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Volumn 57, Issue 9, 2008, Pages 2445-2452

Evidence for interindividual heterogeneity in the glucose gradient across the human red blood cell membrane and its relationship to hemoglobin glycation

Author keywords

[No Author keywords available]

Indexed keywords

FRUCTOSAMINE; GLITAZONE DERIVATIVE; GLUCOSE; HEMOGLOBIN A1C; INSULIN; METFORMIN; SULFONYLUREA; 3' O METHYLGUANOSINE; 3'-O-METHYLGUANOSINE; CARBON; DIAGNOSTIC AGENT; DRUG DERIVATIVE; GLYCOSYLATED HEMOGLOBIN; GUANOSINE; UREA; WATER;

EID: 52749091945     PISSN: 00121797     EISSN: 1939327X     Source Type: Journal    
DOI: 10.2337/db07-1820     Document Type: Article
Times cited : (115)

References (48)
  • 1
    • 0036741885 scopus 로고    scopus 로고
    • High and low hemoglobin glycation phenotypes in type 1 diabetes: A challenge for interpretation of glycemic control
    • Hempe JM, Gomez R, McCarterRJ, Jr, Chalew SA: High and low hemoglobin glycation phenotypes in type 1 diabetes: a challenge for interpretation of glycemic control. J Diabetes Complications 16:313-320, 2002
    • (2002) J Diabetes Complications , vol.16 , pp. 313-320
    • Hempe, J.M.1    Gomez, R.2    McCarterRJ, J.3    Chalew, S.A.4
  • 2
    • 0025231602 scopus 로고
    • Unexplained variability of glycated haemoglobin in non-diabetic subjects not related to glycaemia
    • Yudkin JS, Forrest RD, Jackson CA, Ryle AJ, Davie S, Gould BJ: Unexplained variability of glycated haemoglobin in non-diabetic subjects not related to glycaemia. Diabetologia 33:208-215, 1990
    • (1990) Diabetologia , vol.33 , pp. 208-215
    • Yudkin, J.S.1    Forrest, R.D.2    Jackson, C.A.3    Ryle, A.J.4    Davie, S.5    Gould, B.J.6
  • 3
    • 0030899150 scopus 로고    scopus 로고
    • Investigation of the mechanism underlying the variability of glycated haemoglobin in non-diabetic subjects not related to glycaemia
    • Gould BJ, Davie SJ, Yudkin JS: Investigation of the mechanism underlying the variability of glycated haemoglobin in non-diabetic subjects not related to glycaemia. Clin Chim Acta 260:49-64, 1997
    • (1997) Clin Chim Acta , vol.260 , pp. 49-64
    • Gould, B.J.1    Davie, S.J.2    Yudkin, J.S.3
  • 4
    • 0042170249 scopus 로고    scopus 로고
    • Discordance between A1C and fructosamine: Evidence for a glycosylation gap and its relation to diabetic nephropathy
    • Cohen RM, Holmes YR, Chenier TC, Joiner CH: Discordance between A1C and fructosamine: evidence for a glycosylation gap and its relation to diabetic nephropathy. Diabetes Care 26:163-167, 2003
    • (2003) Diabetes Care , vol.26 , pp. 163-167
    • Cohen, R.M.1    Holmes, Y.R.2    Chenier, T.C.3    Joiner, C.H.4
  • 5
    • 38149037979 scopus 로고    scopus 로고
    • The relationship of prospective glycated hemoglobin to glycated serum proteins in incident diabetic retinopathy: Implications of the glycation gap for mechanism of risk prediction
    • Cohen RM, LeCaire TJ, Lindsell CJ, Smith EP, D'Alessio DJ: The relationship of prospective glycated hemoglobin to glycated serum proteins in incident diabetic retinopathy: implications of the glycation gap for mechanism of risk prediction. Diabetes Care 31:151-153, 2007
    • (2007) Diabetes Care , vol.31 , pp. 151-153
    • Cohen, R.M.1    LeCaire, T.J.2    Lindsell, C.J.3    Smith, E.P.4    D'Alessio, D.J.5
  • 8
    • 0019984296 scopus 로고
    • Glycosylated hemoglobin in human and animal red cells: Role of glucose permeability
    • Higgins PJ, Garlick RL, Bunn HF: Glycosylated hemoglobin in human and animal red cells: role of glucose permeability. Diabetes 31:743-748, 1982
    • (1982) Diabetes , vol.31 , pp. 743-748
    • Higgins, P.J.1    Garlick, R.L.2    Bunn, H.F.3
  • 9
    • 35148814578 scopus 로고    scopus 로고
    • Red blood cell (RBC) survival differences among hematologically normal people with diabetes (DM) make a clinically important difference in A1C (Abstract)
    • Cohen RM, Ciraolo P, Palascak MB, Lindsell CJ, Khera PK, Smith EP, Joiner CH, Franco RS: Red blood cell (RBC) survival differences among hematologically normal people with diabetes (DM) make a clinically important difference in A1C (Abstract). Diabetes 56 (Suppl. 1):A116, 2007
    • (2007) Diabetes , vol.56 , Issue.SUPPL. 1
    • Cohen, R.M.1    Ciraolo, P.2    Palascak, M.B.3    Lindsell, C.J.4    Khera, P.K.5    Smith, E.P.6    Joiner, C.H.7    Franco, R.S.8
  • 10
    • 0025036574 scopus 로고
    • Facilitated diffusion of glucose
    • Carruthers A: Facilitated diffusion of glucose. Physiol Rev 70:1135-1176, 1990
    • (1990) Physiol Rev , vol.70 , pp. 1135-1176
    • Carruthers, A.1
  • 11
    • 0345511996 scopus 로고
    • The distribution of sugar in blood
    • Somogyi M: The distribution of sugar in blood. J Biol Chem 117-127, 1928
    • (1928) J Biol Chem , vol.117-127
    • Somogyi, M.1
  • 12
    • 0020537502 scopus 로고
    • Comparative evaluation of fifteen anti-sickling agents
    • Chang H, Ewert SM, Bookchin RM, Nagel RL: Comparative evaluation of fifteen anti-sickling agents. Blood 61:693-704, 1983
    • (1983) Blood , vol.61 , pp. 693-704
    • Chang, H.1    Ewert, S.M.2    Bookchin, R.M.3    Nagel, R.L.4
  • 13
    • 14044251555 scopus 로고    scopus 로고
    • Quench-flow analysis reveals multiple phases of GluT1-mediated sugar transport
    • Blodgett DM, Carruthers A: Quench-flow analysis reveals multiple phases of GluT1-mediated sugar transport. Biochemistry 44:2650-2660, 2005
    • (2005) Biochemistry , vol.44 , pp. 2650-2660
    • Blodgett, D.M.1    Carruthers, A.2
  • 15
    • 0033593017 scopus 로고    scopus 로고
    • The human erythrocyte sugar transporter presents two sugar import sites
    • Hamill S, Cloherty EK, Carruthers A: The human erythrocyte sugar transporter presents two sugar import sites. Biochemistry 38:16974-16983, 1999
    • (1999) Biochemistry , vol.38 , pp. 16974-16983
    • Hamill, S.1    Cloherty, E.K.2    Carruthers, A.3
  • 16
    • 0034696679 scopus 로고    scopus 로고
    • ATP-dependent substrate occlusion by the human erythrocyte sugar transporter
    • Heard KS, Fidyk N, Carruthers A: ATP-dependent substrate occlusion by the human erythrocyte sugar transporter. Biochemistry 39:3005-3014, 2000
    • (2000) Biochemistry , vol.39 , pp. 3005-3014
    • Heard, K.S.1    Fidyk, N.2    Carruthers, A.3
  • 17
    • 0022979710 scopus 로고
    • ATP regulation of the human red cell sugar transporter
    • Carruthers A: ATP regulation of the human red cell sugar transporter. J Biol Chem 261:11028-11037, 1986
    • (1986) J Biol Chem , vol.261 , pp. 11028-11037
    • Carruthers, A.1
  • 19
    • 0022453086 scopus 로고
    • Phosphorylation of 3-O-methyl-D-glucose by yeast and beef hexokinase
    • Malaisse-Lagae F, Giroix MH, Sener A, Malaisse WJ: Phosphorylation of 3-O-methyl-D-glucose by yeast and beef hexokinase. FEBS Lett 198:292-294, 1986
    • (1986) FEBS Lett , vol.198 , pp. 292-294
    • Malaisse-Lagae, F.1    Giroix, M.H.2    Sener, A.3    Malaisse, W.J.4
  • 21
    • 0018196435 scopus 로고
    • Modulation of ouabain binding and potassium pump fluxes by cellular sodium and potassium in human and sheep erythrocytes
    • Joiner CH, Lauf PK: Modulation of ouabain binding and potassium pump fluxes by cellular sodium and potassium in human and sheep erythrocytes. J Physiol 283:177-196, 1978
    • (1978) J Physiol , vol.283 , pp. 177-196
    • Joiner, C.H.1    Lauf, P.K.2
  • 22
    • 0028116825 scopus 로고
    • Measurement of the hemoglobin concentration in deoxyhemoglobin S polymers and characterization of the polymer water compartment
    • Bookchin RM, Balazs T, Lew VL: Measurement of the hemoglobin concentration in deoxyhemoglobin S polymers and characterization of the polymer water compartment. J Mol Biol 244:100-109, 1994
    • (1994) J Mol Biol , vol.244 , pp. 100-109
    • Bookchin, R.M.1    Balazs, T.2    Lew, V.L.3
  • 23
    • 17144408367 scopus 로고    scopus 로고
    • Properties of the human erythrocyte glucose transport protein are determined by cellular context
    • Levine KB, Robichaud TK, Hamill S, Sultzman LA, Carruthers A: Properties of the human erythrocyte glucose transport protein are determined by cellular context. Biochemistry 44:5606-5616, 2005
    • (2005) Biochemistry , vol.44 , pp. 5606-5616
    • Levine, K.B.1    Robichaud, T.K.2    Hamill, S.3    Sultzman, L.A.4    Carruthers, A.5
  • 24
    • 0022254617 scopus 로고
    • Facilitated transport of glucose from blood into peripheral nerve
    • Rechthand E, Smith QR, Rapoport SI: Facilitated transport of glucose from blood into peripheral nerve. J Neurochem 45:957-964, 1985
    • (1985) J Neurochem , vol.45 , pp. 957-964
    • Rechthand, E.1    Smith, Q.R.2    Rapoport, S.I.3
  • 25
    • 0036853705 scopus 로고    scopus 로고
    • Vagotomy attenuates effects of L-glucose but not of D-glucose on spontaneous alternation performance
    • Talley CP, Clayborn H, Jewel E, McCarty R, Gold PE: Vagotomy attenuates effects of L-glucose but not of D-glucose on spontaneous alternation performance. Physiol Behav 77:243-249, 2002
    • (2002) Physiol Behav , vol.77 , pp. 243-249
    • Talley, C.P.1    Clayborn, H.2    Jewel, E.3    McCarty, R.4    Gold, P.E.5
  • 26
    • 0029845798 scopus 로고    scopus 로고
    • Human erythrocyte sugar transport is incompatible with available carrier models
    • Cloherty EK, Heard KS, Carruthers A: Human erythrocyte sugar transport is incompatible with available carrier models. Biochemistry 35:10411-10421, 1996
    • (1996) Biochemistry , vol.35 , pp. 10411-10421
    • Cloherty, E.K.1    Heard, K.S.2    Carruthers, A.3
  • 27
    • 0028803259 scopus 로고
    • Net sugar transport is a multistep process: Evidence for cytosolic sugar binding sites in erythrocytes
    • Cloherty EK, Sultzman LA, Zottola RJ, Carruthers A: Net sugar transport is a multistep process: evidence for cytosolic sugar binding sites in erythrocytes. Biochemistry 34:15395-15406, 1995
    • (1995) Biochemistry , vol.34 , pp. 15395-15406
    • Cloherty, E.K.1    Sultzman, L.A.2    Zottola, R.J.3    Carruthers, A.4
  • 28
    • 64649097601 scopus 로고
    • Solvent water in the mammalian erythrocyte
    • Macleod J, Ponder E: Solvent water in the mammalian erythrocyte. J Physiol 86:147-152, 1936
    • (1936) J Physiol , vol.86 , pp. 147-152
    • Macleod, J.1    Ponder, E.2
  • 29
    • 0014086235 scopus 로고
    • Nonsolvent water in human erythrocytes
    • Cook JS: Nonsolvent water in human erythrocytes. JGen Physiol 50:1311-1325, 1967
    • (1967) JGen Physiol , vol.50 , pp. 1311-1325
    • Cook, J.S.1
  • 31
    • 0003159170 scopus 로고    scopus 로고
    • Ascorbate function and metabolism in the human erythrocyte
    • May JM: Ascorbate function and metabolism in the human erythrocyte. Front Biosci 3:d1-d10, 1998
    • (1998) Front Biosci , vol.3
    • May, J.M.1
  • 32
    • 0027302594 scopus 로고
    • Mammalian facilitative hexose transporters mediate the transport of dehydroascorbic acid
    • Vera JC, Rivas CI, Fischbarg J, Golde DW: Mammalian facilitative hexose transporters mediate the transport of dehydroascorbic acid. Nature 364: 79-82, 1993
    • (1993) Nature , vol.364 , pp. 79-82
    • Vera, J.C.1    Rivas, C.I.2    Fischbarg, J.3    Golde, D.W.4
  • 33
    • 0022512090 scopus 로고
    • Anomalous asymmetric kinetics of human red cell hexose transfer: Role of cytosolic adenosine 5'-triphosphate
    • Carruthers A: Anomalous asymmetric kinetics of human red cell hexose transfer: role of cytosolic adenosine 5'-triphosphate. Biochemistry 25: 3592-3602, 1986
    • (1986) Biochemistry , vol.25 , pp. 3592-3602
    • Carruthers, A.1
  • 34
    • 33847033312 scopus 로고    scopus 로고
    • ATP-dependent sugar transport complexity in human erythrocytes
    • Leitch JM, Carruthers A: ATP-dependent sugar transport complexity in human erythrocytes Am J Physiol Cell Physiol 292:C974-C986, 2007
    • (2007) Am J Physiol Cell Physiol , vol.292
    • Leitch, J.M.1    Carruthers, A.2
  • 35
    • 0019225834 scopus 로고
    • Asymmetry of hexose transfer system in erythrocytes of fetal and new-born guinea-pigs
    • Aubby DS, Widdas WF: Asymmetry of hexose transfer system in erythrocytes of fetal and new-born guinea-pigs. J Physiol 309:317-327, 1980
    • (1980) J Physiol , vol.309 , pp. 317-327
    • Aubby, D.S.1    Widdas, W.F.2
  • 38
    • 2542426036 scopus 로고    scopus 로고
    • Biological variation in A1C predicts risk of retinopathy and nephropathy in type 1 diabetes
    • McCarter RJ, Hempe JM, Gomez R, Chalew SA: Biological variation in A1C predicts risk of retinopathy and nephropathy in type 1 diabetes. Diabetes Care 27:1259-1264, 2004
    • (2004) Diabetes Care , vol.27 , pp. 1259-1264
    • McCarter, R.J.1    Hempe, J.M.2    Gomez, R.3    Chalew, S.A.4
  • 39
  • 40
    • 33646338641 scopus 로고    scopus 로고
    • Mean blood glucose and biological variation have greater influence on A1C levels than glucose instability: An analysis of data from the Diabetes Control and Complications Trial
    • McCarter RJ, Hempe JM, Chalew SA: Mean blood glucose and biological variation have greater influence on A1C levels than glucose instability: an analysis of data from the Diabetes Control and Complications Trial. Diabetes Care 29:352-355, 2006
    • (2006) Diabetes Care , vol.29 , pp. 352-355
    • McCarter, R.J.1    Hempe, J.M.2    Chalew, S.A.3
  • 41
    • 34347406488 scopus 로고    scopus 로고
    • The hemoglobin glycation index is not an independent predictor of the risk of microvascular complications in the Diabetes Control and Complications Trial
    • Lachin JM, Genuth S, Nathan DM, Rutledge BN: The hemoglobin glycation index is not an independent predictor of the risk of microvascular complications in the Diabetes Control and Complications Trial. Diabetes 56:1913-1921, 2007
    • (2007) Diabetes , vol.56 , pp. 1913-1921
    • Lachin, J.M.1    Genuth, S.2    Nathan, D.M.3    Rutledge, B.N.4
  • 42
    • 21644477869 scopus 로고    scopus 로고
    • Biological variation in A1C predicts risk of retinopathy and nephropathy in type 1 diabetes: response to McCarter et al Letter
    • Genuth S, Lachin JM, Nathan DM: Biological variation in A1C predicts risk of retinopathy and nephropathy in type 1 diabetes: response to McCarter et al (Letter). Diabetes Care 28:233-235, 2005
    • (2005) Diabetes Care , vol.28 , pp. 233-235
    • Genuth, S.1    Lachin, J.M.2    Nathan, D.M.3
  • 43
    • 35148860603 scopus 로고    scopus 로고
    • A1C: Does one size fit all?
    • Cohen RM: A1C: does one size fit all? Diabetes Care 30:2756-2758, 2007
    • (2007) Diabetes Care , vol.30 , pp. 2756-2758
    • Cohen, R.M.1
  • 44
    • 33745880726 scopus 로고    scopus 로고
    • A1C standardisation destination-global IFCC Standardisation. How, why, where and when-a tortuous pathway from kit manufacturers, via inter-laboratory lyophilized and whole blood comparisons to designated national comparison schemes
    • Goodall I: A1C standardisation destination-global IFCC Standardisation. How, why, where and when-a tortuous pathway from kit manufacturers, via inter-laboratory lyophilized and whole blood comparisons to designated national comparison schemes. Clin Biochem Rev 26:5-19, 2005
    • (2005) Clin Biochem Rev , vol.26 , pp. 5-19
    • Goodall, I.1
  • 46
    • 0021356158 scopus 로고
    • The clinical information value of the glycosylated hemoglobin assay
    • Nathan DM, Singer DE, Hurxthal K, Goodson JD: The clinical information value of the glycosylated hemoglobin assay. N Engl J Med 310:341-346, 1984
    • (1984) N Engl J Med , vol.310 , pp. 341-346
    • Nathan, D.M.1    Singer, D.E.2    Hurxthal, K.3    Goodson, J.D.4
  • 48
    • 0027370108 scopus 로고    scopus 로고
    • The effect of intensive treatment of diabetes on the development and progression of long-term complications in insulin-dependent diabetes mellitus: the Diabetes Control and Complications Trial Research Group. N Engl J Med 329:977-986, 1993
    • The effect of intensive treatment of diabetes on the development and progression of long-term complications in insulin-dependent diabetes mellitus: the Diabetes Control and Complications Trial Research Group. N Engl J Med 329:977-986, 1993


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