메뉴 건너뛰기




Volumn 302, Issue 2, 2003, Pages 271-274

Effects of soy protein isolate on LEC rats, a model of Wilson disease: Mechanisms underlying enhancement of liver cell damage

Author keywords

Copper; Ctr1 expression; Glutathione; LEC rats; Metallothionein; Soy protein isolate

Indexed keywords

CARRIER PROTEIN; GLUTATHIONE; GLUTATHIONE DISULFIDE; MESSENGER RNA; METALLOTHIONEIN; METALLOTHIONEIN I; METALLOTHIONEIN II; PROTEIN CTR1; SOYBEAN PROTEIN; UNCLASSIFIED DRUG;

EID: 0037428285     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00159-1     Document Type: Article
Times cited : (4)

References (21)
  • 1
    • 0027516426 scopus 로고
    • Inhibition of the copper incorporation into ceruloplasmin leads to the deficiency in serum ceruloplasmin activity in Lon-Evans cinnamon mutant rat
    • Yamada T., Agui T., Suzuki Y., Sato M., Matsumoto K. Inhibition of the copper incorporation into ceruloplasmin leads to the deficiency in serum ceruloplasmin activity in Lon-Evans cinnamon mutant rat. J. Biol. Chem. 268:1993;8965-8971.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8965-8971
    • Yamada, T.1    Agui, T.2    Suzuki, Y.3    Sato, M.4    Matsumoto, K.5
  • 2
    • 0027977547 scopus 로고
    • Pleiotropic effect of LEC mutation: A rodent model of Wilson's disease
    • Schilsky M.L., Stockert R.J., Sternblieb I. Pleiotropic effect of LEC mutation: a rodent model of Wilson's disease. Am. J. Physiol. 266:1994;G907-G913.
    • (1994) Am. J. Physiol. , vol.266
    • Schilsky, M.L.1    Stockert, R.J.2    Sternblieb, I.3
  • 3
    • 0029810054 scopus 로고    scopus 로고
    • Hepatic iron deprivation prevents spontaneous development of fulminant hepatitis and liver cancer in Long-Evans cinnamon rats
    • Kato J., Kobune M., Kohgo Y., Sugawara N., Hisai H., Nakamura T., Sakamaki S., Sawada N., Niitus Y. Hepatic iron deprivation prevents spontaneous development of fulminant hepatitis and liver cancer in Long-Evans cinnamon rats. J. Clin. Invest. 98:1996;923-929.
    • (1996) J. Clin. Invest. , vol.98 , pp. 923-929
    • Kato, J.1    Kobune, M.2    Kohgo, Y.3    Sugawara, N.4    Hisai, H.5    Nakamura, T.6    Sakamaki, S.7    Sawada, N.8    Niitus, Y.9
  • 5
    • 0024554012 scopus 로고
    • The role of glutathione in copper metabolism and toxicity
    • Freedman J.H., Ciriolo M.R., Peisach J. The role of glutathione in copper metabolism and toxicity. J. Biol. Chem. 264:1989;5598-5605.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5598-5605
    • Freedman, J.H.1    Ciriolo, M.R.2    Peisach, J.3
  • 7
    • 78651195588 scopus 로고
    • Absorption of Cu64, Zn65, Mo99 and Fe59 from ligated segment of the rat gastrointestinal tract
    • Van Campen D.R., Mitchell E.A. Absorption of Cu64, Zn65, Mo99 and Fe59 from ligated segment of the rat gastrointestinal tract. J. Nutr. 86:1965;120-124.
    • (1965) J. Nutr. , vol.86 , pp. 120-124
    • Van Campen, D.R.1    Mitchell, E.A.2
  • 8
    • 0018418908 scopus 로고
    • Inhibitory effect of high dietary zinc on copper absorption in rats. II. Binding of copper and zinc to cytosol proteins in the intestinal mucosa
    • Ogiso T., Ogawa N., Miura T. Inhibitory effect of high dietary zinc on copper absorption in rats. II. Binding of copper and zinc to cytosol proteins in the intestinal mucosa. Chem. Pharm. Bull. 27:1979;515-521.
    • (1979) Chem. Pharm. Bull. , vol.27 , pp. 515-521
    • Ogiso, T.1    Ogawa, N.2    Miura, T.3
  • 9
  • 10
    • 0037477740 scopus 로고    scopus 로고
    • A delicate balance: Homeostatic control of copper uptake and distribution
    • Pena M.M.O., Lee J., Thiele D.J. A delicate balance: homeostatic control of copper uptake and distribution. J. Nutr. 129:1999;1251-1260.
    • (1999) J. Nutr. , vol.129 , pp. 1251-1260
    • Pena, M.M.O.1    Lee, J.2    Thiele, D.J.3
  • 11
    • 0034702881 scopus 로고    scopus 로고
    • Isolation of a murine copper transporter gene, tissue specific expression and functional complementation of a yeast copper transport mutant
    • Lee J., Prohaska J.R., Dagenais S.L., Glover T.W., Thiele D.J. Isolation of a murine copper transporter gene, tissue specific expression and functional complementation of a yeast copper transport mutant. Gene. 254:2000;87-96.
    • (2000) Gene , vol.254 , pp. 87-96
    • Lee, J.1    Prohaska, J.R.2    Dagenais, S.L.3    Glover, T.W.4    Thiele, D.J.5
  • 12
    • 0022272493 scopus 로고
    • Determination of glutathione and glutathione disulfide in biological samples
    • Anderson M.E. Determination of glutathione and glutathione disulfide in biological samples. Methods Enzymol. 113:1985;548-555.
    • (1985) Methods Enzymol. , vol.113 , pp. 548-555
    • Anderson, M.E.1
  • 13
    • 0029017908 scopus 로고
    • Determination of Cu-containing metallothionein: Comparison of Ag saturation assay, thiomolybdate assay, and enzyme-linked immunosorbent assay
    • Bienengrber M., Forderkunz S., Klein D., Summer K.H. Determination of Cu-containing metallothionein: comparison of Ag saturation assay, thiomolybdate assay, and enzyme-linked immunosorbent assay. Anal. Biochem. 228:1995;69-73.
    • (1995) Anal. Biochem. , vol.228 , pp. 69-73
    • Bienengrber, M.1    Forderkunz, S.2    Klein, D.3    Summer, K.H.4
  • 14
    • 0032771207 scopus 로고    scopus 로고
    • Comparative mechanism and toxicity of tetra- and dithiomolybdates in the removal of copper
    • Ogra T., Komada Y., Suzuki K.T. Comparative mechanism and toxicity of tetra- and dithiomolybdates in the removal of copper. J. Inorg. Biochem. 75:1999;199-204.
    • (1999) J. Inorg. Biochem. , vol.75 , pp. 199-204
    • Ogra, T.1    Komada, Y.2    Suzuki, K.T.3
  • 15
    • 0026336011 scopus 로고
    • Determination of metallothionein in tissues by cadmium-hemoglobin affinity assay
    • Eaton D.L., Cherian M.G. Determination of metallothionein in tissues by cadmium-hemoglobin affinity assay. Methods Enzymol. 205:1991;83-88.
    • (1991) Methods Enzymol. , vol.205 , pp. 83-88
    • Eaton, D.L.1    Cherian, M.G.2
  • 16
    • 0017846298 scopus 로고
    • A simplified procedure for determination of metallothionein in animal tissues
    • (in Japanese)
    • Onosaka S., Tanaka K., Doi M., Okahara K. A simplified procedure for determination of metallothionein in animal tissues. Eisei Kagaku. 24:1978;128-131. (in Japanese).
    • (1978) Eisei Kagaku , vol.24 , pp. 128-131
    • Onosaka, S.1    Tanaka, K.2    Doi, M.3    Okahara, K.4
  • 17
    • 0027373911 scopus 로고
    • Selective removal of copper bound to metallothionein in the liver of LEC rats by tetrathiomolybdate
    • Suzuki K.T., Yamamoto K., Kanno S., Aoki Y., Takeichi N. Selective removal of copper bound to metallothionein in the liver of LEC rats by tetrathiomolybdate. Toxicology. 83:1993;149-158.
    • (1993) Toxicology , vol.83 , pp. 149-158
    • Suzuki, K.T.1    Yamamoto, K.2    Kanno, S.3    Aoki, Y.4    Takeichi, N.5
  • 19
    • 0029872621 scopus 로고
    • Evidence for differences in the post-transcriptional regulation of rat metallothionein isoforms
    • Vasconcelos M.H., Tam S.-C., Beattie J.H., Hesketh J.E. Evidence for differences in the post-transcriptional regulation of rat metallothionein isoforms. Biochem. J. 315:1989;665-671.
    • (1989) Biochem. J. , vol.315 , pp. 665-671
    • Vasconcelos, M.H.1    Tam, S.-C.2    Beattie, J.H.3    Hesketh, J.E.4
  • 20
    • 0037025363 scopus 로고    scopus 로고
    • Copper ion-sensing transcription factor Mac1p post-translationally controls the degradation of its target gene product Ctr1
    • Yonkovich J., Mckenndry R., Shi X., Zhu Z. Copper ion-sensing transcription factor Mac1p post-translationally controls the degradation of its target gene product Ctr1. J. Biol. Chem. 277:2002;23981-23984.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23981-23984
    • Yonkovich, J.1    Mckenndry, R.2    Shi, X.3    Zhu, Z.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.