메뉴 건너뛰기




Volumn 9, Issue 2-3, 2012, Pages 1-23

Effect of short-term hyperglycemia on protein kinase C alpha activation in human erythrocytes

Author keywords

Acute hyperglycemia; Erythrocyte; Protein kinase C

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM ION; GLUCOSE; GLUCOSE TRANSPORTER 1; HEMOGLOBIN; PHORBOL ESTER; PROTEIN KINASE C ALPHA;

EID: 84872455346     PISSN: 16136071     EISSN: 16140575     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (3)

References (53)
  • 1
    • 0034641568 scopus 로고    scopus 로고
    • Association of glycaemia with macrovascular and microvascular complications of type 2 diabetes (UKPDS 35): Prospective observational study
    • Stratton IM, Adler AI, Neil HA, Matthews DR, Manley SE, Cull CA, Hadden D, Turner RC, Holman RR. Association of glycaemia with macrovascular and microvascular complications of type 2 diabetes (UKPDS 35): prospective observational study. BMJ 2000. 321(7258):405-412.
    • (2000) BMJ , vol.321 , Issue.7258 , pp. 405-412
    • Stratton, I.M.1    Adler, A.I.2    Neil, H.A.3    Matthews, D.R.4    Manley, S.E.5    Cull, C.A.6    Hadden, D.7    Turner, R.C.8    Holman, R.R.9
  • 2
    • 77951737282 scopus 로고    scopus 로고
    • Endothelial dysfunction: The common consequence in diabetes and hypertension
    • Wong WT, Wong SL, Tian XY, Huang Y. Endothelial dysfunction: the common consequence in diabetes and hypertension. J Cardiovasc Pharmacol 2010. 55:300-307.
    • (2010) J Cardiovasc Pharmacol , vol.55 , pp. 300-307
    • Wong, W.T.1    Wong, S.L.2    Tian, X.Y.3    Huang, Y.4
  • 3
    • 76149093955 scopus 로고    scopus 로고
    • Hemorheological disorders in diabetes mellitus
    • Cho YI, Mooney MP, Cho DJ. Hemorheological disorders in diabetes mellitus. J Diabetes Sci Technol 2008. 2(6):1130-1138.
    • (2008) J Diabetes Sci Technol , vol.2 , Issue.6 , pp. 1130-1138
    • Cho, Y.I.1    Mooney, M.P.2    Cho, D.J.3
  • 4
    • 27744579487 scopus 로고    scopus 로고
    • Effects of ageing on carbonyl stress and antioxidant defense in RBCs of obese type 2 diabetic patients
    • Constantin A, Constantinescu E, Dumitrescu M, Calin A, Popov D. Effects of ageing on carbonyl stress and antioxidant defense in RBCs of obese type 2 diabetic patients. J Cell Mol Med 2005. 9:683-691.
    • (2005) J Cell Mol Med , vol.9 , pp. 683-691
    • Constantin, A.1    Constantinescu, E.2    Dumitrescu, M.3    Calin, A.4    Popov, D.5
  • 5
    • 0018843839 scopus 로고
    • Nonenzymatic glycosylation of erythrocyte membrane proteins. Relevance to diabetes
    • Miller JA, Gravallese E, Bunn HF. Nonenzymatic glycosylation of erythrocyte membrane proteins. Relevance to diabetes. J Clin Invest 1980. 65:896-901.
    • (1980) J Clin Invest , vol.65 , pp. 896-901
    • Miller, J.A.1    Gravallese, E.2    Bunn, H.F.3
  • 6
    • 0021037676 scopus 로고
    • Alteration of rheological properties of human erythrocytes by crosslinking of membrane proteins
    • Maeda N, Kon K, Imaizumi K, Sekiya M, Shiga T. Alteration of rheological properties of human erythrocytes by crosslinking of membrane proteins. Biochim Biophys Acta 1983. 735:104-112.
    • (1983) Biochim Biophys Acta , vol.735 , pp. 104-112
    • Maeda, N.1    Kon, K.2    Imaizumi, K.3    Sekiya, M.4    Shiga, T.5
  • 8
    • 0023835005 scopus 로고
    • Association between the glycation of erythrocyte membrane proteins and membrane fluidity
    • Bryszewska M, Szosland K. Association between the glycation of erythrocyte membrane proteins and membrane fluidity. Clin Biochem 1988. 21:49-51.
    • (1988) Clin Biochem , vol.21 , pp. 49-51
    • Bryszewska, M.1    Szosland, K.2
  • 11
    • 0022480470 scopus 로고
    • Effects of hyperglycaemia and sorbitol accumulation on erythrocyte deformability in diabetes mellitus
    • Bareford D, Jennings PE, Stone PC, Baar S, Barnett AH, Stuart J. Effects of hyperglycaemia and sorbitol accumulation on erythrocyte deformability in diabetes mellitus. J Clin Pathol 1986. 39:722-727.
    • (1986) J Clin Pathol , vol.39 , pp. 722-727
    • Bareford, D.1    Jennings, P.E.2    Stone, P.C.3    Baar, S.4    Barnett, A.H.5    Stuart, J.6
  • 12
    • 0027981889 scopus 로고
    • Characterization of the mechanism for the chronic activation of diacylglycerol-protein kinase C pathway in diabetes and hypergalactosemia
    • Xia P, Inoguchi T, Kern TS, Engerman RL, Oates PJ, King GL. Characterization of the mechanism for the chronic activation of diacylglycerol-protein kinase C pathway in diabetes and hypergalactosemia. Diabetes 1994. 43:1122-1129.
    • (1994) Diabetes , vol.43 , pp. 1122-1129
    • Xia, P.1    Inoguchi, T.2    Kern, T.S.3    Engerman, R.L.4    Oates, P.J.5    King, G.L.6
  • 13
    • 0018843839 scopus 로고
    • Nonenzymatic glycosylation of erythrocyte membrane proteins. Relevance to diabetes
    • Miller JA, Gravallese E, Bunn HF. Nonenzymatic glycosylation of erythrocyte membrane proteins. Relevance to diabetes. J Clin Invest 1980. 65:896-901.
    • (1980) J Clin Invest , vol.65 , pp. 896-901
    • Miller, J.A.1    Gravallese, E.2    Bunn, H.F.3
  • 15
    • 0036741867 scopus 로고    scopus 로고
    • Erythrocyte membrane glycation and NA(+)-K(+) levels in NIDDM
    • Umudum F, Yucel O, Sahin Y, Bakan E. Erythrocyte membrane glycation and NA(+)-K(+) levels in NIDDM. J Diabetes Complications 2002. 16:359-362.
    • (2002) J Diabetes Complications , vol.16 , pp. 359-362
    • Umudum, F.1    Yucel, O.2    Sahin, Y.3    Bakan, E.4
  • 16
    • 0028557178 scopus 로고
    • Relationship between hemorheological and microcirculatory abnormalities in diabetes mellitus
    • Le Devehat C, Khodabandehlou T, Vimeux M. Relationship between hemorheological and microcirculatory abnormalities in diabetes mellitus. Diabetes Metab 1994. 20:401-404.
    • (1994) Diabetes Metab , vol.20 , pp. 401-404
    • Le Devehat, C.1    Khodabandehlou, T.2    Vimeux, M.3
  • 17
    • 77955769377 scopus 로고    scopus 로고
    • The spectrin-ankyrin-4.1-adducin membrane skeleton: Adapting eukaryotic cells to the demands of animal life
    • Baines AJ. The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life. Protoplasma 2010. 244:99-131.
    • (2010) Protoplasma , vol.244 , pp. 99-131
    • Baines, A.J.1
  • 19
    • 77953139384 scopus 로고    scopus 로고
    • Altered phosphorylation of cytoskeleton proteins in sickle red blood cells: The role of protein kinase C, Rac GTPases, and reactive oxygen species
    • George A, Pushkaran S, Li L, An X, Zheng Y, Mohandas N, Joiner CH, Kalfa TA. Altered phosphorylation of cytoskeleton proteins in sickle red blood cells: the role of protein kinase C, Rac GTPases, and reactive oxygen species. Blood Cells Mol Dis 2010. 45(1):41-45.
    • (2010) Blood Cells Mol Dis , vol.45 , Issue.1 , pp. 41-45
    • George, A.1    Pushkaran, S.2    Li, L.3    An, X.4    Zheng, Y.5    Mohandas, N.6    Joiner, C.H.7    Kalfa, T.A.8
  • 20
    • 14844314119 scopus 로고    scopus 로고
    • Modulation of erythrocyte membrane mechanical function by protein 4.1 phosphorylation
    • Manno S, Takakuwa Y, Mohandas N. Modulation of erythrocyte membrane mechanical function by protein 4.1 phosphorylation. J Biol Chem 2005 280:7581-7587.
    • (2005) J Biol Chem , vol.280 , pp. 7581-7587
    • Manno, S.1    Takakuwa, Y.2    Mohandas, N.3
  • 21
    • 0022381636 scopus 로고
    • Protein kinase C in the human erythrocyte. Translocation to the plasma membrane and phosphorylation of bands 4.1 and 4.9 and other membrane proteins
    • Palfrey HC, Waseem A. Protein kinase C in the human erythrocyte. Translocation to the plasma membrane and phosphorylation of bands 4.1 and 4.9 and other membrane proteins. J Biol Chem 1985. 260:16021-16029.
    • (1985) J Biol Chem , vol.260 , pp. 16021-16029
    • Palfrey, H.C.1    Waseem, A.2
  • 22
    • 0023874060 scopus 로고
    • Modulation of red cell band 4.1 function by cAMP-dependent kinase and protein kinase C phosphorylation
    • Ling E, Danilov YN, Cohen CM. Modulation of red cell band 4.1 function by cAMP-dependent kinase and protein kinase C phosphorylation. J Biol Chem 1988. 263:2209-2216.
    • (1988) J Biol Chem , vol.263 , pp. 2209-2216
    • Ling, E.1    Danilov, Y.N.2    Cohen, C.M.3
  • 23
    • 0033058376 scopus 로고    scopus 로고
    • Effect of protein kinase C and insulin on Na+/H+ exchange in red blood cells of essential hypertensives
    • Ceolotto G, Sartori M, Felice M, Clari G, Bordin L, Semplicini A. Effect of protein kinase C and insulin on Na+/H+ exchange in red blood cells of essential hypertensives. J Hum Hypertens 1999. 13:321-327.
    • (1999) J Hum Hypertens , vol.13 , pp. 321-327
    • Ceolotto, G.1    Sartori, M.2    Felice, M.3    Clari, G.4    Bordin, L.5    Semplicini, A.6
  • 24
    • 0024375112 scopus 로고
    • Phosphorylation of the human erythrocyte glucose transporter by protein kinase C: Localization of the site of in vivo and in vitro phosphorylation
    • Deziel MR, Lippes HA, Rampal AL, Jung CY. Phosphorylation of the human erythrocyte glucose transporter by protein kinase C: localization of the site of in vivo and in vitro phosphorylation. Int J Biochem 1989. 21:807-814.
    • (1989) Int J Biochem , vol.21 , pp. 807-814
    • Deziel, M.R.1    Lippes, H.A.2    Rampal, A.L.3    Jung, C.Y.4
  • 25
    • 0030834974 scopus 로고    scopus 로고
    • Protein kinase C phosphorylates the a forms of plasma membrane Ca2+ pump isoforms 2 and 3 and prevents binding of calmodulin
    • Enyedi A, Elwess NL, Filoteo AG, Verma AK, Paszty K, Penniston JT. Protein kinase C phosphorylates the a forms of plasma membrane Ca2+ pump isoforms 2 and 3 and prevents binding of calmodulin. J Biol Chem 1997. 272:27525-27528.
    • (1997) J Biol Chem , vol.272 , pp. 27525-27528
    • Enyedi, A.1    Elwess, N.L.2    Filoteo, A.G.3    Verma, A.K.4    Paszty, K.5    Penniston, J.T.6
  • 26
    • 27644585878 scopus 로고    scopus 로고
    • Regulation of human erythrocyte metabolism by insulin: Cellular distribution of 6-phosphofructo-1-kinase and its implication for red blood cell function
    • Zancan P, Sola-Penna M. Regulation of human erythrocyte metabolism by insulin: cellular distribution of 6-phosphofructo-1-kinase and its implication for red blood cell function. Mol Genet Metab 2005. 86:401-411.
    • (2005) Mol Genet Metab , vol.86 , pp. 401-411
    • Zancan, P.1    Sola-Penna, M.2
  • 27
    • 77952468064 scopus 로고    scopus 로고
    • Activation of protein kinase C isoforms and its impact on diabetic complications
    • Geraldes P, King GL. Activation of protein kinase C isoforms and its impact on diabetic complications. Circ Res 2010. 106:1319-1331.
    • (2010) Circ Res , vol.106 , pp. 1319-1331
    • Geraldes, P.1    King, G.L.2
  • 30
    • 0030250879 scopus 로고    scopus 로고
    • Phosphorylation of threonine 638 critically controls the dephosphorylation and inactivation of protein kinase Calpha
    • Bornancin F, Parker PJ. Phosphorylation of threonine 638 critically controls the dephosphorylation and inactivation of protein kinase Calpha. Curr Biol 1996. 6:1114-1123.
    • (1996) Curr Biol , vol.6 , pp. 1114-1123
    • Bornancin, F.1    Parker, P.J.2
  • 31
    • 34547472118 scopus 로고    scopus 로고
    • Phorbol esters: Structure, biological activity, and toxicity in animals
    • Goel G, Makkar HP, Francis G, Becker K. Phorbol esters: structure, biological activity, and toxicity in animals. Int J Toxicol 2007. 26:279-288.
    • (2007) Int J Toxicol , vol.26 , pp. 279-288
    • Goel, G.1    Makkar, H.P.2    Francis, G.3    Becker, K.4
  • 32
    • 0032759706 scopus 로고    scopus 로고
    • Adenine nucleotide synthesis in human erythrocytes depends on the mode of supplementation of cell suspension with adenosine
    • Komarova SV, Mosharov EV, Vitvitsky VM, Ataullakhanov FI. Adenine nucleotide synthesis in human erythrocytes depends on the mode of supplementation of cell suspension with adenosine. Blood Cells Mol Dis 1999. 25:170-179.
    • (1999) Blood Cells Mol Dis , vol.25 , pp. 170-179
    • Komarova, S.V.1    Mosharov, E.V.2    Vitvitsky, V.M.3    Ataullakhanov, F.I.4
  • 34
    • 0025036574 scopus 로고
    • Facilitated diffusion of glucose
    • Carruthers A. Facilitated diffusion of glucose. Physiol Rev 1990. 70:1135-1176.
    • (1990) Physiol Rev , vol.70 , pp. 1135-1176
    • Carruthers, A.1
  • 35
    • 0022931548 scopus 로고
    • Phorbol ester- and Ca2+-dependent phosphorylation of human red cell membrane skeletal proteins
    • Cohen CM, Foley SF. Phorbol ester- and Ca2+-dependent phosphorylation of human red cell membrane skeletal proteins. J Biol Chem 1986. 261:7701-7709.
    • (1986) J Biol Chem , vol.261 , pp. 7701-7709
    • Cohen, C.M.1    Foley, S.F.2
  • 36
    • 0023161127 scopus 로고
    • Red cell deformability and its relevance to blood flow
    • Chien S. Red cell deformability and its relevance to blood flow. Annu Rev Physiol 1987. 49:177-192.
    • (1987) Annu Rev Physiol , vol.49 , pp. 177-192
    • Chien, S.1
  • 37
    • 0023189831 scopus 로고
    • Equilibrium ligand binding to the human erythrocyte sugar transporter. Evidence for two sugar-binding sites per carrier
    • Helgerson AL, Carruthers A. Equilibrium ligand binding to the human erythrocyte sugar transporter. Evidence for two sugar-binding sites per carrier. J Biol Chem 1987. 262:5464-5475.
    • (1987) J Biol Chem , vol.262 , pp. 5464-5475
    • Helgerson, A.L.1    Carruthers, A.2
  • 38
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function, and regulation
    • Newton AC. Protein kinase C: structure, function, and regulation. J Biol Chem 1995. 270:28495-28498.
    • (1995) J Biol Chem , vol.270 , pp. 28495-28498
    • Newton, A.C.1
  • 39
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka Y. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 1992. 258:607-614.
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 40
    • 0022259317 scopus 로고
    • Phosphorylation of the glucose transporter in vitro and in vivo by protein kinase C
    • Witters LA, Vater CA, Lienhard GE. Phosphorylation of the glucose transporter in vitro and in vivo by protein kinase C. Nature 1985. 315:777-778.
    • (1985) Nature , vol.315 , pp. 777-778
    • Witters, L.A.1    Vater, C.A.2    Lienhard, G.E.3
  • 41
    • 0031711701 scopus 로고    scopus 로고
    • Transmembrane phospholipid distribution in blood cells: Control mechanisms and pathophysiological significance
    • Bevers EM, Comfurius P, Dekkers DW, Harmsma M, Zwaal RF. Transmembrane phospholipid distribution in blood cells: control mechanisms and pathophysiological significance. Biol Chem 1998. 379:973-986.
    • (1998) Biol Chem , vol.379 , pp. 973-986
    • Bevers, E.M.1    Comfurius, P.2    Dekkers, D.W.3    Harmsma, M.4    Zwaal, R.F.5
  • 44
    • 12844261286 scopus 로고    scopus 로고
    • A dynamic and stationary rheological study of erythrocytes incubated in a glucose medium
    • Riquelme B, Foresto P, D'Arrigo M, Valverde J, Rasia R. A dynamic and stationary rheological study of erythrocytes incubated in a glucose medium. J Biochem Biophys Methods 2005. 62(2):131-141.
    • (2005) J Biochem Biophys Methods , vol.62 , Issue.2 , pp. 131-141
    • Riquelme, B.1    Foresto, P.2    D'Arrigo, M.3    Valverde, J.4    Rasia, R.5
  • 45
    • 38749106232 scopus 로고    scopus 로고
    • Rheological characteristics of erythrocytes incubated in glucose media
    • Shin S, Ku YH, Suh JS, Singh M. Rheological characteristics of erythrocytes incubated in glucose media. Clin Hemorheol Microcirc 2008. 38:153-161.
    • (2008) Clin Hemorheol Microcirc , vol.38 , pp. 153-161
    • Shin, S.1    Ku, Y.H.2    Suh, J.S.3    Singh, M.4
  • 46
    • 18844454493 scopus 로고    scopus 로고
    • In vitro effects of high glucose concentrations on membrane protein oxidation, G-actin and deformability of human erythrocytes
    • Resmi H, Akhunlar H, Temiz Artmann A, Guner G. In vitro effects of high glucose concentrations on membrane protein oxidation, G-actin and deformability of human erythrocytes. Cell Biochem Funct 2005. 23:163-168.
    • (2005) Cell Biochem Funct , vol.23 , pp. 163-168
    • Resmi, H.1    Akhunlar, H.2    Temiz, A.A.3    Guner, G.4
  • 47
    • 0041666333 scopus 로고    scopus 로고
    • Is the current definition for diabetes relevant to mortality risk from all causes and cardiovascular and noncardiovascular diseases?
    • DECODE Study Group, EDEG
    • DECODE Study Group, EDEG. Is the current definition for diabetes relevant to mortality risk from all causes and cardiovascular and noncardiovascular diseases? Diabetes Care 2003. 26(3):688-696.
    • (2003) Diabetes Care , vol.26 , Issue.3 , pp. 688-696
  • 48
    • 1842833576 scopus 로고    scopus 로고
    • Hyperglycaemia and mortality from all causes and from cardiovascular disease in five populations of Asian origin
    • Nakagami T. Hyperglycaemia and mortality from all causes and from cardiovascular disease in five populations of Asian origin. Diabetologia 2004. 47:385-394.
    • (2004) Diabetologia , vol.47 , pp. 385-394
    • Nakagami, T.1
  • 50
    • 0034793515 scopus 로고    scopus 로고
    • Protein kinase C isoforms in human erythrocytes
    • Govekar RB, Zingde SM. Protein kinase C isoforms in human erythrocytes. Ann Hematol 2001. 80:531-534.
    • (2001) Ann Hematol , vol.80 , pp. 531-534
    • Govekar, R.B.1    Zingde, S.M.2
  • 51
    • 0028032824 scopus 로고
    • Differential regulation of mRNAs encoding protein kinase C isoenzymes in activated human B cells
    • Brick-Ghannam C, Ericson ML, Schelle I, Charron D. Differential regulation of mRNAs encoding protein kinase C isoenzymes in activated human B cells. Hum Immunol 1994. 41:216-224.
    • (1994) Hum Immunol , vol.41 , pp. 216-224
    • Brick-Ghannam, C.1    Ericson, M.L.2    Schelle, I.3    Charron, D.4
  • 53
    • 0025159434 scopus 로고
    • Isozymes of protein kinase C in human neutrophils and their modification by two endogenous proteinases
    • Pontremoli S, Melloni E, Sparatore B, Michetti M, Salamino F, Horecker BL. Isozymes of protein kinase C in human neutrophils and their modification by two endogenous proteinases. J Biol Chem 1990. 265:706-712.
    • (1990) J Biol Chem , vol.265 , pp. 706-712
    • Pontremoli, S.1    Melloni, E.2    Sparatore, B.3    Michetti, M.4    Salamino, F.5    Horecker, B.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.