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Volumn 25, Issue 3, 2010, Pages 445-458

Proteomic profiling of non-obese type 2 diabetic skeletal muscle

Author keywords

Carbonic anhydrase; Goto Kakazaki; Monoglyceride lipase; Muscle proteomics; Type 2 diabetes

Indexed keywords

3 HYDROXYISOBUTYRATE DEHYDROGENASE; 3 MERCAPTOPYRUVATE SULFOTRANSFERASE; ACYLGLYCEROL LIPASE; ADENYLATE KINASE; ALPHA ACTIN; ANAZOLENE SODIUM; BETA GLOBULIN; CARBONATE DEHYDRATASE III; COPPER ZINC SUPEROXIDE DISMUTASE; CYTOCHROME C OXIDASE; ENOLASE; FRUCTOSE BISPHOSPHATE ALDOLASE; HEAT SHOCK PROTEIN 27; IMMUNOGLOBULIN LIGHT CHAIN; ISOCITRATE DEHYDROGENASE; MUSCLE PROTEIN; PHOSPHOGLUCOMUTASE; UNCLASSIFIED DRUG;

EID: 76949100689     PISSN: 11073756     EISSN: 1791244X     Source Type: Journal    
DOI: 10.3892/ijmm_00000364     Document Type: Article
Times cited : (37)

References (53)
  • 1
    • 0031752685 scopus 로고    scopus 로고
    • Global burden of diabetes, 1995-2025: Prevalence, numerical estimates, and projections
    • King H, Aubert RE and Herman WH: Global burden of diabetes, 1995-2025: prevalence, numerical estimates, and projections. Diabetes Care 21: 1414-1431, 1998.
    • (1998) Diabetes Care , vol.21 , pp. 1414-1431
    • King, H.1    Aubert, R.E.2    Herman, W.H.3
  • 2
    • 19944363176 scopus 로고    scopus 로고
    • Genes and type 2 diabetes mellitus
    • Luna MTT: Genes and type 2 diabetes mellitus. Arch Med Res 36: 210-222, 2005.
    • (2005) Arch Med Res , vol.36 , pp. 210-222
    • Luna, M.T.T.1
  • 3
    • 1542284225 scopus 로고    scopus 로고
    • Pathophysiology of type 2 diabetes
    • Scheen AJ: Pathophysiology of type 2 diabetes. Acta Clin Belg 58: 335-341, 2003.
    • (2003) Acta Clin Belg , vol.58 , pp. 335-341
    • Scheen, A.J.1
  • 4
    • 0037026745 scopus 로고    scopus 로고
    • Pathogenesis of skeletal muscle insulin resistance in type 2 diabetes mellitus
    • Petersen KF and Shulman GI: Pathogenesis of skeletal muscle insulin resistance in type 2 diabetes mellitus. Am J Cardiol 90: G11-G18, 2002.
    • (2002) Am J Cardiol , vol.90
    • Petersen, K.F.1    Shulman, G.I.2
  • 5
    • 6344276998 scopus 로고    scopus 로고
    • Diabetes mellitus and heart failure
    • Sander GE and Giles TD: Diabetes mellitus and heart failure. Am Heart Hosp J 1: 273-280, 2003.
    • (2003) Am Heart Hosp , vol.J 1 , pp. 273-280
    • Sander, G.E.1    Giles, T.D.2
  • 8
    • 42949093113 scopus 로고    scopus 로고
    • Type 2 diabetes mellitus and skeletal muscle metabolic function
    • Phielix E and Mensink M: Type 2 diabetes mellitus and skeletal muscle metabolic function. Physiol Behav 94: 252-258, 2008.
    • (2008) Physiol Behav , vol.94 , pp. 252-258
    • Phielix, E.1    Mensink, M.2
  • 9
    • 43249083481 scopus 로고    scopus 로고
    • Free fatty acids and skeletal muscle insulin resistance
    • Kraegen EW and Cooney GJ: Free fatty acids and skeletal muscle insulin resistance. Curr Opin Lipidol 19: 235-241, 2008.
    • (2008) Curr Opin Lipidol , vol.19 , pp. 235-241
    • Kraegen, E.W.1    Cooney, G.J.2
  • 10
    • 23744438103 scopus 로고    scopus 로고
    • Diabetes mellitus in the era of proteomics
    • Korc M: Diabetes mellitus in the era of proteomics. Mol Cell Proteomics 2: 399-404, 2003.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 399-404
    • Korc, M.1
  • 12
    • 0018123653 scopus 로고
    • Activities of hepatic enzymes in spontaneous diabetes rats produced by selective breeding of normal Wistar rats
    • Kitahara A, Toyota T, Kakizaki M and Goto Y: Activities of hepatic enzymes in spontaneous diabetes rats produced by selective breeding of normal Wistar rats. Tohoku J Exp Med 126: 7-11, 1978.
    • (1978) Tohoku J Exp Med , vol.126 , pp. 7-11
    • Kitahara, A.1    Toyota, T.2    Kakizaki, M.3    Goto, Y.4
  • 13
    • 0028144530 scopus 로고
    • Impact of diabetic inheritance on glucose tolerance and insulin secretion in spontaneously diabetic GK-Wistar rats
    • Abdel-Halim SM, Guenifi A, Luthman H, Grill V, Efendic S and Ostenson CG: Impact of diabetic inheritance on glucose tolerance and insulin secretion in spontaneously diabetic GK-Wistar rats. Diabetes 43: 281-288, 1994.
    • (1994) Diabetes , vol.43 , pp. 281-288
    • Abdel-Halim, S.M.1    Guenifi, A.2    Luthman, H.3    Grill, V.4    Efendic, S.5    Ostenson, C.G.6
  • 14
    • 0030827388 scopus 로고    scopus 로고
    • Improved glucose tolerance restores insulin-stimulated Akt kinase activity and glucose transport in skeletal muscle from diabetic Goto-Kakizaki rats
    • Krook A, Kawano Y, Song XM, Efendic S, Roth RA, Wallberg-Henriksson H and Zierath JR: Improved glucose tolerance restores insulin-stimulated Akt kinase activity and glucose transport in skeletal muscle from diabetic Goto-Kakizaki rats. Diabetes 46: 2110-2114, 1997.
    • (1997) Diabetes , vol.46 , pp. 2110-2114
    • Krook, A.1    Kawano, Y.2    Song, X.M.3    Efendic, S.4    Roth, R.A.5    Wallberg-Henriksson, H.6    Zierath, J.R.7
  • 15
    • 0025877358 scopus 로고
    • Beta-cell insensitivity to glucose in the GK rat, a spontaneous nonobese model for type II diabetes
    • Portha B, Serradas P, Bailbe D, Suzuki K, Goto Y and Giroix MH: Beta-cell insensitivity to glucose in the GK rat, a spontaneous nonobese model for type II diabetes. Diabetes 40: 486-491, 1991.
    • (1991) Diabetes , vol.40 , pp. 486-491
    • Portha, B.1    Serradas, P.2    Bailbe, D.3    Suzuki, K.4    Goto, Y.5    Giroix, M.H.6
  • 16
    • 0036324622 scopus 로고    scopus 로고
    • Dysfunction of soluble guanylyl cyclase in aorta and kidney of Goto-Kakizaki rats: Influence of age and diabetic state
    • Witte K, Jacke K, Stahrenberg R, Arlt G, Reitenbach I, Schilling L and Lemmer B: Dysfunction of soluble guanylyl cyclase in aorta and kidney of Goto-Kakizaki rats: influence of age and diabetic state. Nitric Oxide 6: 85-95, 2002.
    • (2002) Nitric Oxide , vol.6 , pp. 85-95
    • Witte, K.1    Jacke, K.2    Stahrenberg, R.3    Arlt, G.4    Reitenbach, I.5    Schilling, L.6    Lemmer, B.7
  • 17
    • 27644491656 scopus 로고    scopus 로고
    • Expression of the skeletal muscle dystrophin-dystroglycan complex and syntrophin-nitric oxide synthase complex is severely affected in the type 2 diabetic Goto-Kakizaki rat
    • Mulvey C, Harno E, Keenan A and Ohlendieck K: Expression of the skeletal muscle dystrophin-dystroglycan complex and syntrophin-nitric oxide synthase complex is severely affected in the type 2 diabetic Goto-Kakizaki rat. Eur J Cell Biol 84: 867-883, 2005.
    • (2005) Eur J Cell Biol , vol.84 , pp. 867-883
    • Mulvey, C.1    Harno, E.2    Keenan, A.3    Ohlendieck, K.4
  • 18
    • 69249110069 scopus 로고    scopus 로고
    • 2+-handling apparatus in diabetes-related muscle weakness (review)
    • 2+-handling apparatus in diabetes-related muscle weakness (review). Mol Med Rep 1: 297-306, 2008.
    • (2008) Mol Med Rep , vol.1 , pp. 297-306
    • Mulvey, C.1    Mullen, E.2    Ohlendieck, K.3
  • 19
    • 0034637069 scopus 로고    scopus 로고
    • Elevated expression and activity of protein-tyrosine phosphatase 1B in skeletal muscle of insulin-resistant type II diabetic Goto-Kakizaki rats
    • Dadke SS, Li HC, Kusari AB, Begum N and Kusari J: Elevated expression and activity of protein-tyrosine phosphatase 1B in skeletal muscle of insulin-resistant type II diabetic Goto-Kakizaki rats. Biochem Biophys Res Commun 274: 583-589, 2000.
    • (2000) Biochem Biophys Res Commun , vol.274 , pp. 583-589
    • Dadke, S.S.1    Li, H.C.2    Kusari, A.B.3    Begum, N.4    Kusari, J.5
  • 20
    • 0344394280 scopus 로고    scopus 로고
    • Effect of hyperglycemia on signal transduction in skeletal muscle from diabetic Goto-Kakizaki rats
    • Steiler TL, Galuska D, Leng Y, Chibalin AV, Gilbert M and Zierath JR: Effect of hyperglycemia on signal transduction in skeletal muscle from diabetic Goto-Kakizaki rats. Endocrinology 144: 5259-5267, 2003.
    • (2003) Endocrinology , vol.144 , pp. 5259-5267
    • Steiler, T.L.1    Galuska, D.2    Leng, Y.3    Chibalin, A.V.4    Gilbert, M.5    Zierath, J.R.6
  • 21
    • 48449104125 scopus 로고    scopus 로고
    • A Combination of nutriments improves mitochondrial biogenesis and function in skeletal muscle of type 2 diabetic Goto-Kakizaki rats
    • Shen W, Hao J, Tian C, Ren J, Yang L, Li X, Luo C, Cotma CW and Liu J: A Combination of nutriments improves mitochondrial biogenesis and function in skeletal muscle of type 2 diabetic Goto-Kakizaki rats. PLoS ONE 3: E2328, 2008.
    • (2008) PLoS ONE , vol.3
    • Shen, W.1    Hao, J.2    Tian, C.3    Ren, J.4    Yang, L.5    Li, X.6    Luo, C.7    Cotma, C.W.8    Liu, J.9
  • 23
    • 34247881871 scopus 로고    scopus 로고
    • Proteomic profiling of pathological and aged skeletal muscle fibres by peptide mass fingerprinting (review)
    • Doran P, Donoghue P, O'Connell K, Gannon J and Ohlendieck K: Proteomic profiling of pathological and aged skeletal muscle fibres by peptide mass fingerprinting (review). Int J Mol Med 19: 547-564, 2007.
    • (2007) Int J Mol Med , vol.19 , pp. 547-564
    • Doran, P.1    Donoghue, P.2    O'Connell, K.3    Gannon, J.4    Ohlendieck, K.5
  • 24
    • 38349131087 scopus 로고    scopus 로고
    • Proteomic profiling of animal models mimicking skeletal muscle disorders
    • Doran P, Gannon J, O'Connell K and Ohlendieck K: Proteomic profiling of animal models mimicking skeletal muscle disorders. Proteomics Clin Appl 1: 1169-1184, 2007.
    • (2007) Proteomics Clin Appl , vol.1 , pp. 1169-1184
    • Doran, P.1    Gannon, J.2    O'Connell, K.3    Ohlendieck, K.4
  • 25
    • 33748339008 scopus 로고    scopus 로고
    • Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP
    • Doran P, Martin G, Dowling P, Jockusch H and Ohlendieck K: Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP. Proteomics 6: 4610-4621, 2006.
    • (2006) Proteomics , vol.6 , pp. 4610-4621
    • Doran, P.1    Martin, G.2    Dowling, P.3    Jockusch, H.4    Ohlendieck, K.5
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254, 1976.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 38949107303 scopus 로고    scopus 로고
    • Opposite pathobiochemical fate of pyruvate kinase and adenylate kinase in aged rat skeletal muscle as revealed by proteomic DIGE analysis
    • Doran P, O'Connell K, Gannon J, Kavanagh M and Ohlendieck K: Opposite pathobiochemical fate of pyruvate kinase and adenylate kinase in aged rat skeletal muscle as revealed by proteomic DIGE analysis. Proteomics 8: 364-377, 2008.
    • (2008) Proteomics , vol.8 , pp. 364-377
    • Doran, P.1    O'Connell, K.2    Gannon, J.3    Kavanagh, M.4    Ohlendieck, K.5
  • 29
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff V, Arold N, Taube D and Ehrhardt W: Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 9: 255-262, 1988.
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 30
    • 0021988172 scopus 로고
    • Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining
    • Heukeshoven J and Dernick R: Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining. Electrophoresis 6: 103-112, 1985.
    • (1985) Electrophoresis , vol.6 , pp. 103-112
    • Heukeshoven, J.1    Dernick, R.2
  • 31
    • 0035346790 scopus 로고    scopus 로고
    • A comparison between Sypro Ruby and ruthenium II tris (bathophenanthroline disulfonate) as fluorescent stains for protein detection in gels
    • Rabilloud T, Strub JM, Luche S, van Dorsselaer A and Lunardi J: A comparison between Sypro Ruby and ruthenium II tris (bathophenanthroline disulfonate) as fluorescent stains for protein detection in gels. Proteomics 1: 699-704, 2001.
    • (2001) Proteomics , vol.1 , pp. 699-704
    • Rabilloud, T.1    Strub, J.M.2    Luche, S.3    van Dorsselaer, A.4    Lunardi, J.5
  • 33
    • 69949091179 scopus 로고    scopus 로고
    • Drastic increase of myosin light chain MLC-2 in senescent skeletal muscle indicates fast-to-slow fibre transition in sarcopenia of old age
    • Gannon J, Doran P, Kirwan A and Ohlendieck K: Drastic increase of myosin light chain MLC-2 in senescent skeletal muscle indicates fast-to-slow fibre transition in sarcopenia of old age. Eur J Cell Biol 88: 685-700, 2009.
    • (2009) Eur J Cell Biol , vol.88 , pp. 685-700
    • Gannon, J.1    Doran, P.2    Kirwan, A.3    Ohlendieck, K.4
  • 35
    • 31344475538 scopus 로고    scopus 로고
    • 2-D protein maps of rat gastrocnemius and soleus muscles: A tool for muscle plasticity assessment
    • Gelfi C, Vigano A, De Palma S, Ripamonti M, Begum S, Cerretelli P and Wait R: 2-D protein maps of rat gastrocnemius and soleus muscles: a tool for muscle plasticity assessment. Proteomics 6: 321-340, 2006.
    • (2006) Proteomics , vol.6 , pp. 321-340
    • Gelfi, C.1    Vigano, A.2    De Palma, S.3    Ripamonti, M.4    Begum, S.5    Cerretelli, P.6    Wait, R.7
  • 36
    • 35449004149 scopus 로고    scopus 로고
    • Proteomic profiling reveals a severely perturbed protein expression pattern in aged skeletal muscle
    • O'Connell K, Gannon J, Doran P and Ohlendieck K: Proteomic profiling reveals a severely perturbed protein expression pattern in aged skeletal muscle. Int J Mol Med 20: 145-153, 2007.
    • (2007) Int J Mol Med , vol.20 , pp. 145-153
    • O'Connell, K.1    Gannon, J.2    Doran, P.3    Ohlendieck, K.4
  • 38
    • 0035294573 scopus 로고    scopus 로고
    • Separation and identification of rat skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry
    • Yan JX, Harry RA, Wait R, Welson SY, Emery PW, Preedy VR and Dunn MJ: Separation and identification of rat skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry. Proteomics 1: 424-434, 2001.
    • (2001) Proteomics , vol.1 , pp. 424-434
    • Yan, J.X.1    Harry, R.A.2    Wait, R.3    Welson, S.Y.4    Emery, P.W.5    Preedy, V.R.6    Dunn, M.J.7
  • 40
    • 34548654361 scopus 로고    scopus 로고
    • Aging skeletal muscle shows a drastic increase in the small heat shock proteins αB-crystallin/HspB5 and cvHsp/HspB7
    • Doran P, Gannon J, O'Connell K and Ohlendieck K: Aging skeletal muscle shows a drastic increase in the small heat shock proteins αB-crystallin/HspB5 and cvHsp/HspB7. Eur J Cell Biol 86: 629-640, 2007.
    • (2007) Eur J Cell Biol , vol.86 , pp. 629-640
    • Doran, P.1    Gannon, J.2    O'Connell, K.3    Ohlendieck, K.4
  • 41
    • 0035856920 scopus 로고    scopus 로고
    • Global and societal implications of the diabetes epidemic
    • Zimmet P, Alberti KG and Shaw J: Global and societal implications of the diabetes epidemic. Nature 414: 782-787, 2001.
    • (2001) Nature , vol.414 , pp. 782-787
    • Zimmet, P.1    Alberti, K.G.2    Shaw, J.3
  • 43
  • 44
    • 0034100924 scopus 로고    scopus 로고
    • Carbon dioxide transport and carbonic anhydrase in blood and muscle
    • Geers C and Gros G: Carbon dioxide transport and carbonic anhydrase in blood and muscle. Physiol Rev 80: 681-715, 2000.
    • (2000) Physiol Rev , vol.80 , pp. 681-715
    • Geers, C.1    Gros, G.2
  • 45
    • 0031560445 scopus 로고    scopus 로고
    • A polypeptide derived from mitochondrial dihydrolipoamide succinyltransferase is located on the plasma membrane of skeletal muscle
    • Matuda S, Kodama J, Goshi N, Takase C, Nakano K, Nakagawa S and Ohta S: A polypeptide derived from mitochondrial dihydrolipoamide succinyltransferase is located on the plasma membrane of skeletal muscle. Biochem Biophys Res Comm 241: 151-156, 1997.
    • (1997) Biochem Biophys Res Comm , vol.241 , pp. 151-156
    • Matuda, S.1    Kodama, J.2    Goshi, N.3    Takase, C.4    Nakano, K.5    Nakagawa, S.6    Ohta, S.7
  • 47
    • 34248161002 scopus 로고    scopus 로고
    • Coenzyme Q, oxidative stress and aging
    • Sohal RS and Forster MJ: Coenzyme Q, oxidative stress and aging. Mitochondrion 7: S103-S111, 2007.
    • (2007) Mitochondrion , vol.7
    • Sohal, R.S.1    Forster, M.J.2
  • 48
    • 17844391820 scopus 로고    scopus 로고
    • Proteome analysis of skeletal muscle from obese and morbidly obese women
    • Hittel DS, Hathout Y, Hoffman EP and Houmard JA: Proteome analysis of skeletal muscle from obese and morbidly obese women. Diabetes 54: 1283-1288, 2005.
    • (2005) Diabetes , vol.54 , pp. 1283-1288
    • Hittel, D.S.1    Hathout, Y.2    Hoffman, E.P.3    Houmard, J.A.4
  • 49
  • 51
    • 38949109352 scopus 로고    scopus 로고
    • Stentz FB and Kitabchi AE: Transcriptome and proteome expressions involved in insulin resistance in muscle and activated T-lymphocytes of patients with type 2 diabetes. Genomics Proteomics Bioinformatics 5: 216-235, 2007.
    • Stentz FB and Kitabchi AE: Transcriptome and proteome expressions involved in insulin resistance in muscle and activated T-lymphocytes of patients with type 2 diabetes. Genomics Proteomics Bioinformatics 5: 216-235, 2007.
  • 53
    • 34248180415 scopus 로고    scopus 로고
    • Two-dimensional difference gel electrophoresis
    • Viswanathan S, Unlu M and Minden JS: Two-dimensional difference gel electrophoresis. Nat Protoc 1: 1351-1358, 2006.
    • (2006) Nat Protoc , vol.1 , pp. 1351-1358
    • Viswanathan, S.1    Unlu, M.2    Minden, J.S.3


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