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Volumn 9, Issue 1, 2012, Pages

Altered gene and protein expression in liver of the obese spontaneously hypertensive/NDmcr-cp rat

Author keywords

Liver; Metabolic syndrome; Microarray analysis; Obesity; Pathophysiology; Proteomics analysis

Indexed keywords

ION CHANNEL; MESSENGER RNA; TRANSFERASE;

EID: 84866479446     PISSN: None     EISSN: 17437075     Source Type: Journal    
DOI: 10.1186/1743-7075-9-87     Document Type: Article
Times cited : (7)

References (38)
  • 2
    • 74949084667 scopus 로고    scopus 로고
    • Impact of body mass index and the metabolic syndrome on the risk of cardiovascular disease and death in middle-aged men
    • Arnlöv J, Ingelsson E, Sundström J, Lind L: Impact of body mass index and the metabolic syndrome on the risk of cardiovascular disease and death in middle-aged men. Circulation 2010, 121:392-400.
    • (2010) Circulation , vol.121 , pp. 392-400
    • Arnlöv, J.1    Ingelsson, E.2    Sundström, J.3    Lind, L.4
  • 4
    • 77950608681 scopus 로고    scopus 로고
    • Clustering of other metabolic risk factors in subjects with metabolic syndrome
    • Hsieh SD, Muto T, Tsuji H, Arase Y, Murase T: Clustering of other metabolic risk factors in subjects with metabolic syndrome. Metabolism 2010, 59:697-702.
    • (2010) Metabolism , vol.59 , pp. 697-702
    • Hsieh, S.D.1    Muto, T.2    Tsuji, H.3    Arase, Y.4    Murase, T.5
  • 6
    • 0037463608 scopus 로고    scopus 로고
    • The metabolic syndrome: Prevalence and associated risk factor findings in the US population from the third national health and nutrition examination survey
    • Park YW, Zhu S, Palaniappan L, Heshka S, Carnethon MR, Heymsfield SB: The metabolic syndrome: prevalence and associated risk factor findings in the US population from the Third National Health and Nutrition Examination Survey. Arch Intern Med 2003, 163:427-436.
    • (2003) Arch Intern Med , vol.163 , pp. 427-436
    • Park, Y.W.1    Zhu, S.2    Palaniappan, L.3    Heshka, S.4    Carnethon, M.R.5    Heymsfield, S.B.6
  • 7
    • 0031751841 scopus 로고    scopus 로고
    • Long-term effects of perindopril on metabolic parameters and the heart in the spontaneously hypertensive/NIH-corpulent rat with non-insulin-dependent diabetes mellitus and hypertension
    • Striffler JS, Bhathena SJ, Michaelis OE 4th, Campbell JD, Hansen CT, Scalbert E, Thibault N, Velasquez MT: Long-term effects of perindopril on metabolic parameters and the heart in the spontaneously hypertensive/NIH-corpulent rat with non-insulin-dependent diabetes mellitus and hypertension. Metabolism 1998, 47:1199-1204.
    • (1998) Metabolism , vol.47 , pp. 1199-1204
    • Striffler, J.S.1    Bhathena, S.J.2    Michaelis, O.E.3    Campbell, J.D.4    Hansen, C.T.5    Scalbert, E.6    Thibault, N.7    Velasquez, M.T.8
  • 8
    • 0015891045 scopus 로고
    • Obese spontaneously hypertensive rats - A model for study of atherosclerosis
    • Koletsky S: Obese spontaneously hypertensive rats-a model for study of atherosclerosis. Exp Mol Pathol 1973, 19:53-60.
    • (1973) Exp Mol Pathol , vol.19 , pp. 53-60
    • Koletsky, S.1
  • 9
    • 44649145068 scopus 로고    scopus 로고
    • Obese and hypertensive SHR/NDmcr-cp rats - A model of metabolic syndrome
    • Yamamoto J, Ikena K, Yamori Y: Obese and hypertensive SHR/NDmcr-cp rats - A model of metabolic syndrome. Adiposcience 2005, 2:243-248.
    • (2005) Adiposcience , vol.2 , pp. 243-248
    • Yamamoto, J.1    Ikena, K.2    Yamori, Y.3
  • 10
    • 31344455023 scopus 로고    scopus 로고
    • Pravastatin increases survival and suppresses an increase in myocardial matrix metalloproteinase activity in a rat model of heart failure
    • Ichihara S, Noda A, Nagata K, Obata K, Xu J, Ichihara G, Oikawa S, Kawanishi S, Yamada Y, Yokota M: Pravastatin increases survival and suppresses an increase in myocardial matrix metalloproteinase activity in a rat model of heart failure. Cardiovasc Res 2006, 69:726-735.
    • (2006) Cardiovasc Res , vol.69 , pp. 726-735
    • Ichihara, S.1    Noda, A.2    Nagata, K.3    Obata, K.4    Xu, J.5    Ichihara, G.6    Oikawa, S.7    Kawanishi, S.8    Yamada, Y.9    Yokota, M.10
  • 12
    • 34147161968 scopus 로고    scopus 로고
    • Application of highly sensitive fluorescent dyes (CyDye DIGE fluor saturation dyes) to laser microdissection and two-dimensional difference gel electrophoresis (2D-DIGE) for cancer proteomics
    • 2940-2056
    • Kondo T, Hirohashi S: Application of highly sensitive fluorescent dyes (CyDye DIGE Fluor saturation dyes) to laser microdissection and two-dimensional difference gel electrophoresis (2D-DIGE) for cancer proteomics. Nat Protoc 2006, 1:2940-2056.
    • (2006) Nat Protoc , vol.1
    • Kondo, T.1    Hirohashi, S.2
  • 17
    • 58149252168 scopus 로고    scopus 로고
    • Analysis of mechanisms of T-2 toxin toxicity using Yeast DNA microarrays
    • Iwahashi Y, Kitagawa E, Iwahashi H: Analysis of mechanisms of T-2 toxin toxicity using yeast DNA microarrays. Int J Mol Sci 2008, 9:2585-2600.
    • (2008) Int J Mol Sci , vol.9 , pp. 2585-2600
    • Iwahashi, Y.1    Kitagawa, E.2    Iwahashi, H.3
  • 19
    • 0032545405 scopus 로고    scopus 로고
    • Molecular cloning, expression, and characterization of novel human SULT1C sulfotransferases that catalyze the sulfonation of N-hydroxy-2-acetylaminofluorene
    • Sakakibara Y, Yanagisawa K, Katafuchi J, Ringer DP, Takami Y, Nakayama T, Suiko M, Liu M-C: Molecular cloning, expression, and characterization of novel human SULT1C sulfotransferases that catalyze the sulfonation of N-hydroxy-2-acetylaminofluorene. J Biol Chem 1998, 273:33929-33935
    • (1998) J Biol Chem , vol.273 , pp. 33929-33935
    • Sakakibara, Y.1    Yanagisawa, K.2    Katafuchi, J.3    Ringer, D.P.4    Takami, Y.5    Nakayama, T.6    Suiko, M.7    Liu, M.-C.8
  • 21
    • 79960086104 scopus 로고    scopus 로고
    • Estrogen sulfotransferase is expressed in subcutaneous adipose tissue of obese humans in associated with TNF - A and SOCS3
    • Ahima RS, Stanley TL, Khor VK, Zanni MV, Grinspoon SK: Estrogen sulfotransferase is expressed in subcutaneous adipose tissue of obese humans in associated with TNF-a and SOCS3. J Clin Endocrinol Metab 2011, 96:E1153-E1158.
    • (2011) J Clin Endocrinol Metab , vol.96 , pp. E1153-E1158
    • Ahima, R.S.1    Stanley, T.L.2    Khor, V.K.3    Zanni, M.V.4    Grinspoon, S.K.5
  • 26
    • 57249105121 scopus 로고    scopus 로고
    • Investigating the correspondence between transcriptomic and proteomic expression profiles using coupled cluster models
    • Rogers S, Girolami M, Kolch W, Waters KM, Liu T, Thrall B, Wiley HS: Investigating the correspondence between transcriptomic and proteomic expression profiles using coupled cluster models. Bioinformatics 2008, 24:2894-2900.
    • (2008) Bioinformatics , vol.24 , pp. 2894-2900
    • Rogers, S.1    Girolami, M.2    Kolch, W.3    Waters, K.M.4    Liu, T.5    Thrall, B.6    Wiley, H.S.7
  • 27
    • 58149287647 scopus 로고    scopus 로고
    • Transcriptional control of the calreticulin gene in health and disease
    • Qiu Y, Marek M: Transcriptional control of the calreticulin gene in health and disease. Int J Biochem Cell Biol 2009, 41:531-538.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 531-538
    • Qiu, Y.1    Marek, M.2
  • 29
    • 70349850507 scopus 로고    scopus 로고
    • Cell adhesion and spreading affect adipogenesis from embryonic stem cells
    • Szabo E, Feng T, Dziak E, Opas M: Cell adhesion and spreading affect adipogenesis from embryonic stem cells. The role of calreticulin. Stem Cells 2009, 27:2092-2102.
    • (2009) The Role of Calreticulin. Stem Cells , vol.27 , pp. 2092-2102
    • Szabo, E.1    Feng, T.2    Dziak, E.3    Opas, M.4
  • 30
    • 33751426035 scopus 로고    scopus 로고
    • Ultrastructural analysis of development of myocardium in calreticulin-deficient mice
    • Lozyk MD, Papp S, Zhang X, Nakamura K, Michalak M, Opas M: Ultrastructural analysis of development of myocardium in calreticulin-deficient mice. BMC Dev Biol 2006, 6:54
    • (2006) BMC Dev Biol , vol.6 , pp. 54
    • Lozyk, M.D.1    Papp, S.2    Zhang, X.3    Nakamura, K.4    Michalak, M.5    Opas, M.6
  • 31
    • 0032482220 scopus 로고    scopus 로고
    • Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization
    • Bass J, Chiu G, Argon Y, Steiner DF: Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization. J Cell Biol 1998, 141:637-646
    • (1998) J Cell Biol , vol.141 , pp. 637-646
    • Bass, J.1    Chiu, G.2    Argon, Y.3    Steiner, D.F.4
  • 32
    • 27944477788 scopus 로고    scopus 로고
    • Calreticulin destabilizes glucose transporter-1 mRNA in vascular endothelial and smooth muscle cells under high-glucose conditions
    • Jain HT, Many TN, Riahi Y, Kaiser N, Eckel J, Sasson S: Calreticulin destabilizes glucose transporter-1 mRNA in vascular endothelial and smooth muscle cells under high-glucose conditions. Cir Res 2005, 97:1001-1008.
    • (2005) Cir Res , vol.97 , pp. 1001-1008
    • Jain, H.T.1    Many, T.N.2    Riahi, Y.3    Kaiser, N.4    Eckel, J.5    Sasson, S.6
  • 33
    • 84954358020 scopus 로고    scopus 로고
    • Calreticulin regulates insulin receptor expression and its downstream PI3 kinase/Akt signalling pathway
    • Jalali S, Aghasi M, Yeganeh B, Mesaeli N: Calreticulin regulates insulin receptor expression and its downstream PI3 Kinase/Akt signalling pathway. Biochim Biophy Acta 2008, 1783:2344-2351
    • (2008) Biochim Biophy Acta , vol.1783 , pp. 2344-2351
    • Jalali, S.1    Aghasi, M.2    Yeganeh, B.3    Mesaeli, N.4
  • 34
    • 34848927255 scopus 로고    scopus 로고
    • Substrate recognition by the protein disulfide isomerases
    • Hatahet F, Ruddock LW: Substrate recognition by the protein disulfide isomerases. FEBS J 2007, 274:5223-5234
    • (2007) FEBS J , vol.274 , pp. 5223-5234
    • Hatahet, F.1    Ruddock, L.W.2
  • 35
    • 0028321726 scopus 로고
    • Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme
    • Puig A, Gilbert HF: Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme. J Biol Chem 1994, 269:7764-7771
    • (1994) J Biol Chem , vol.269 , pp. 7764-7771
    • Puig, A.1    Gilbert, H.F.2
  • 37
    • 77956684691 scopus 로고    scopus 로고
    • Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins
    • Rutkevich LA, Cohen-Doyle MF, Brockmeier U, Williams DB: Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins. Mol Biol Cell 2010, 21:3093-3105.
    • (2010) Mol Biol Cell , vol.21 , pp. 3093-3105
    • Rutkevich, L.A.1    Cohen-Doyle, M.F.2    Brockmeier, U.3    Williams, D.B.4
  • 38
    • 79959630948 scopus 로고    scopus 로고
    • Infusion of glucose and lipids at physiological rates causes acute endoplasmic reticulum stress in rat liver
    • Boden G, Song W, Duan X, Cheung P, Kresge K, Barrero C, Merali S: Infusion of glucose and lipids at physiological rates causes acute endoplasmic reticulum stress in rat liver. Obesity 2011, 19:1366-1373
    • (2011) Obesity , vol.19 , pp. 1366-1373
    • Boden, G.1    Song, W.2    Duan, X.3    Cheung, P.4    Kresge, K.5    Barrero, C.6    Merali, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.