메뉴 건너뛰기




Volumn 57, Issue 3, 2011, Pages 497-504

Dietary iron restriction prevents hypertensive cardiovascular remodeling in dahl salt-sensitive rats

Author keywords

anemia; dahl salt sensitive rats; heart failure; hypertension; iron restriction; nitric oxide synthesis; oxidative stress

Indexed keywords

8 HYDROXYDEOXYGUANOSINE; CREATININE; ENDOTHELIAL NITRIC OXIDE SYNTHASE; FERRITIN; FERRITIN H; FERRITIN L; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; IRON; N(G) NITROARGININE METHYL ESTER; PROTEIN KINASE B; SODIUM CHLORIDE; TRANSFERRIN RECEPTOR; UNCLASSIFIED DRUG;

EID: 79953254028     PISSN: 0194911X     EISSN: 15244563     Source Type: Journal    
DOI: 10.1161/HYPERTENSIONAHA.110.159681     Document Type: Article
Times cited : (45)

References (25)
  • 1
    • 0033537671 scopus 로고    scopus 로고
    • Iron-deficient diet reduces atherosclerotic lesions in apoE-deficient mice
    • Lee TS, Shiao MS, Pan CC, Chau LY. Iron-deficient diet reduces atherosclerotic lesions in apoE-deficient mice. Circulation. 1999;99: 1222-1229.
    • (1999) Circulation , vol.99 , pp. 1222-1229
    • Lee, T.S.1    Shiao, M.S.2    Pan, C.C.3    Chau, L.Y.4
  • 3
    • 13944269223 scopus 로고    scopus 로고
    • The plasticity of aging: Insights from long-lived mutants
    • DOI 10.1016/j.cell.2005.02.002
    • Kenyon C. The plasticity of aging: Insights from long-lived mutants. Cell. 2005;120:449-460. (Pubitemid 40269760)
    • (2005) Cell , vol.120 , Issue.4 , pp. 449-460
    • Kenyon, C.1
  • 4
    • 0021363341 scopus 로고
    • Effect of weight loss in moderate obesity on plasma lipoprotein and apolipoprotein levels and on high density lipoprotein composition
    • Zimmerman J, Kaufmann NA, Fainaru M, Eisenberg S, Oschry Y, Friedlander Y, Stein Y. Effect of weight loss in moderate obesity on plasma lipoprotein and apolipoprotein levels and on high density lipoprotein composition. Arteriosclerosis. 1984;4:115-123. (Pubitemid 14152889)
    • (1984) Arteriosclerosis , vol.4 , Issue.2 , pp. 115-123
    • Zimmerman, J.1    Kaufmann, N.A.2    Fainaru, M.3
  • 5
    • 33748615141 scopus 로고    scopus 로고
    • Moderate calorie restriction improves cardiac remodeling and diastolic dysfunction in the Dahl-SS rat
    • DOI 10.1016/j.yjmcc.2006.07.012, PII S0022282806007279
    • Seymour EM, Parikh RV, Singer AA, Bolling SF. Moderate calorie restriction improves cardiac remodeling and diastolic dysfunction in the Dahl-SS rat. J Mol Cell Cardiol. 2006;41:661-668. (Pubitemid 44376792)
    • (2006) Journal of Molecular and Cellular Cardiology , vol.41 , Issue.4 , pp. 661-668
    • Seymour, E.M.1    Parikh, R.V.2    Singer, A.A.M.3    Bolling, S.F.4
  • 6
    • 37349051709 scopus 로고    scopus 로고
    • Cardioprotective effects of short-term caloric restriction are mediated by adiponectin via activation of AMP-activated protein kinase
    • DOI 10.1161/CIRCULATIONAHA.107.725697
    • Shinmura K, Tamaki K, Saito K, Nakano Y, Tobe T, Bolli R. Cardioprotective effects of short-term caloric restriction are mediated by adiponectin via activation of AMP-activated protein kinase. Circulation. 2007;116:2809-2817. (Pubitemid 350291223)
    • (2007) Circulation , vol.116 , Issue.24 , pp. 2809-2817
    • Shinmura, K.1    Tamaki, K.2    Saito, K.3    Nakano, Y.4    Tobe, T.5    Bolli, R.6
  • 8
    • 0036900095 scopus 로고    scopus 로고
    • Augmented diurnal variations of the cardiac renin-angiotensin system in hypertensive rats
    • DOI 10.1161/01.HYP.0000039960.66987.89
    • Naito Y, Tsujino T, Fujioka Y, Ohyanagi M, Iwasaki T. Augmented diurnal variations of the cardiac renin-angiotensin system in hypertensive rats. Hypertension. 2002;40:827-833. (Pubitemid 35434902)
    • (2002) Hypertension , vol.40 , Issue.6 , pp. 827-833
    • Naito, Y.1    Tsujino, T.2    Fujioka, Y.3    Ohyanagi, M.4    Iwasaki, T.5
  • 9
    • 33750008791 scopus 로고    scopus 로고
    • The transferrin receptor part I: Biology and targeting with cytotoxic antibodies for the treatment of cancer
    • DOI 10.1016/j.clim.2006.06.010, PII S1521661606007807
    • Daniels TR, Delgado T, Rodriguez JA, Helguera G, Penichet ML. The transferrin receptor part I: Biology and targeting with cytotoxic antibodies for the treatment of cancer. Clinical Immunology. 2006;121:144-158. (Pubitemid 44592578)
    • (2006) Clinical Immunology , vol.121 , Issue.2 , pp. 144-158
    • Daniels, T.R.1    Delgado, T.2    Rodriguez, J.A.3    Helguera, G.4    Penichet, M.L.5
  • 11
    • 0030778795 scopus 로고    scopus 로고
    • Body iron stores and the risk of carotid atherosclerosis: Prospective results from the bruneck study
    • Kiechl S, Willeit J, Egger G, Poewe W, Oberhollenzer F. Body iron stores and the risk of carotid atherosclerosis: prospective results from the Bruneck study. Circulation. 1997;96:3300-3307. (Pubitemid 27513398)
    • (1997) Circulation , vol.96 , Issue.10 , pp. 3300-3307
    • Kiechl, S.1    Willeit, J.2    Egger, G.3    Poewe, W.4    Oberhollenzer, F.5
  • 12
    • 33646132038 scopus 로고    scopus 로고
    • Development of heart failure in chronic hypertensive Dahl rats: Focus on heart failure with preserved ejection fraction
    • DOI 10.1161/01.HYP.0000215579.81408.8e, PII 0000426820060500000020
    • Klotz S, Hay I, Zhang G, Maurer M, Wang J, Burkhoff D. Development of heart failure in chronic hypertensive Dahl rats: focus on heart failure with preserved ejection fraction. Hypertension. 2006;47:901-911. (Pubitemid 44297562)
    • (2006) Hypertension , vol.47 , Issue.5 , pp. 901-911
    • Klotz, S.1    Hay, I.2    Zhang, G.3    Maurer, M.4    Wang, J.5    Burkhoff, D.6
  • 13
    • 0025951842 scopus 로고
    • Dual hemodynamic mechanisms for salt-induced hypertension in Dahl salt-sensitive rats
    • Simchon S, Manger WM, Brown TW. Dual hemodynamic mechanisms for salt-induced hypertension in Dahl salt-sensitive rats. Hypertension. 1991;17:1063-1071.
    • (1991) Hypertension , vol.17 , pp. 1063-1071
    • Simchon, S.1    Manger, W.M.2    Brown, T.W.3
  • 14
    • 25144483332 scopus 로고    scopus 로고
    • Dietary iron deficiency induces ventricular dilation, mitochondrial ultrastructural aberrations and cytochrome c release: Involvement of nitric oxide synthase and protein tyrosine nitration
    • DOI 10.1042/CS20040278
    • Dong F, Zhang X, Culver B, Chew HG Jr., Kelley RO, Ren J. Dietary iron deficiency induces ventricular dilation, mitochondrial ultrastructural aberrations and cytochrome c release: involvement of nitric oxide synthase and protein tyrosine nitration. Clin Sci (Lond). 2005;109:277-286. (Pubitemid 41337132)
    • (2005) Clinical Science , vol.109 , Issue.3 , pp. 277-286
    • Dong, F.1    Zhang, X.2    Culver, B.3    Chew Jr., H.G.4    Kelley, R.O.5    Ren, J.6
  • 16
    • 0033542476 scopus 로고    scopus 로고
    • Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation
    • Dimmeler S, Fleming I, Fisslthaler B, Hermann C, Busse R, Zeiher AM. Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation. Nature. 1999;399:601-605.
    • (1999) Nature , vol.399 , pp. 601-605
    • Dimmeler, S.1    Fleming, I.2    Fisslthaler, B.3    Hermann, C.4    Busse, R.5    Zeiher, A.M.6
  • 18
  • 19
    • 0034634281 scopus 로고    scopus 로고
    • Endothelial dysfunction in cardiovascular diseases: The role of oxidant stress
    • Cai H, Harrison DG. Endothelial dysfunction in cardiovascular diseases: the role of oxidant stress. Circ Res. 2000;87:840-844.
    • (2000) Circ Res , vol.87 , pp. 840-844
    • Cai, H.1    Harrison, D.G.2
  • 20
    • 54449096299 scopus 로고    scopus 로고
    • Bidirectional actions of hydrogen peroxide on endothelial nitric-oxide synthase phosphorylation and function: Co-commitment and interplay of Akt and AMPK
    • Hu Z, Chen J, Wei Q, Xia Y. Bidirectional actions of hydrogen peroxide on endothelial nitric-oxide synthase phosphorylation and function: co-commitment and interplay of Akt and AMPK. J Biol Chem. 2008; 283:25256-25263.
    • (2008) J Biol Chem , vol.283 , pp. 25256-25263
    • Hu, Z.1    Chen, J.2    Wei, Q.3    Xia, Y.4
  • 21
    • 34447518891 scopus 로고    scopus 로고
    • ERK activation contributes to regulation of spontaneous contractile tone via superoxide anion in isolated rat aorta of angiotensin II-induced hypertension
    • DOI 10.1152/ajpheart.00388.2006
    • Ding L, Chapman A, Boyd R, Wang HD. ERK activation contributes to regulation of spontaneous contractile tone via superoxide anion in isolated rat aorta of angiotensin II-induced hypertension. Am J Physiol Heart Circ Physiol. 2007;292:H2997-H3005. (Pubitemid 47084552)
    • (2007) American Journal of Physiology - Heart and Circulatory Physiology , vol.292 , Issue.6
    • Ding, L.1    Chapman, A.2    Boyd, R.3    Wang, H.D.4
  • 22
    • 0037428060 scopus 로고    scopus 로고
    • Oxidative stress-induced iron signaling is responsible for peroxide-dependent oxidation of dichlorodihydrofluorescein in endothelial cells role of transferrin receptor-dependent iron uptake in apoptosis
    • DOI 10.1161/01.RES.0000048195.15637.AC
    • Tampo Y, Kotamraju S, Chitambar CR, Kalivendi SV, Keszler A, Joseph J, Kalyanaraman B. Oxidative stress-induced iron signaling is responsible for peroxide-dependent oxidation of dichlorodihydrofluorescein in endothelial cells: role of transferrin receptor-dependent iron uptake in apoptosis. Circ Res. 2003;92:56-63. (Pubitemid 36105607)
    • (2003) Circulation Research , vol.92 , Issue.1 , pp. 56-63
    • Tampo, Y.1    Kotamraju, S.2    Chitambar, C.R.3    Kalivendi, S.V.4    Keszler, A.5    Kalyanaraman, J.J.B.6
  • 23
    • 0024245282 scopus 로고
    • Mechanism of ferritin iron uptake: Activity of the H-chain and deletion mapping of the ferro-oxidase site. A study of iron uptake and ferro-oxidase activity of human liver, recombinant H-chain ferritins, and of two H-chain deletion mutants
    • Levi S, Luzzago A, Cesareni G Cozze A, Franceschinelli F, Albertini A, Arosio P. Mechanism of ferritin iron uptake: activity of the H-chain and deletion mapping of the ferro-oxidase site: a study of iron uptake and ferro-oxidase activity of human liver, recombinant H-chain ferritins, and of two H-chain deletion mutants. J Biol Chem. 1988;263:18086-18092. (Pubitemid 19005083)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.34 , pp. 18086-18092
    • Levi, S.1    Luzzago, A.2    Cesareni, G.3    Cozzi, A.4    Franceschinelli, F.5    Albertini, A.6    Arosio, P.7
  • 24
    • 0037093202 scopus 로고    scopus 로고
    • Regulation of ferritin genes and protein
    • DOI 10.1182/blood.V99.10.3505
    • Torti FM, Torti SV. Regulation of ferritin genes and protein. Blood. 2002;99:3505-3516. (Pubitemid 34534516)
    • (2002) Blood , vol.99 , Issue.10 , pp. 3505-3516
    • Torti, F.M.1    Torti, S.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.