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Volumn 5, Issue 3, 2013, Pages 1226-1234

β-Glucan administration to diabetic rats alleviates oxidative stress by lowering hyperglycaemia, decreasing non-enzymatic glycation and protein O-GlcNAcylation

Author keywords

Glucan enriched extract; Advanced glycation end products; Antioxidant; Diabetes mellitus; Hyperglycaemia; O GlcNAcylation

Indexed keywords

RATTUS;

EID: 84880765831     PISSN: 17564646     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jff.2013.04.005     Document Type: Article
Times cited : (18)

References (35)
  • 2
    • 16244413938 scopus 로고    scopus 로고
    • Mechanisms of antioxidant and pro-oxidant effects of alpha-lipoic acid in the diabetic and non-diabetic kidney
    • Bhatti F., Mankhey R.W., Asico L., Quinn M.T., Welch W.J., Maric C. Mechanisms of antioxidant and pro-oxidant effects of alpha-lipoic acid in the diabetic and non-diabetic kidney. Kidney International 2005, 67:1371-1380.
    • (2005) Kidney International , vol.67 , pp. 1371-1380
    • Bhatti, F.1    Mankhey, R.W.2    Asico, L.3    Quinn, M.T.4    Welch, W.J.5    Maric, C.6
  • 3
    • 0022644227 scopus 로고
    • Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking
    • Brownlee M., Vlassara H., Kooney A., Ulrich P., Cerami A. Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking. Science 1986, 232:1629-1632.
    • (1986) Science , vol.232 , pp. 1629-1632
    • Brownlee, M.1    Vlassara, H.2    Kooney, A.3    Ulrich, P.4    Cerami, A.5
  • 4
    • 34447526486 scopus 로고    scopus 로고
    • Medicinal importance of fungal β-(1-3), (1-6)-glucans
    • Chen J., Seviour R. Medicinal importance of fungal β-(1-3), (1-6)-glucans. Mycological Research 2007, 111:635-652.
    • (2007) Mycological Research , vol.111 , pp. 635-652
    • Chen, J.1    Seviour, R.2
  • 5
    • 33646343715 scopus 로고    scopus 로고
    • Amadori-modified glycated serum proteins and accelerated atherosclerosis in diabetes: Pathogenic and therapeutic implications
    • Cohen M.P., Ziyadeh F.N., Chen S. Amadori-modified glycated serum proteins and accelerated atherosclerosis in diabetes: Pathogenic and therapeutic implications. Journal of Laboratory and Clinical Medicine 2006, 147:211-219.
    • (2006) Journal of Laboratory and Clinical Medicine , vol.147 , pp. 211-219
    • Cohen, M.P.1    Ziyadeh, F.N.2    Chen, S.3
  • 6
    • 0002474463 scopus 로고
    • Spectrophotometric studies preparations from washed blood cells
    • Drabkin D., Austin H. Spectrophotometric studies preparations from washed blood cells. Journal of Biological Chemistry 1935, 112:51-55.
    • (1935) Journal of Biological Chemistry , vol.112 , pp. 51-55
    • Drabkin, D.1    Austin, H.2
  • 7
    • 33646581015 scopus 로고    scopus 로고
    • Akt1 is dynamically modified with O-GlcNAc following treatments with PUGNAc and insulin-like growth factor-1
    • Gandy J.C., Rountree A.E., Bijur G.N. Akt1 is dynamically modified with O-GlcNAc following treatments with PUGNAc and insulin-like growth factor-1. FEBS Letters 2006, 580:3051-3058.
    • (2006) FEBS Letters , vol.580 , pp. 3051-3058
    • Gandy, J.C.1    Rountree, A.E.2    Bijur, G.N.3
  • 8
    • 0037709390 scopus 로고    scopus 로고
    • The transcription factor PDX-1 is post-translationally modified by O-linked N-acetylglucosamine and this modification is correlated with its DNA binding activity and insulin secretion in min6 beta-cells
    • Gao Y., Miyazaki J., Hart G.W. The transcription factor PDX-1 is post-translationally modified by O-linked N-acetylglucosamine and this modification is correlated with its DNA binding activity and insulin secretion in min6 beta-cells. Archives of Biochemistry and Biophysics 2003, 415:155-163.
    • (2003) Archives of Biochemistry and Biophysics , vol.415 , pp. 155-163
    • Gao, Y.1    Miyazaki, J.2    Hart, G.W.3
  • 9
    • 78349297565 scopus 로고    scopus 로고
    • Oxidative stress and diabetic complications
    • Giacco F., Brownlee M. Oxidative stress and diabetic complications. Circulation Research 2010, 107:1058-1070.
    • (2010) Circulation Research , vol.107 , pp. 1058-1070
    • Giacco, F.1    Brownlee, M.2
  • 11
    • 55649110871 scopus 로고    scopus 로고
    • O-GlcNAc modification of transcription factors, glucose sensing and glucotoxicity
    • Issad T., Kuo M. O-GlcNAc modification of transcription factors, glucose sensing and glucotoxicity. Trends in Endocrinology and Metabolism 2008, 19:380-389.
    • (2008) Trends in Endocrinology and Metabolism , vol.19 , pp. 380-389
    • Issad, T.1    Kuo, M.2
  • 12
    • 0020655989 scopus 로고
    • Fructosamine: A new approach to the estimation of serum glycosylprotein. An index of diabetic control
    • Johnson R.N., Metcalf P.A., Baker J.R. Fructosamine: A new approach to the estimation of serum glycosylprotein. An index of diabetic control. Clinica Chimica Acta 1983, 127:87-95.
    • (1983) Clinica Chimica Acta , vol.127 , pp. 87-95
    • Johnson, R.N.1    Metcalf, P.A.2    Baker, J.R.3
  • 13
    • 79959469238 scopus 로고    scopus 로고
    • O-GlcNAc modification: Friend or foe in diabetic cardiovascular disease
    • Karunakaran U., Jeoung N.H. O-GlcNAc modification: Friend or foe in diabetic cardiovascular disease. Korean Diabetes Journal 2010, 34:211-219.
    • (2010) Korean Diabetes Journal , vol.34 , pp. 211-219
    • Karunakaran, U.1    Jeoung, N.H.2
  • 14
    • 70449705798 scopus 로고    scopus 로고
    • Effects of two storage b-1,3-glucans, laminaran from Eisenia bicyclis and paramylon from Euglena gracilis, on cecal environment and plasma lipid levels in rats
    • Kuda T., Toshiki Enomoto T., Yano T. Effects of two storage b-1,3-glucans, laminaran from Eisenia bicyclis and paramylon from Euglena gracilis, on cecal environment and plasma lipid levels in rats. Journal of Functional Foods 2009, 1:399-404.
    • (2009) Journal of Functional Foods , vol.1 , pp. 399-404
    • Kuda, T.1    Toshiki Enomoto, T.2    Yano, T.3
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of heat of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of heat of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0032566537 scopus 로고    scopus 로고
    • Oxidation-reduction properties of methylglyoxal-modified protein in relation to free radical generation
    • Lee C., Yim M.B., Chock P.B., Yim H.S., Kang S.O. Oxidation-reduction properties of methylglyoxal-modified protein in relation to free radical generation. Journal of Biological Chemistry 1998, 273:25272-25278.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 25272-25278
    • Lee, C.1    Yim, M.B.2    Chock, P.B.3    Yim, H.S.4    Kang, S.O.5
  • 17
    • 33644616965 scopus 로고    scopus 로고
    • Effects of ingested fruiting bodies, submerged culture biomass, and acidic polysaccharide glucuronoxylomannan of Tremella mesenterica Retz: Fr on glycemic responses in normal and diabetic rats
    • Lo H.C., Tsai F.A., Wasser S.P., Yang J.G., Huang B.M. Effects of ingested fruiting bodies, submerged culture biomass, and acidic polysaccharide glucuronoxylomannan of Tremella mesenterica Retz: Fr on glycemic responses in normal and diabetic rats. Life Science 2006, 78:1957-1966.
    • (2006) Life Science , vol.78 , pp. 1957-1966
    • Lo, H.C.1    Tsai, F.A.2    Wasser, S.P.3    Yang, J.G.4    Huang, B.M.5
  • 18
    • 0037223526 scopus 로고    scopus 로고
    • Advanced glycosylation end products and chronic complications of diabetes mellitus
    • Mendez J.D. Advanced glycosylation end products and chronic complications of diabetes mellitus. Gaceta medica de Mexico 2003, 139:49-55.
    • (2003) Gaceta medica de Mexico , vol.139 , pp. 49-55
    • Mendez, J.D.1
  • 19
    • 84870248818 scopus 로고    scopus 로고
    • Alpha-lipoic acid preserves the structural and functional integrity of red blood cells by adjusting the redox disturbance and decreasing O-GlcNAc modifications of antioxidant enzymes and heat shock proteins in diabetic rats
    • Mihailović M., Arambašić J., Uskoković A., Dinić S., Grdović N., Marković J., et al. Alpha-lipoic acid preserves the structural and functional integrity of red blood cells by adjusting the redox disturbance and decreasing O-GlcNAc modifications of antioxidant enzymes and heat shock proteins in diabetic rats. European Journal of Nutrition 2012, 51:975-986.
    • (2012) European Journal of Nutrition , vol.51 , pp. 975-986
    • Mihailović, M.1    Arambašić, J.2    Uskoković, A.3    Dinić, S.4    Grdović, N.5    Marković, J.6
  • 21
    • 0015523099 scopus 로고
    • The role of superoxide anion in the autooxidation of epinephrine and simple assay for superoxide dismutase
    • Misra H.P., Fridovich I. The role of superoxide anion in the autooxidation of epinephrine and simple assay for superoxide dismutase. Journal of Biological Chemistry 1972, 247:3170-3175.
    • (1972) Journal of Biological Chemistry , vol.247 , pp. 3170-3175
    • Misra, H.P.1    Fridovich, I.2
  • 22
    • 0033568661 scopus 로고    scopus 로고
    • Repression of gene expression by oxidative stress
    • Morel Y., Barouki R. Repression of gene expression by oxidative stress. Biochemical Journal 1999, 342:481-496.
    • (1999) Biochemical Journal , vol.342 , pp. 481-496
    • Morel, Y.1    Barouki, R.2
  • 25
    • 0013463358 scopus 로고    scopus 로고
    • Insulin resistance of glycogen synthase mediated by O-linked N-acetylglucosamine
    • Parker G.J., Lund K.C., Taylor R.P., McClain D.A. Insulin resistance of glycogen synthase mediated by O-linked N-acetylglucosamine. Journal of Biological Chemistry 2003, 278:10022-10027.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 10022-10027
    • Parker, G.J.1    Lund, K.C.2    Taylor, R.P.3    McClain, D.A.4
  • 27
    • 34548299920 scopus 로고    scopus 로고
    • Novel inhibitors of glycation and AGE formation
    • Rahbar S. Novel inhibitors of glycation and AGE formation. Cell Biochemistry and Biophysics 2007, 48:147-157.
    • (2007) Cell Biochemistry and Biophysics , vol.48 , pp. 147-157
    • Rahbar, S.1
  • 29
    • 0035728371 scopus 로고    scopus 로고
    • Erythrocyte membrane and cytoskeletal protein glycation and oxidation in short-term diabetic rabbits
    • Resmi H., Pekçetin Ç., Güner G. Erythrocyte membrane and cytoskeletal protein glycation and oxidation in short-term diabetic rabbits. Clinical and Experimental Medicine 2001, 1:187-193.
    • (2001) Clinical and Experimental Medicine , vol.1 , pp. 187-193
    • Resmi, H.1    Pekçetin, Ç.2    Güner, G.3
  • 30
    • 0038263891 scopus 로고    scopus 로고
    • Glycemic carbohydrate and body weight regulation
    • Saris W.H. Glycemic carbohydrate and body weight regulation. Nutrition Reviews 2003, 61:10-16.
    • (2003) Nutrition Reviews , vol.61 , pp. 10-16
    • Saris, W.H.1
  • 32
    • 0035937586 scopus 로고    scopus 로고
    • Glycosylation of nucleocytoplasmic proteins: Signal transduction and O-GlcNAc
    • Wells L., Vosseller K., Hart G.W. Glycosylation of nucleocytoplasmic proteins: Signal transduction and O-GlcNAc. Science 2001, 291(2001):2376-2378.
    • (2001) Science , vol.291 , Issue.2001 , pp. 2376-2378
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 33
    • 77950898257 scopus 로고    scopus 로고
    • The RAGE Axis: A fundamental mechanism signaling danger to the vulnerable vasculature
    • Yan S.F., Ramasamy R., Schmidt A.M. The RAGE Axis: A fundamental mechanism signaling danger to the vulnerable vasculature. Circulation Research 2010, 106:842-853.
    • (2010) Circulation Research , vol.106 , pp. 842-853
    • Yan, S.F.1    Ramasamy, R.2    Schmidt, A.M.3
  • 35
    • 72449187655 scopus 로고    scopus 로고
    • The intersections between O-GlcNAcylation and phosphorylation: Implications for multiple signaling pathways
    • Zeidan Q., Hart G.W. The intersections between O-GlcNAcylation and phosphorylation: Implications for multiple signaling pathways. Journal of Cell Science 2010, 123:13-22.
    • (2010) Journal of Cell Science , vol.123 , pp. 13-22
    • Zeidan, Q.1    Hart, G.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.