메뉴 건너뛰기




Volumn 2, Issue 5, 2008, Pages 654-669

Proteomic studies in animal models of diabetes

Author keywords

Animal models of diabetes; Diabetic complications; Diabetic treatment; Type 1 2 diabetes

Indexed keywords

2 [(4 CHLOROPHENOXY)METHYL] 7A (3,4 DICHLOROPHENYL)TETRAHYDROPYRROLO[2,1 B]OXAZOL 5(6H) ONE; ANTIDIABETIC AGENT; APOLIPOPROTEIN A1; APOLIPOPROTEIN A4; CALBINDIN; CHAPERONE; DIPEPTIDYL PEPTIDASE IV INHIBITOR; GLITAZONE DERIVATIVE; GLUCAGON LIKE PEPTIDE 1 DERIVATIVE; GLUTAMATE DEHYDROGENASE; HAPTOGLOBIN; HYDROXYPYRUVATE REDUCTASE; INSULIN; IOXAGLIC ACID; METFORMIN; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR AGONIST; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR ALPHA AGONIST; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA AGONIST; PIRINIXIC ACID; ROSIGLITAZONE; SULFONYLUREA;

EID: 44649118613     PISSN: 18628346     EISSN: None     Source Type: Journal    
DOI: 10.1002/prca.200780030     Document Type: Review
Times cited : (7)

References (84)
  • 1
  • 2
    • 0035856920 scopus 로고    scopus 로고
    • Global and societal implications of the diabetes epidemic
    • Zimmet, P., Alberti, K. G., Shaw, J., Global and societal implications of the diabetes epidemic. Nature 2001, 414, 782-787.
    • (2001) Nature , vol.414 , pp. 782-787
    • Zimmet, P.1    Alberti, K.G.2    Shaw, J.3
  • 4
    • 0016637146 scopus 로고
    • Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissues. A novel approach to testing for induced point mutations in mammals
    • Klose, J., Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissues. A novel approach to testing for induced point mutations in mammals. Human-genetik 1975, 26, 231-243.
    • (1975) Human-genetik , vol.26 , pp. 231-243
    • Klose, J.1
  • 5
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P. H., High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 1975, 250, 4007-4021.
    • (1975) J. Biol. Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 6
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • Gorg, A., Weiss, W., Dunn, M. J., Current two-dimensional electrophoresis technology for proteomics. Proteomics 2004, 4, 3665-3685.
    • (2004) Proteomics , vol.4 , pp. 3665-3685
    • Gorg, A.1    Weiss, W.2    Dunn, M.J.3
  • 7
    • 33750575732 scopus 로고    scopus 로고
    • Protein stains for proteomic applications: Which, when, why?
    • Miller, I., Crawford, J., Gianazza, E., Protein stains for proteomic applications: which, when, why? Proteomics 2006, 6, 5385-5408.
    • (2006) Proteomics , vol.6 , pp. 5385-5408
    • Miller, I.1    Crawford, J.2    Gianazza, E.3
  • 8
    • 26444574929 scopus 로고    scopus 로고
    • Protein detection methods in proteomics research
    • Westermeier, R., Marouga, R., Protein detection methods in proteomics research. Biosci. Reports 2005, 25, 19-32.
    • (2005) Biosci. Reports , vol.25 , pp. 19-32
    • Westermeier, R.1    Marouga, R.2
  • 9
    • 14644429693 scopus 로고    scopus 로고
    • Numerical approaches for quantitative analysis of two-dimensional maps: A review of commercial software and home-made systems
    • Marengo, E., Robotti, E., Antonucci, F., Cecconi, D. et al., Numerical approaches for quantitative analysis of two-dimensional maps: a review of commercial software and home-made systems. Proteomics 2005, 5, 654-666.
    • (2005) Proteomics , vol.5 , pp. 654-666
    • Marengo, E.1    Robotti, E.2    Antonucci, F.3    Cecconi, D.4
  • 10
    • 0037253267 scopus 로고    scopus 로고
    • A novel experimental design for comparative two-dimensional gel analysis: Two-dimensional difference gel electrophoresis incorporating a pooled internal standard
    • Alban, A., David, S. O., Bjorkesten, L., Andersson, C. et al., A novel experimental design for comparative two-dimensional gel analysis: two-dimensional difference gel electrophoresis incorporating a pooled internal standard. Proteomics 2003, 3, 36-44.
    • (2003) Proteomics , vol.3 , pp. 36-44
    • Alban, A.1    David, S.O.2    Bjorkesten, L.3    Andersson, C.4
  • 11
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu, M., Morgan, M. E., Minden, J. S., Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 1997, 18, 2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 12
    • 33746102929 scopus 로고    scopus 로고
    • separation, identification and quantification
    • Proteome research based on modern liquid chromatography-tandem mass spectrometry
    • Frohlich, T., Arnold, G. J., Proteome research based on modern liquid chromatography-tandem mass spectrometry: separation, identification and quantification. J. Neural Transm. 2006, 113, 973-994.
    • (2006) J. Neural Transm , vol.113 , pp. 973-994
    • Frohlich, T.1    Arnold, G.J.2
  • 13
    • 34250372908 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture for quantitative proteomics
    • Ong, S. E., Mann, M., Stable isotope labeling by amino acids in cell culture for quantitative proteomics. Methods Mol. Biol. (Clifton NJ) 2007, 359, 37-52.
    • (2007) Methods Mol. Biol. (Clifton NJ) , vol.359 , pp. 37-52
    • Ong, S.E.1    Mann, M.2
  • 14
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross, P. L., Huang, Y. N., Marchese, J. N., Williamson, B. et al., Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell. Proteomics 2004, 3, 1154-1169.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3    Williamson, B.4
  • 15
    • 20644442887 scopus 로고    scopus 로고
    • MSight: An image analysis software for liquid chromatography-mass spectrometry
    • Palagi, P. M., Walther, D., Quadroni, M., Catherinet, S. et al., MSight: an image analysis software for liquid chromatography-mass spectrometry. Proteomics 2005, 5, 2381-2384.
    • (2005) Proteomics , vol.5 , pp. 2381-2384
    • Palagi, P.M.1    Walther, D.2    Quadroni, M.3    Catherinet, S.4
  • 16
    • 3142773316 scopus 로고    scopus 로고
    • Multiplexed sandwich assays in microarray format
    • Nielsen, U. B., Geierstanger, B. H., Multiplexed sandwich assays in microarray format. J. Immunol. Methods 2004, 290, 107-120.
    • (2004) J. Immunol. Methods , vol.290 , pp. 107-120
    • Nielsen, U.B.1    Geierstanger, B.H.2
  • 17
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber, S. A., Rush, J., Stemman, O., Kirschner, M. W., Gygi, S. P., Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc. Natl. Acad. Sci. USA 2003, 100, 6940-6945.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 18
    • 0028362968 scopus 로고
    • Nicotinamide prevents interleukin-1 effects on accumulated insulin release and nitric oxide production in rat islets of Langerhans
    • Andersen, H. U., Jorgensen, K. H., Egeberg, J., Mandrup-Poulsen, T., Nerup, J., Nicotinamide prevents interleukin-1 effects on accumulated insulin release and nitric oxide production in rat islets of Langerhans. Diabetes 1994, 43, 770-777.
    • (1994) Diabetes , vol.43 , pp. 770-777
    • Andersen, H.U.1    Jorgensen, K.H.2    Egeberg, J.3    Mandrup-Poulsen, T.4    Nerup, J.5
  • 19
    • 0022596377 scopus 로고
    • Affinity-purified human interleukin I is cytotoxic to isolated islets of Langerhans
    • Mandrup-Poulsen, T., Bendtzen, K., Nerup, J., Dinarello, C. A. et al., Affinity-purified human interleukin I is cytotoxic to isolated islets of Langerhans. Diabetologia 1986, 29, 63-67.
    • (1986) Diabetologia , vol.29 , pp. 63-67
    • Mandrup-Poulsen, T.1    Bendtzen, K.2    Nerup, J.3    Dinarello, C.A.4
  • 20
    • 0026633029 scopus 로고
    • Interleukin-1 beta increases the activity of superoxide dismutase in rat pancreatic islets
    • Borg, L. A., Cagliero, E., Sandler, S., Welsh, N., Eizirik, D. L., Interleukin-1 beta increases the activity of superoxide dismutase in rat pancreatic islets. Endocrinology 1992, 130, 2851-2857.
    • (1992) Endocrinology , vol.130 , pp. 2851-2857
    • Borg, L.A.1    Cagliero, E.2    Sandler, S.3    Welsh, N.4    Eizirik, D.L.5
  • 21
    • 0032585927 scopus 로고    scopus 로고
    • IL-1beta induces serine protease inhibitor 3 (SPI-3) gene expression in rat pancreatic beta-cells. Detection by differential display of messenger RNA
    • Chen, M. C., Schuit, F., Pipeleers, D. G., Eizirik, D. L., IL-1beta induces serine protease inhibitor 3 (SPI-3) gene expression in rat pancreatic beta-cells. Detection by differential display of messenger RNA. Cytokine 1999, 11, 856-862.
    • (1999) Cytokine , vol.11 , pp. 856-862
    • Chen, M.C.1    Schuit, F.2    Pipeleers, D.G.3    Eizirik, D.L.4
  • 22
    • 0030608664 scopus 로고    scopus 로고
    • Interleukin-1beta induced changes in the protein expression of rat islets: A computerized database
    • Andersen, H. U., Fey, S. J., Larsen, P. M., Nawrocki, A. et al., Interleukin-1beta induced changes in the protein expression of rat islets: a computerized database. Electrophoresis 1997, 18, 2091-2103.
    • (1997) Electrophoresis , vol.18 , pp. 2091-2103
    • Andersen, H.U.1    Fey, S.J.2    Larsen, P.M.3    Nawrocki, A.4
  • 23
    • 0035033679 scopus 로고    scopus 로고
    • Proteome analysis of interleukin-1beta-induced changes in protein expression in rat islets of Langerhans
    • Larsen, P. M., Fey, S. J., Larsen, M. R., Nawrocki, A. et al., Proteome analysis of interleukin-1beta-induced changes in protein expression in rat islets of Langerhans. Diabetes 2001, 50, 1056-1063.
    • (2001) Diabetes , vol.50 , pp. 1056-1063
    • Larsen, P.M.1    Fey, S.J.2    Larsen, M.R.3    Nawrocki, A.4
  • 24
    • 0033869974 scopus 로고    scopus 로고
    • Islet protein expression changes during diabetes development in islet syngrafts in BB-DP rats and during rejection of BB-DP islet allografts
    • Christensen, U. B., Larsen, P. M., Fey, S. J., Andersen, H. U. et al., Islet protein expression changes during diabetes development in islet syngrafts in BB-DP rats and during rejection of BB-DP islet allografts. Autoimmunity 2000, 32, 1-15.
    • (2000) Autoimmunity , vol.32 , pp. 1-15
    • Christensen, U.B.1    Larsen, P.M.2    Fey, S.J.3    Andersen, H.U.4
  • 25
    • 0036435663 scopus 로고    scopus 로고
    • IL-1beta induced protein changes in diabetes prone BB rat islets of Langerhans identified by proteome analysis
    • Sparre, T., Christensen, U. B., Mose Larsen, P., Fey, S. J. et al., IL-1beta induced protein changes in diabetes prone BB rat islets of Langerhans identified by proteome analysis. Diabetologia 2002, 45, 1550-1561.
    • (2002) Diabetologia , vol.45 , pp. 1550-1561
    • Sparre, T.1    Christensen, U.B.2    Mose Larsen, P.3    Fey, S.J.4
  • 26
    • 2942596542 scopus 로고    scopus 로고
    • Changes in expression of IL-1 beta influenced proteins in transplanted islets during development of diabetes in diabetes-prone BB rats
    • Sparre, T., Christensen, U. B., Gotfredsen, C. F., Larsen, P. M. et al., Changes in expression of IL-1 beta influenced proteins in transplanted islets during development of diabetes in diabetes-prone BB rats. Diabetologia 2004, 47, 892-908.
    • (2004) Diabetologia , vol.47 , pp. 892-908
    • Sparre, T.1    Christensen, U.B.2    Gotfredsen, C.F.3    Larsen, P.M.4
  • 28
    • 0029817047 scopus 로고    scopus 로고
    • The role of interleukin-1 in the pathogenesis of IDDM
    • Mandrup-Poulsen, T., The role of interleukin-1 in the pathogenesis of IDDM. Diabetologia 1996, 39, 1005-1029.
    • (1996) Diabetologia , vol.39 , pp. 1005-1029
    • Mandrup-Poulsen, T.1
  • 29
    • 33746956078 scopus 로고    scopus 로고
    • Different islet protein expression profiles during spontaneous diabetes development vs. allograft rejection in BB-DP rats
    • Christensen, U. B., Larsen, P. M., Fey, S., Karlsen, A. E. et al., Different islet protein expression profiles during spontaneous diabetes development vs. allograft rejection in BB-DP rats. Autoimmunity 2006, 39, 315-321.
    • (2006) Autoimmunity , vol.39 , pp. 315-321
    • Christensen, U.B.1    Larsen, P.M.2    Fey, S.3    Karlsen, A.E.4
  • 30
    • 33745626777 scopus 로고    scopus 로고
    • D'Hertog, W., Mathieu, C., Overbergh, L., Type 1 diabetes: entering the proteomic era. Expert Rev. Proteomics 2006, 3, 223-236.
    • D'Hertog, W., Mathieu, C., Overbergh, L., Type 1 diabetes: entering the proteomic era. Expert Rev. Proteomics 2006, 3, 223-236.
  • 31
    • 17844364214 scopus 로고    scopus 로고
    • Unraveling the pathogenesis of type 1 diabetes with proteomics: Present and future directions
    • Sparre, T., Larsen, M. R., Heding, P. E., Karlsen, A. E. et al., Unraveling the pathogenesis of type 1 diabetes with proteomics: present and future directions. Mol. Cell. Proteomics 2005, 4, 441-457.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 441-457
    • Sparre, T.1    Larsen, M.R.2    Heding, P.E.3    Karlsen, A.E.4
  • 32
    • 33751072352 scopus 로고    scopus 로고
    • Serum, liver, and kidney proteomic analysis for the alloxan-induced type I diabetic mice after insulin gene transfer of naked plasmid through electroporation
    • Diao, W. F., Chen, W. Q., Wu, Y., Liu, P. et al., Serum, liver, and kidney proteomic analysis for the alloxan-induced type I diabetic mice after insulin gene transfer of naked plasmid through electroporation. Proteomics 2006, 6, 5837-5845.
    • (2006) Proteomics , vol.6 , pp. 5837-5845
    • Diao, W.F.1    Chen, W.Q.2    Wu, Y.3    Liu, P.4
  • 33
    • 14844296371 scopus 로고    scopus 로고
    • New insights into amino acid metabolism, beta-cell function and diabetes
    • Newsholme, P., Brennan, L., Rubi, B., Maechler, P., New insights into amino acid metabolism, beta-cell function and diabetes. Clin. Sci. (Lond) 2005, 108, 185-194.
    • (2005) Clin. Sci. (Lond) , vol.108 , pp. 185-194
    • Newsholme, P.1    Brennan, L.2    Rubi, B.3    Maechler, P.4
  • 34
    • 1542374749 scopus 로고    scopus 로고
    • Insulin secretion profiles are modified by over-expression of glutamate dehydrogenase in pancreatic islets
    • Carobbio, S., Ishihara, H., Fernandez-Pascual, S., Bartley, C. et al., Insulin secretion profiles are modified by over-expression of glutamate dehydrogenase in pancreatic islets. Diabetologia 2004, 47, 266-276.
    • (2004) Diabetologia , vol.47 , pp. 266-276
    • Carobbio, S.1    Ishihara, H.2    Fernandez-Pascual, S.3    Bartley, C.4
  • 35
    • 0022994713 scopus 로고
    • Alterations in plasma levels of apolipoprotein A-IV in various clinical entities
    • Miyata, V., Koga, S., Ibayashi, H., Alterations in plasma levels of apolipoprotein A-IV in various clinical entities. Gastroenterol. Jpn. 1986, 21, 479-485.
    • (1986) Gastroenterol. Jpn , vol.21 , pp. 479-485
    • Miyata, V.1    Koga, S.2    Ibayashi, H.3
  • 36
    • 0034789428 scopus 로고    scopus 로고
    • Effect of the inflammation, chronic hyperglycemia, or malabsorption on the apolipoprotein A-IV concentration in type 1 diabetes mellitus and in diabetes secondary to chronic pancreatitis
    • Quilliot, D., Walters, E., Guerci, B., Fruchart, J. C. et al., Effect of the inflammation, chronic hyperglycemia, or malabsorption on the apolipoprotein A-IV concentration in type 1 diabetes mellitus and in diabetes secondary to chronic pancreatitis. Metabolism 2001, 50, 1019-1024.
    • (2001) Metabolism , vol.50 , pp. 1019-1024
    • Quilliot, D.1    Walters, E.2    Guerci, B.3    Fruchart, J.C.4
  • 37
    • 0029055371 scopus 로고    scopus 로고
    • Verges, B., Apolipoprotein A-IV in diabetes mellitus. Diabete Metab. 1995, 21, 99-105.
    • Verges, B., Apolipoprotein A-IV in diabetes mellitus. Diabete Metab. 1995, 21, 99-105.
  • 39
    • 0024454923 scopus 로고
    • Increased levels of acute-phase serum proteins in diabetes
    • McMillan, D. E., Increased levels of acute-phase serum proteins in diabetes. Metabolism 1989, 38, 1042-1046.
    • (1989) Metabolism , vol.38 , pp. 1042-1046
    • McMillan, D.E.1
  • 40
    • 33646229805 scopus 로고    scopus 로고
    • Proteomic analysis of differential protein expression in early process of pancreatic regeneration in pancreatectomized rats
    • Yang, M., Liu, W., Wang, C. Y., Liu, T. et al., Proteomic analysis of differential protein expression in early process of pancreatic regeneration in pancreatectomized rats. Acta Pharmacol. Sin. 2006, 27, 568-578.
    • (2006) Acta Pharmacol. Sin , vol.27 , pp. 568-578
    • Yang, M.1    Liu, W.2    Wang, C.Y.3    Liu, T.4
  • 41
    • 0029034804 scopus 로고
    • Sequential expression and differential localization of I-, L-, and T-fimbrin during differentiation of the mouse intestine and yolk sac
    • Chafel, M. M., Shen, W., Matsudaira, P., Sequential expression and differential localization of I-, L-, and T-fimbrin during differentiation of the mouse intestine and yolk sac. Dev. Dyn. 1995, 203, 141-151.
    • (1995) Dev. Dyn , vol.203 , pp. 141-151
    • Chafel, M.M.1    Shen, W.2    Matsudaira, P.3
  • 42
    • 0030057595 scopus 로고    scopus 로고
    • Vimentin filaments follow the preexisting cytokeratin network during epithelial-mesenchymal transition of cultured neonatal rat hepatocytes
    • Pagan, R., Martin, I., Alonso, A., Llobera, M., Vilaro, S., Vimentin filaments follow the preexisting cytokeratin network during epithelial-mesenchymal transition of cultured neonatal rat hepatocytes. Exp. Cell Res. 1996, 222, 333-344.
    • (1996) Exp. Cell Res , vol.222 , pp. 333-344
    • Pagan, R.1    Martin, I.2    Alonso, A.3    Llobera, M.4    Vilaro, S.5
  • 43
    • 0032841562 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transition in proliferative vitreoretinopathy: Intermediate filament protein expression in retinal pigment epithelial cells
    • Casaroli-Marano, R. P., Pagan, R., Vilaro, S., Epithelial-mesenchymal transition in proliferative vitreoretinopathy: intermediate filament protein expression in retinal pigment epithelial cells. Invest. Ophthalmol. Vis. Sci. 1999, 40, 2062-2072.
    • (1999) Invest. Ophthalmol. Vis. Sci , vol.40 , pp. 2062-2072
    • Casaroli-Marano, R.P.1    Pagan, R.2    Vilaro, S.3
  • 44
    • 0034917293 scopus 로고    scopus 로고
    • Expression of Xenopus L-arginine:glycine amidinotransferase (XAT) during early embryonic development
    • Zhao, H., Cao, Y., Grunz, H., Expression of Xenopus L-arginine:glycine amidinotransferase (XAT) during early embryonic development. Dev. Genes Evol. 2001, 211, 358-360.
    • (2001) Dev. Genes Evol , vol.211 , pp. 358-360
    • Zhao, H.1    Cao, Y.2    Grunz, H.3
  • 45
    • 33644669952 scopus 로고    scopus 로고
    • New data analysis and mining approaches identify unique proteome and transcriptome markers of susceptibility to autoimmune diabetes
    • Gerling, I. C., Singh, S., Lenchik, N. I., Marshall, D. R., Wu, J., New data analysis and mining approaches identify unique proteome and transcriptome markers of susceptibility to autoimmune diabetes. Mol. Cell. Proteomics 2006, 5, 293-305.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 293-305
    • Gerling, I.C.1    Singh, S.2    Lenchik, N.I.3    Marshall, D.R.4    Wu, J.5
  • 46
    • 17644361955 scopus 로고    scopus 로고
    • a model of immune dysregulation
    • The NOD mouse
    • Anderson, M. S., Bluestone, J. A., The NOD mouse: a model of immune dysregulation. Ann. Rev. Immunol. 2005, 23, 447-485.
    • (2005) Ann. Rev. Immunol , vol.23 , pp. 447-485
    • Anderson, M.S.1    Bluestone, J.A.2
  • 47
    • 19344362719 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis characterization of the mouse leukocyte proteome, using a tri-reagent for protein extraction
    • Lenchik, N. I., Desiderio, D. M., Gerling, I. C., Two-dimensional gel electrophoresis characterization of the mouse leukocyte proteome, using a tri-reagent for protein extraction. Proteomics 2005, 5, 2202-2209.
    • (2005) Proteomics , vol.5 , pp. 2202-2209
    • Lenchik, N.I.1    Desiderio, D.M.2    Gerling, I.C.3
  • 48
    • 0035225642 scopus 로고    scopus 로고
    • The mouse SWISS-2D PAGE database: A tool for proteomics study of diabetes and obesity
    • Sanchez, J. C., Chiappe, D., Converset, V., Hoogland, C. et al., The mouse SWISS-2D PAGE database: a tool for proteomics study of diabetes and obesity. Proteomics 2001, 1, 136-163.
    • (2001) Proteomics , vol.1 , pp. 136-163
    • Sanchez, J.C.1    Chiappe, D.2    Converset, V.3    Hoogland, C.4
  • 49
    • 3543009434 scopus 로고    scopus 로고
    • The high-fat diet-fed mouse: A model for studying mechanisms and treatment of impaired glucose tolerance and type 2 diabetes
    • Winzell, M. S., Ahren, B., The high-fat diet-fed mouse: a model for studying mechanisms and treatment of impaired glucose tolerance and type 2 diabetes. Diabetes 2004, 53 Suppl 3, S215-219.
    • (2004) Diabetes , vol.53 , Issue.SUPPL. 3
    • Winzell, M.S.1    Ahren, B.2
  • 50
    • 33845934827 scopus 로고    scopus 로고
    • Enhanced mitochondrial metabolism may account for the adaptation to insulin resistance in islets from C57BL/6J mice fed a high-fat diet
    • Fex, M., Nitert, M. D., Wierup, N., Sundler, F. et al., Enhanced mitochondrial metabolism may account for the adaptation to insulin resistance in islets from C57BL/6J mice fed a high-fat diet. Diabetologia 2007, 50, 74-83.
    • (2007) Diabetologia , vol.50 , pp. 74-83
    • Fex, M.1    Nitert, M.D.2    Wierup, N.3    Sundler, F.4
  • 51
    • 24044453711 scopus 로고    scopus 로고
    • Proteomic profiling of hepatic endoplasmic reticulum-associated proteins in an animal model of insulin resistance and metabolic dyslipidemia
    • Morand, J. P., Macri, J., Adeli, K., Proteomic profiling of hepatic endoplasmic reticulum-associated proteins in an animal model of insulin resistance and metabolic dyslipidemia. J. Biol. Chem. 2005, 280, 17626-17633.
    • (2005) J. Biol. Chem , vol.280 , pp. 17626-17633
    • Morand, J.P.1    Macri, J.2    Adeli, K.3
  • 52
    • 0242524321 scopus 로고    scopus 로고
    • Intrauterine programming of fetal islet gene expression in rats-effects of maternal protein restriction during gestation revealed by proteome analysis
    • Sparre, T., Reusens, B., Cherif, H., Larsen, M. R. et al., Intrauterine programming of fetal islet gene expression in rats-effects of maternal protein restriction during gestation revealed by proteome analysis. Diabetologia 2003, 46, 1497-1511.
    • (2003) Diabetologia , vol.46 , pp. 1497-1511
    • Sparre, T.1    Reusens, B.2    Cherif, H.3    Larsen, M.R.4
  • 53
    • 33750839046 scopus 로고    scopus 로고
    • Differential serum proteomic analysis in a model of metabolic disease
    • Matsumura, T., Suzuki, T., Kada, N., Aizawa, K. et al., Differential serum proteomic analysis in a model of metabolic disease. Biochem. Biophys. Res. Commun. 2006, 351, 965-971.
    • (2006) Biochem. Biophys. Res. Commun , vol.351 , pp. 965-971
    • Matsumura, T.1    Suzuki, T.2    Kada, N.3    Aizawa, K.4
  • 54
    • 28844468987 scopus 로고    scopus 로고
    • Peptidomics biomarker discovery in mouse models of obesity and type 2 diabetes
    • Budde, P., Schulte, I., Appel, A., Neitz, S. et al., Peptidomics biomarker discovery in mouse models of obesity and type 2 diabetes. Comb. Chem. High Throughput Screen. 2005, 8, 775-781.
    • (2005) Comb. Chem. High Throughput Screen , vol.8 , pp. 775-781
    • Budde, P.1    Schulte, I.2    Appel, A.3    Neitz, S.4
  • 55
    • 8844268481 scopus 로고    scopus 로고
    • Discovering disease-associated enzymes by proteome reactivity profiling
    • Barglow, K. T., Cravatt, B. F., Discovering disease-associated enzymes by proteome reactivity profiling. Chem. Biol. 2004, 11, 1523-1531.
    • (2004) Chem. Biol , vol.11 , pp. 1523-1531
    • Barglow, K.T.1    Cravatt, B.F.2
  • 56
    • 0033522908 scopus 로고    scopus 로고
    • Flux of the L-serine metabolism in rat liver. The predominant contribution of serine dehydratase
    • Xue, H. H., Fujie, M., Sakaguchi, T., Oda, T. et al., Flux of the L-serine metabolism in rat liver. The predominant contribution of serine dehydratase. J. Biol. Chem. 1999, 274, 16020-16027.
    • (1999) J. Biol. Chem , vol.274 , pp. 16020-16027
    • Xue, H.H.1    Fujie, M.2    Sakaguchi, T.3    Oda, T.4
  • 57
    • 0033523088 scopus 로고    scopus 로고
    • Flux of the L-serine metabolism in rabbit, human, and dog livers. Substantial contributions of both mitochondrial and peroxisomal serine:pyruvate/ alanine:glyoxylate aminotransferase
    • Xue, H. H., Sakaguchi, T., Fujie, M., Ogawa, H., Ichiyama, A., Flux of the L-serine metabolism in rabbit, human, and dog livers. Substantial contributions of both mitochondrial and peroxisomal serine:pyruvate/ alanine:glyoxylate aminotransferase. J. Biol. Cchem. 1999, 274, 16028-16033.
    • (1999) J. Biol. Cchem , vol.274 , pp. 16028-16033
    • Xue, H.H.1    Sakaguchi, T.2    Fujie, M.3    Ogawa, H.4    Ichiyama, A.5
  • 58
    • 34247361278 scopus 로고    scopus 로고
    • Carbonylation of adipose proteins in obesity and insulin resistance: Identification of adipocyte fatty acid-binding protein as a cellular target of 4-hydroxynonenal
    • Grimsrud, P.A., Picklo Sr, M. J., Griffin, T. J., Bernlohr, D. A., Carbonylation of adipose proteins in obesity and insulin resistance: Identification of adipocyte fatty acid-binding protein as a cellular target of 4-hydroxynonenal. Mol. Cell. Proteomics 2007.
    • (2007) Mol. Cell. Proteomics
    • Grimsrud, P.A.1    Picklo Sr, M.J.2    Griffin, T.J.3    Bernlohr, D.A.4
  • 59
    • 33745833415 scopus 로고    scopus 로고
    • Inflammatory response in white adipose tissue in the non-obese hormone-sensitive lipase null mouse model
    • Hansson, O., Strom, K., Guner, N., Wierup, N. et al., Inflammatory response in white adipose tissue in the non-obese hormone-sensitive lipase null mouse model. J. Proteome Res. 2006, 5, 1701-1710.
    • (2006) J. Proteome Res , vol.5 , pp. 1701-1710
    • Hansson, O.1    Strom, K.2    Guner, N.3    Wierup, N.4
  • 60
    • 0042316795 scopus 로고    scopus 로고
    • Quantitative protein profiling in heart mitochondria from diabetic rats
    • Turko, I. V., Murad, F., Quantitative protein profiling in heart mitochondria from diabetic rats. J. Biol. Cchem. 2003, 278, 35844-35849.
    • (2003) J. Biol. Cchem , vol.278 , pp. 35844-35849
    • Turko, I.V.1    Murad, F.2
  • 61
    • 0036023992 scopus 로고    scopus 로고
    • Quantitative analysis of two-dimensional gel-separated proteins using isotopically marked alkylating agents and matrix-assisted laser desorption/ionization mass spectrometry
    • Gehanne, S., Cecconi, D., Carboni, L., Righetti, P. G. et al., Quantitative analysis of two-dimensional gel-separated proteins using isotopically marked alkylating agents and matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun. Mass Spectrom. 2002, 16, 1692-1698.
    • (2002) Rapid Commun. Mass Spectrom , vol.16 , pp. 1692-1698
    • Gehanne, S.1    Cecconi, D.2    Carboni, L.3    Righetti, P.G.4
  • 62
    • 0035983628 scopus 로고    scopus 로고
    • A method to identify and simultaneously determine the relative quantities of proteins isolated by gel electrophoresis
    • Sechi, S., A method to identify and simultaneously determine the relative quantities of proteins isolated by gel electrophoresis. Rapid Commun. Mass Spectrom. 2002, 16, 1416-1424.
    • (2002) Rapid Commun. Mass Spectrom , vol.16 , pp. 1416-1424
    • Sechi, S.1
  • 63
    • 6044224889 scopus 로고    scopus 로고
    • Cardiac mitochondrial damage and biogenesis in a chronic model of type 1 diabetes
    • Shen, X., Zheng, S., Thongboonkerd, V., Xu, M. et al., Cardiac mitochondrial damage and biogenesis in a chronic model of type 1 diabetes. Am. J. Physiol. Endocrinol. Metab. 2004, 287, E896-905.
    • (2004) Am. J. Physiol. Endocrinol. Metab , vol.287
    • Shen, X.1    Zheng, S.2    Thongboonkerd, V.3    Xu, M.4
  • 64
    • 0024459130 scopus 로고
    • Calmodulin-induced early-onset diabetes in transgenic mice
    • Epstein, P. N., Overbeek, P. A., Means, A. R., Calmodulin-induced early-onset diabetes in transgenic mice. Cell 1989, 58, 1067-1073.
    • (1989) Cell , vol.58 , pp. 1067-1073
    • Epstein, P.N.1    Overbeek, P.A.2    Means, A.R.3
  • 65
    • 34047111193 scopus 로고    scopus 로고
    • Alterations in the diabetic myocardial proteome coupled with increased myocardial oxidative stress underlies diabetic cardiomyopathy
    • Hamblin, M., Friedman, D. B., Hill, S., Caprioli, R. M. et al., Alterations in the diabetic myocardial proteome coupled with increased myocardial oxidative stress underlies diabetic cardiomyopathy. J. Mol. Cell. Cardiol. 2007.
    • (2007) J. Mol. Cell. Cardiol
    • Hamblin, M.1    Friedman, D.B.2    Hill, S.3    Caprioli, R.M.4
  • 66
    • 9444262472 scopus 로고    scopus 로고
    • Development of late-stage diabetic nephropathy in OVE26 diabetic mice
    • Zheng, S., Noonan, W. T., Metreveli, N. S., Coventry, S. et al., Development of late-stage diabetic nephropathy in OVE26 diabetic mice. Diabetes 2004, 53, 3248-3257.
    • (2004) Diabetes , vol.53 , pp. 3248-3257
    • Zheng, S.1    Noonan, W.T.2    Metreveli, N.S.3    Coventry, S.4
  • 67
    • 0030766387 scopus 로고    scopus 로고
    • Ultrastructural and functional analyses of nephropathy in calmodulin-induced diabetic transgenic mice
    • Carlson, E. C., Audette, J. L., Klevay, L. M., Nguyen, H., Epstein, P. N., Ultrastructural and functional analyses of nephropathy in calmodulin-induced diabetic transgenic mice. Anat. Rec. 1997, 247, 9-19.
    • (1997) Anat. Rec , vol.247 , pp. 9-19
    • Carlson, E.C.1    Audette, J.L.2    Klevay, L.M.3    Nguyen, H.4    Epstein, P.N.5
  • 68
    • 10744221885 scopus 로고    scopus 로고
    • Alterations in the renal elastin-elastase system in type 1 diabetic nephropathy identified by proteomic analysis
    • Thongboonkerd, V., Barati, M. T., McLeish, K. R., Benarafa, C. et al., Alterations in the renal elastin-elastase system in type 1 diabetic nephropathy identified by proteomic analysis. J. Am. Soc. Nephrol. 2004, 15, 650-662.
    • (2004) J. Am. Soc. Nephrol , vol.15 , pp. 650-662
    • Thongboonkerd, V.1    Barati, M.T.2    McLeish, K.R.3    Benarafa, C.4
  • 69
    • 85056024824 scopus 로고    scopus 로고
    • Proteomic Identification and Immunolocalization of Increased Renal Calbindin-D28k Expression in OVE26 Diabetic Mice
    • Thongboonkerd, V., Zheng, S., McLeish, K. R., Epstein, P. N., Klein, J. B., Proteomic Identification and Immunolocalization of Increased Renal Calbindin-D28k Expression in OVE26 Diabetic Mice. Rev. Diabet. Stud. 2005, 2, 19-26.
    • (2005) Rev. Diabet. Stud , vol.2 , pp. 19-26
    • Thongboonkerd, V.1    Zheng, S.2    McLeish, K.R.3    Epstein, P.N.4    Klein, J.B.5
  • 70
    • 0033918672 scopus 로고    scopus 로고
    • The role of calbindin and 1,25 dihydroxyvitamin D3 in the kidney
    • Sooy, K., Kohut, J., Christakos, S., The role of calbindin and 1,25 dihydroxyvitamin D3 in the kidney. Curr. Opin. Nephrol. Hypertens. 2000, 9, 341-347.
    • (2000) Curr. Opin. Nephrol. Hypertens , vol.9 , pp. 341-347
    • Sooy, K.1    Kohut, J.2    Christakos, S.3
  • 71
    • 34249654462 scopus 로고    scopus 로고
    • Application of two-dimensional electrophoresis in the research of retinal proteins of diabetic rat
    • Liu, S. Q., Zhang, Y. Y., Xie, X. Y., Hu, W. M, et al., Application of two-dimensional electrophoresis in the research of retinal proteins of diabetic rat. Cell. Mol. Immunol. 2007, 4, 65-70.
    • (2007) Cell. Mol. Immunol , vol.4 , pp. 65-70
    • Liu, S.Q.1    Zhang, Y.Y.2    Xie, X.Y.3    Hu, W.M.4
  • 72
    • 34249108840 scopus 로고    scopus 로고
    • Differences in expression of retinal proteins between diabetic and normal rats
    • Liu, S. Q., Kang, J., Li, C. J., Tang, E. J. et al., Differences in expression of retinal proteins between diabetic and normal rats. World J. Gastroenterol. 2007, 13, 2118-2124.
    • (2007) World J. Gastroenterol , vol.13 , pp. 2118-2124
    • Liu, S.Q.1    Kang, J.2    Li, C.J.3    Tang, E.J.4
  • 73
    • 34547903199 scopus 로고    scopus 로고
    • Proteome map of normal rat retina and comparison with the proteome of diabetic rat retina: New insight in the pathogenesis of diabetic retinopathy
    • Quin, G. G., Len, A. C., Billson, F. A., Gillies, M. C., Proteome map of normal rat retina and comparison with the proteome of diabetic rat retina: new insight in the pathogenesis of diabetic retinopathy. Proteomics 2007, 7, 2636-2650.
    • (2007) Proteomics , vol.7 , pp. 2636-2650
    • Quin, G.G.1    Len, A.C.2    Billson, F.A.3    Gillies, M.C.4
  • 74
    • 23644456172 scopus 로고    scopus 로고
    • Therapeutic roles of peroxisome proliferator-activated receptor agonists
    • Staels, B., Fruchart, J. C., Therapeutic roles of peroxisome proliferator-activated receptor agonists. Diabetes 2005, 54, 2460-2470.
    • (2005) Diabetes , vol.54 , pp. 2460-2470
    • Staels, B.1    Fruchart, J.C.2
  • 75
    • 0032951971 scopus 로고    scopus 로고
    • A proteome analysis of livers from obese (ob/ob) mice treated with the peroxisome proliferator WY14,643
    • Edvardsson, U., Alexandersson, M. Brockenhuus von Lowenhielm, H., Nystrom, A. C. et al., A proteome analysis of livers from obese (ob/ob) mice treated with the peroxisome proliferator WY14,643. Electrophoresis 1999, 20, 935-942.
    • (1999) Electrophoresis , vol.20 , pp. 935-942
    • Edvardsson, U.1    Alexandersson, M.2    Brockenhuus von Lowenhielm, H.3    Nystrom, A.C.4
  • 76
    • 0032587268 scopus 로고    scopus 로고
    • Rosiglitazone (BRL49653), a PPARgamma-selective agonist, causes peroxisome proliferator-like liver effects in obese mice
    • Edvardsson, U., Bergstrom, M., Alexandersson, M., Bamberg, K. et al., Rosiglitazone (BRL49653), a PPARgamma-selective agonist, causes peroxisome proliferator-like liver effects in obese mice. J. Lipid Res. 1999, 40, 1177-1184.
    • (1999) J. Lipid Res , vol.40 , pp. 1177-1184
    • Edvardsson, U.1    Bergstrom, M.2    Alexandersson, M.3    Bamberg, K.4
  • 77
    • 0037388895 scopus 로고    scopus 로고
    • Hepatic protein expression of lean mice and obese diabetic mice treated with peroxisome proliferator-activated receptor activators
    • Edvardsson, U., von Lowenhielm, H. B., Panfilov, O., Nystrom, A. C. et al., Hepatic protein expression of lean mice and obese diabetic mice treated with peroxisome proliferator-activated receptor activators. Proteomics 2003, 3, 468-478.
    • (2003) Proteomics , vol.3 , pp. 468-478
    • Edvardsson, U.1    von Lowenhielm, H.B.2    Panfilov, O.3    Nystrom, A.C.4
  • 78
    • 0036652155 scopus 로고    scopus 로고
    • Effect of rosiglitazone on the differential expression of diabetes-associated proteins in pancreatic islets of C57BI/6 lep/lep mice
    • Sanchez, J. C., Converset, V., Nolan, A., Schmid, G. et al., Effect of rosiglitazone on the differential expression of diabetes-associated proteins in pancreatic islets of C57BI/6 lep/lep mice. Mol. Cell. Proteomics 2002, 1, 509-516.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 509-516
    • Sanchez, J.C.1    Converset, V.2    Nolan, A.3    Schmid, G.4
  • 79
    • 0041358763 scopus 로고    scopus 로고
    • Effect of rosiglitazone on the differential expression of obesity and insulin resistance associated proteins in lep/lep mice
    • Sanchez, J. C., Converset, V., Nolan, A., Schmid, G. et al., Effect of rosiglitazone on the differential expression of obesity and insulin resistance associated proteins in lep/lep mice. Proteomics 2003, 3, 1500-1520.
    • (2003) Proteomics , vol.3 , pp. 1500-1520
    • Sanchez, J.C.1    Converset, V.2    Nolan, A.3    Schmid, G.4
  • 80
    • 0032514958 scopus 로고    scopus 로고
    • Changes in the liver protein pattern of female Wistar rats treated with the hypoglycemic agent SDZ PGU 693
    • Arce, A., Aicher, L., Wahl, D., Anderson, N. L. et al., Changes in the liver protein pattern of female Wistar rats treated with the hypoglycemic agent SDZ PGU 693. Life Sci. 1998, 63, 2243-2250.
    • (1998) Life Sci , vol.63 , pp. 2243-2250
    • Arce, A.1    Aicher, L.2    Wahl, D.3    Anderson, N.L.4
  • 82
    • 17444386712 scopus 로고    scopus 로고
    • Data analysis methods for detection of differential protein expression in two-dimensional gel electrophoresis
    • Meunier, B., Bouley, J., Piec, I., Bernard, C. et al., Data analysis methods for detection of differential protein expression in two-dimensional gel electrophoresis. Anal. Biochem. 2005, 340, 226-230.
    • (2005) Anal. Biochem , vol.340 , pp. 226-230
    • Meunier, B.1    Bouley, J.2    Piec, I.3    Bernard, C.4
  • 83
    • 34548409217 scopus 로고    scopus 로고
    • Experimental and statistical considerations to avoid false conclusions in proteomic studies using differential in-gel electrophoresis
    • Karp, N. A., McCormick, P. S., Russell, M. R., Lilley, K. S., Experimental and statistical considerations to avoid false conclusions in proteomic studies using differential in-gel electrophoresis. Mol. Cell. Proteomics 2007.
    • (2007) Mol. Cell. Proteomics
    • Karp, N.A.1    McCormick, P.S.2    Russell, M.R.3    Lilley, K.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.