred slowly compared with the uptake of deoxyglucose (Fig 4A and B).5 µL per 10 million cells. a prominent band with an estimated Mr of 50. no immunoreactive band was observed in samples probed with GLUT3 and GLUT4 antibodies (Fig 3). A weakly reactive band with an estimated Mr of 50. On the other hand. and ovary). total erythrocyte membrane proteins were loaded on each lane of a sodium dodecyl sulfate-containing polyacrylamide gel. No immunoreactivity was observed when the samples were treated with GLUT3 and GLUT4 antibodies. View larger version (96K): [in this window] [in a new window] Functional studies showed that human erythrocytes had the capacity to take up fructose. One broad immunoreactive band. The presence of GLUT1. prostate. As expected from the immunolocalization experiments. approaching steady state in about 10 minutes. and GLUT5 antibodies were preabsorbed with the corresponding peptide used to generate the antibodies. the low-affinity glucose-fructose transporter GLUT2. liver. transferred to Immobilon.

Because these experiments were performed at 4°C. Similarly. with a Km for transport of about 70 mmol/L. DISCUSSION Abstract Introduction Methods Results . did not affect the uptake of fructose by human erythrocytes at concentrations that caused a total inhibition of the uptake of deoxyglucose by these cells (Fig 4E).5 mmol/L deoxyglucose. cytochalasin B. a potent inhibitor of the functional activities of GLUT1 and GLUT2 that does not inhibit GLUT5. the difference in uptake cannot be accounted for by differences in intracellular metabolism. (B) Time course of the uptake of 0. data represent the mean ± SD of at least four samples.the same conditions. Measurements were performed at 0. (C) Double-reciprocal plot of the substrate dependence for fructose transport. (D) Semilog plot of the concentration dependence for inhibition of fructose transport by View larger version (31K): deoxyglucose. our data point to GLUT5 as the main route of entry of fructose in human erythrocytes. Consistent with this notion was the finding in competition experiments that uptake of fructose was not decreased in the presence of high concentrations of deoxyglucose that completely blocked the transport of methylglucose by the human erythrocytes (Fig 4D). On the other hand. (A) Time course of the uptake of 0. (E) [in a new window] Semilog plot of the concentration dependence for inhibition of fructose ( ) and deoxyglucose transport ( ) by cytochalasin B. Thus. Fig 4. The data are compatible with the concept that GLUT5 is mainly responsible for the cellular uptake of fructose in human erythrocytes. the Km for the transport of fructose by GLUT5 is in the range of 10 mmol/L. Uptake was measured in the presence of concentrations of fructose ranging from 3 to 40 mmol/L. Where appropriate.5 mmol/L fructose. Cells were preincubated for 5 minutes with cytochalasin B. The second functional component did not show evidence of saturation at concentrations of fructose of 50 mmol/L or higher. Measurements were performed at 0. Kinetic analysis of the uptake of fructose by erythrocytes.5 mmol/L fructose or deoxyglucose using 1-minute uptake assays. The high-affinity component presented an apparent Km for the transport of fructose of approximately 10 mmol/L (Fig 4C).5 [in this window] mmol/L fructose using 1-minute uptake assays. no further attempt to characterize this activity was undertaken. Because these fructose concentrations greatly exceeded the normal fructose content of blood even after a meal rich in fructose. It is known that GLUT2 transports fructose with low-affinity. Dose-response experiments examining uptake at 4°C using incubation times of 5 minutes indicated the presence of two functional components involved in the transport of fructose in human erythrocytes.

15 The properties of a second transport system that did not approach saturation at concentrations of fructose as high as 50 mmol/L are compatible with the expression of low levels of GLUT2 in human erythrocytes. and not GLUT2.3 The lack of a measurable effect of deoxyglucose on fructose transport by human erythrocytes is also consistent with a major role for GLUT5 in the uptake of fructose by these cells. followed by the abundant expression of GLUT5 and low level expression of GLUT2.2. The transport data are consistent with the expression of GLUT5 and GLUT2 in human erythrocytes and support the concept that GLUT5 is the physiological transporter of fructose in these cells. and that this transporter is directly involved in the uptake of fructose by these cells. GLUT2. but not by GLUT5. The alkaloid cytochalasin B strongly inhibits the functional activity of GLUT1.Discussion References We show here that human erythrocytes express the fructose transporter GLUT5. A plausible explanation is that the membrane translocation of fructose mediated by GLUT5 occurs very slowly. Although the transport data are consistent with the immunolocalization data that suggest that GLUT5 is not as abundant as GLUT1 in human erythrocytes. GLUT3. immunoblotting and transport assays. The apparent Km for the transport of fructose by human erythrocytes is similar to the Km for transport of fructose by GLUT5. GLUT2. Deoxyglucose is transported by GLUT1 and GLUT2. a side-by-side comparison of the data indicates that the large difference in transport velocity cannot be explained solely by differences in expression.16 Thus. is the main transporter involved in the uptake of fructose by these cells. but does not inhibit GLUT5-mediated fructose transport. the proteins GLUT1. and GLUT4. The time-course experiments showed that fructose entered human erythrocytes at a velocity that was only a fraction of the velocity of uptake of deoxyglucose by these cells. but the Km for fructose transport is greater than 70 mmol/L. it is expected that deoxyglucose would compete for the transport of fructose if GLUT2 were the main transporter involved in the transport of fructose by human erythrocytes.16 The lack of effect of cytochalasin B on the transport of fructose by human erythrocytes is also consistent with the concept that GLUT5.1 The results of the immunofluorescent localization and the immunoblotting experiments indicating a higher degree of reactivity with GLUT1 antibodies compared with GLUT5 and GLUT2 antibodies are consistent with the concept that GLUT1 is the main hexose transporter expressed in human erythrocytes.3. The immunolocalization data indicate the presence in human erythrocytes of three members of the family of mammalian facilitative hexose transporters. and GLUT5. GLUT2 is capable of transporting fructose. An example of slow transport of a molecule across the cell membrane is the transport of a fluorescent glucose analog by GLUT1.17 The demonstration that human erythrocytes express the fructose transporter GLUT5 and have the capacity to transport fructose has implications for our understanding of human red blood cell metabolism. The glucose transporter GLUT1 present in human erythrocytes has been extensively studied using whole cells as well as reconstituted systems. There has been an increased consumption of fructose in . This conclusion is supported by the results of immunolocalization.

19 It is conceivable then that GLUT5 is directly involved in the transport of fructose in these tissues. Instituto de Bioquímica. FOOTNOTES Submitted September 25. Chile.21 Fructose-3-phosphate and its metabolic product. Universidad Austral de Chile. Facultad de Ciencias.22 Although phosphorylated fructose intermediaries are generated intracellularly from glucose. fructose can be phosphorylated to fructose-1-phosphate by fructokinase. component of nonhepatic clearance of dietary fructose. may be important sites for fructose metabolism.S.15 In the intact organism and under normal conditions. and by Memorial Sloan-Kettering Institutional Funds.modern times due to the widespread use of fructose as a natural sweetener. and to a lesser degree muscle tissue. for tissue samples. Grants No. The publication costs of this article were defrayed in part by page charge payment. S-95-24 from the Universidad Austral de Chile. R01 HL42107. 1996. This article must therefore be hearly marked ``advertisment'' in accordance with 18 U. it is generally believed that the first step in the metabolism of fructose in human erythrocytes is the phosphorylation to fructose-6-phosphate by hexokinase. Concha. Santiago. Fructose crosses the brush border membrane of the small intestinal enterocytes through GLUT5. adipose and muscle tissue do not express measurable amounts of GLUT2. and fructose-1-phosphate is a potent activator of glucose phosphorylation to glucose-6-phosphate. the liver is the major site of fructose metabolism. 196-0485 from FONDECYT. Universidad Austral de Chile. Chile.9 In liver. 3-deoxyglucosone. Campus Isla Teja. accepted January 15. 1997. A better understanding of the metabolic pathways involved in the metabolism of fructose by human erythrocytes is slowly emerging.18 In liver. Similar to liver. but instead express low levels of GLUT5. but also has low affinity for fructose. our results indicate that fructose of dietary origin can be transported into human erythrocytes with the direct participation of the high-affinity fructose transporter GLUT5.20 It has been described recently that human erythrocytes accumulate measurable amounts of fructose-3-phosphate when incubated in the presence of fructose. PhD. have also been found in the lens of diabetic rats. ACKNOWLEDGMENT We thank Dr Luis Norambuena from the Instituto de Histología y Patología. REFERENCES Abstract Introduction Methods Results . On the other hand. an enzyme that primarily phosphorylates glucose. although there is also evidence indicating that adipose tissue. Valdivia. R01 CA30388. and P30 CA08748 from the National Institutes of Health. Grant No. Supported in part by Grant No. Casilla 567. The data presented here are compatible with the notion that human erythrocytes may be a significant.C. and until now unrecognized. section 1734 solely to indicate this fact. the transport of fructose is mediated by GLUT2. which is a potent glycosylating agent. Address reprint requests to Ilona I.

Physiol Rev 74:993. Waddell ID. Zomerschoe AG. role of hexokinase in erythrocyte aging. Paglia DE. Steinmann B. Delgado-Lopez F. Cancer 72:2979. Bashan N: Fructose metabolism in the human red blood cell. Evidence for two sugar-binding sites per carrier. J Biol Chem 265:17424. Oka T. Sone K. Wahl RL: Overexpression of Glut-1 glucose transporter in human breast cancer. p 905 8. Holman GD: The glucose transporter family: Structure. Young JD: Extraction and partial purification of the nucleoside-transport system from human erythrocytes based on the assay of nitrobenzylthioinosine-binding activity. Physiol Rev 70:1135. Gitzelmann R. Burant CF: Sequence. Davidson NO. Voice MW. Jarvis SM. Biochem J 303:877. Hediger MA. tissue distribution. Naiman JC: Hereditary hemolytic anemia with hexokinase deficiency. Szwergold BS. Comparison with liver plasma-membrane glucose-transport protein GLUT 2. Vera JC: Expression of the fructose transporter Glut5 in human breast cancer. Takeda E: Characterization of the rabbit intestinal fructose transporter (GLUT5). Kappler F. Biochim Biophys Acta 1154:17. Van den Berghe G: Disorders of fructose metabolism. Brown RS. Proc Natl Acad Sci USA 93:1847. Rand EB. Biochem J 194:331. Biochem J 295:329. 1993[Medline] [Order article via Infotrieve] 12. Minami H. Depaoli AM. 1993[Medline] [Order article via Infotrieve] 14. 1990[Free Full Text] 2. Rhoads DB: Molecular physiology of sodium-glucose cotransporters. Gould GW. New York. Concha II. Israel J Med Sci 10:707. Sly WS. Morimoto A. 1974[Medline] [Order article via Infotrieve] 10. 1990[Abstract/Free Full Text] 11. Tatsumi S. Bauchan MA. Helgerson AL. 1994[Abstract] 4. Rivas CI. Bell GI. J Biol Chem 262:5464. NY. Am J . Baldwin SA: Mammalian passive glucose transporters: Members of an ubiquitous family of active and passive transport proteins. Baselga J. 1992[Medline] [Order article via Infotrieve] 6. Beaudet AL. 1967[Medline] [Order article via Infotrieve] 9. Burchell A: Cloning and expression of a hepatic microsomal glucose transport protein. 1994[Free Full Text] 5. Petersen A. 1996[Abstract/Free Full Text] 13. vol 1. Miyamoto K. Schneider AS. Carruthers A: Equilibrium ligand binding to the human erythrocyte sugar transporter. function and tissue-specific expression. 1987[Abstract/Free Full Text] 7. McGraw-Hill. Valentine WN. Yamamoto H. Biochem J 286:173. Nakabou Y. 1995. Brown TR: Identification of sorbitol 3-phosphate and fructose 3-phosphate in normal and diabetic human erythrocytes. in Scriver CR.Discussion References 1. Eur J Biochem 219:713. N Engl J Med 276:1. Moses SW. 1993[Medline] [Order article via Infotrieve] 3. Weingarten M. 1994[Medline] [Order article via Infotrieve] 16. and functional characterization of the rat fructose transporter GLUT5. Taketani Y. Oski FA. Golde DW. 1981[Medline] [Order article via Infotrieve] 15. Nualart F. Valle D (eds): The Metabolic and Molecular Bases of Inherited Disease. Mueckler M: Facilitative glucose transporters. Zamora-Leon SP. An immunohistochemical study. Carruthers A: Facilitated diffusion of glucose.

172. Szwergold BS. Geleoc. Educ. Wells-Knecht K. (2000) 170153097. Animal Models. Kappler F. 31(3): 163 . [Abstract] [Full Text] . 97(22): 11759 . J. Malaisse-Lagae F. and L. 1996[Abstract] 21. Petersen A. [Abstract] [Full Text] [PDF] J.Physiol 264:G1169. R. renal. This article has been cited by other articles: (Search Google Scholar for Other Citing Articles) N. Baynes JW. Malaisse WJ. Randall WC. Phosphorylation to fructose 3-phosphate. [Abstract] [Full Text] [PDF] C. Burchmore. Brown TR: Metabolism of fructose-3-phosphate in the diabetic rat lens. Kutchai H: Asymmetric transport of a fluorescent glucose analogue by human erythrocytes. Van Schaftingen E: Regulation of glucokinase by a fructose-1-phosphate-sensitive protein in pancreatic islets. and Human Studies Biochem. G. Woodrow. August 17. Biochim Biophys Acta 815:75. Brown TR: Fructose metabolism in the human erythrocyte. 1996 20. Vandercammen A. Harbott Molecular mechanisms of sound amplification in the mammalian cochlea PNAS. 1962[Free Full Text] 19. and liver glucose fluxes. 2003. Arch Biochem Biophys 318:191. Charron What We Know about Facilitative Glucose Transporters: Lessons from Cultured Cells. J. Kappler F. F. 1995[Medline] [Order article via Infotrieve] © 1997 by The American Society of Hematology. Eur J Biochem 190:539. May 1.. J. Krishna Hexose permeation pathways in Plasmodium falciparum-infected erythrocytes PNAS. Am J Physiol 270:G541. 1993 17. Taylor AH. Ginsberg JL: Fructose metabolism of adipose tissue. Lal S. 1992[Medline] [Order article via Infotrieve] 22. Speizer L. J Biol Chem 237:3317. Gorovits and M. 2000. 2000. Davies DR. Haugland R. 1985[Medline] [Order article via Infotrieve] 18. S. and S. October 24. Biochem J 284:363. Thorens B: Glucose transporters in the regulation of intestinal. Froesch ER. Ashmore.11764. Szwergold BS. G.

and S. Articles by Golde. 2000. Articles citing this Article PubMed PubMed Citation Articles by Concha. D. I. Alert me if a correction is posted [Abstract] [Full Text] [PDF] Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Google Scholar Articles by Concha. J.9936.This Article Abstract C. Articles by Golde. I. Burchmore. W. D. August 29. W. 97(18): 9931 . R. J. Woodrow. Related Collections Red Cells . Krishna Full Text (PDF) Hexose permeation pathways in Plasmodium falciparum-infected erythrocytes Alert me when this article is cited PNAS. I. I.