메뉴 건너뛰기




Volumn 25, Issue 11, 2005, Pages 2235-2237

Iron chelation and vascular function: In search of the mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

DEFEROXAMINE; HEME OXYGENASE 1; IRON; IRON CHELATING AGENT; RAZOXANE;

EID: 27644585384     PISSN: 10795642     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.ATV.0000189303.45609.1f     Document Type: Editorial
Times cited : (17)

References (21)
  • 1
    • 0019434645 scopus 로고
    • Iron and the sex difference in heart disease risk
    • Sullivan JL. Iron and the sex difference in heart disease risk. Lancet. 1981;1:1293-1294.
    • (1981) Lancet , vol.1 , pp. 1293-1294
    • Sullivan, J.L.1
  • 2
    • 1242340476 scopus 로고    scopus 로고
    • Iron and peripheral arterial disease: Revisiting the iron hypothesis in a different light
    • Ramakrishna G, Rooke TW, Cooper LT. Iron and peripheral arterial disease: revisiting the iron hypothesis in a different light. Vasc Med. 2003;8:203-210.
    • (2003) Vasc Med , vol.8 , pp. 203-210
    • Ramakrishna, G.1    Rooke, T.W.2    Cooper, L.T.3
  • 3
    • 0033606807 scopus 로고    scopus 로고
    • Iron, atherosclerosis, and ischemic heart disease
    • de Valk B, Marx JJ. Iron, atherosclerosis, and ischemic heart disease. Arch Intern Med. 1999;159:1542-1548.
    • (1999) Arch Intern Med , vol.159 , pp. 1542-1548
    • De Valk, B.1    Marx, J.J.2
  • 4
    • 0037794084 scopus 로고    scopus 로고
    • Mechanism of low-density lipoprotein oxidation by hemoglobin-derived iron
    • Grinshtein N, Bamm VV, Tsemakhovich VA, Shaklai N. Mechanism of low-density lipoprotein oxidation by hemoglobin-derived iron. Biochemistry. 2003;42:6977-6985.
    • (2003) Biochemistry , vol.42 , pp. 6977-6985
    • Grinshtein, N.1    Bamm, V.V.2    Tsemakhovich, V.A.3    Shaklai, N.4
  • 7
    • 0028839288 scopus 로고
    • Role of RNA secondary structure of the iron-responsive element in translational regulation of ferritin synthesis
    • Kikinis Z, Eisenstein RS, Bettany AJ, Munro HN. Role of RNA secondary structure of the iron-responsive element in translational regulation of ferritin synthesis. Nucleic Acids Res. 1995;23:4190-4195.
    • (1995) Nucleic Acids Res , vol.23 , pp. 4190-4195
    • Kikinis, Z.1    Eisenstein, R.S.2    Bettany, A.J.3    Munro, H.N.4
  • 8
    • 0027255106 scopus 로고
    • Oxidative stress resulting from ultraviolet a irradiation of human skin fibroblasts leads to a heme oxygenase-dependent increase in ferritin
    • Vile GF, Tyrrell RM. Oxidative stress resulting from ultraviolet A irradiation of human skin fibroblasts leads to a heme oxygenase-dependent increase in ferritin. J Biol Chem. 1993;268:14678-14681.
    • (1993) J Biol Chem , vol.268 , pp. 14678-14681
    • Vile, G.F.1    Tyrrell, R.M.2
  • 11
    • 0033596677 scopus 로고    scopus 로고
    • Coronary heart disease and iron status: Meta-analyses of prospective studies
    • Danesh J, Appleby P. Coronary heart disease and iron status: meta-analyses of prospective studies. Circulation. 1999;99:852-854.
    • (1999) Circulation , vol.99 , pp. 852-854
    • Danesh, J.1    Appleby, P.2
  • 13
    • 0037132637 scopus 로고    scopus 로고
    • Association between increased iron stores and impaired endothelial function in patients with hereditary hemochromatosis
    • Gaenzer H, Marschang P, Sturm W, Neumayr G, Vogel W, Patsch J, Weiss G. Association between increased iron stores and impaired endothelial function in patients with hereditary hemochromatosis. J Am Coll Cardiol. 2002;40:2189-2194.
    • (2002) J Am Coll Cardiol , vol.40 , pp. 2189-2194
    • Gaenzer, H.1    Marschang, P.2    Sturm, W.3    Neumayr, G.4    Vogel, W.5    Patsch, J.6    Weiss, G.7
  • 15
    • 0036636392 scopus 로고    scopus 로고
    • Effect of dexrazoxane on homocysteine-induced endothelial dysfunction in normal subjects
    • Zheng H, Dimayuga C, Hudaihed A, Katz SD. Effect of dexrazoxane on homocysteine-induced endothelial dysfunction in normal subjects. Arterioscler Thromb Vasc Biol. 2002;22:e15-e18.
    • (2002) Arterioscler Thromb Vasc Biol , vol.22
    • Zheng, H.1    Dimayuga, C.2    Hudaihed, A.3    Katz, S.D.4
  • 16
    • 0032951905 scopus 로고    scopus 로고
    • Nitric oxide and iron proteins
    • Cooper CE. Nitric oxide and iron proteins. Biochim Biophys Acta. 1999;1411:290-309.
    • (1999) Biochim Biophys Acta , vol.1411 , pp. 290-309
    • Cooper, C.E.1
  • 17
    • 27644535717 scopus 로고    scopus 로고
    • Iron chelation supresses the ferritin upregulation and attenuates vascular dysfunction in the aorta of angiotensin II-infused rats
    • Ishizaka N, Saito K, Mori I, Nagai R. Iron chelation supresses the ferritin upregulation and attenuates vascular dysfunction in the aorta of angiotensin II-infused rats. Arterioscler Thromb Vasc Biol. 2005;25:2282-2288.
    • (2005) Arterioscler Thromb Vasc Biol , vol.25 , pp. 2282-2288
    • Ishizaka, N.1    Saito, K.2    Mori, I.3    Nagai, R.4
  • 18
    • 23844456029 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of lipophilic iron chelators as protective agents from oxidative stress
    • Yavin E, Kikkiri R, Gil S, Arad-Yellin R, Shanzer A. Synthesis and biological evaluation of lipophilic iron chelators as protective agents from oxidative stress. Org Biomol Chem. 2005;3:2685-2687.
    • (2005) Org Biomol Chem , vol.3 , pp. 2685-2687
    • Yavin, E.1    Kikkiri, R.2    Gil, S.3    Arad-Yellin, R.4    Shanzer, A.5
  • 19
    • 1242306194 scopus 로고    scopus 로고
    • Reactions of desferrioxamine with peroxynitrite-derived carbonate and nitrogen dioxide radicals
    • Bartesaghi S, Trujillo M, Denicola A, Folkes L, Wardman P, Radi R. Reactions of desferrioxamine with peroxynitrite-derived carbonate and nitrogen dioxide radicals. Free Radic Biol Med. 2004;36:471-483.
    • (2004) Free Radic Biol Med , vol.36 , pp. 471-483
    • Bartesaghi, S.1    Trujillo, M.2    Denicola, A.3    Folkes, L.4    Wardman, P.5    Radi, R.6
  • 20
    • 0022982227 scopus 로고
    • Superoxide-dependent and -independent mechanisms of iron mobilization from ferritin by xanthine oxidase. Implications for oxygen-free-radical-induced tissue destruction during ischaemia and inflammation
    • Biemond P, Swaak AJ, Beindorff CM, Koster JF. Superoxide-dependent and -independent mechanisms of iron mobilization from ferritin by xanthine oxidase. Implications for oxygen-free-radical-induced tissue destruction during ischaemia and inflammation. Biochem J. 1986;239:169-173.
    • (1986) Biochem J , vol.239 , pp. 169-173
    • Biemond, P.1    Swaak, A.J.2    Beindorff, C.M.3    Koster, J.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.