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Volumn 44, Issue 1, 2008, Pages 99-108

Protective role of calreticulin in HFE hemochromatosis

Author keywords

Calreticulin; Hereditary hemochromatosis; HFE; Iron; Oxidative stress

Indexed keywords

CALRETICULIN; HEPCIDIN; HFE PROTEIN; IRON; MESSENGER RNA;

EID: 36249031555     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2007.09.014     Document Type: Article
Times cited : (17)

References (40)
  • 1
    • 33144456592 scopus 로고    scopus 로고
    • Hemochromatosis: genetics and pathophysiology
    • Beutler E. Hemochromatosis: genetics and pathophysiology. Annu. Rev. Med. 57 (2006) 331-347
    • (2006) Annu. Rev. Med. , vol.57 , pp. 331-347
    • Beutler, E.1
  • 3
    • 15244342393 scopus 로고    scopus 로고
    • The hereditary hemochromatosis protein, HFE, lowers intracellular iron levels independently of transferrin receptor 1 in TRVb cells
    • Carlson H., Zhang A.-S., Fleming W.H., and Enns C.A. The hereditary hemochromatosis protein, HFE, lowers intracellular iron levels independently of transferrin receptor 1 in TRVb cells. Blood 105 (2005) 2564-2570
    • (2005) Blood , vol.105 , pp. 2564-2570
    • Carlson, H.1    Zhang, A.-S.2    Fleming, W.H.3    Enns, C.A.4
  • 4
    • 4444226451 scopus 로고    scopus 로고
    • Nontransferrin-bound iron uptake by hepatocytes is increased in the Hfe knockout mouse model of hereditary hemochromatosis
    • Chua A.C., Olynyk J.K., Leedman P.J., and Trinder D. Nontransferrin-bound iron uptake by hepatocytes is increased in the Hfe knockout mouse model of hereditary hemochromatosis. Blood 104 (2004) 1519-1525
    • (2004) Blood , vol.104 , pp. 1519-1525
    • Chua, A.C.1    Olynyk, J.K.2    Leedman, P.J.3    Trinder, D.4
  • 5
    • 33749393565 scopus 로고    scopus 로고
    • Hereditary hemochromatosis protein, HFE, interaction with transferrin receptor 2 suggests a molecular mechanism for mammalian iron sensing
    • Goswami T., and Andrews N.C. Hereditary hemochromatosis protein, HFE, interaction with transferrin receptor 2 suggests a molecular mechanism for mammalian iron sensing. J. Biol. Chem. 281 (2006) 28494-28498
    • (2006) J. Biol. Chem. , vol.281 , pp. 28494-28498
    • Goswami, T.1    Andrews, N.C.2
  • 7
    • 0037132786 scopus 로고    scopus 로고
    • Penetrance of 845G → A (C282Y) HFE hereditary haemochromatosis mutation in the USA
    • Beutler E., Felitti V.J., Koziol J.A., Ho N.J., and Gelbart T. Penetrance of 845G → A (C282Y) HFE hereditary haemochromatosis mutation in the USA. Lancet 359 (2002) 211-218
    • (2002) Lancet , vol.359 , pp. 211-218
    • Beutler, E.1    Felitti, V.J.2    Koziol, J.A.3    Ho, N.J.4    Gelbart, T.5
  • 8
    • 0030732164 scopus 로고    scopus 로고
    • Hereditary hemochromatosis: effects of C282Y and H63D mutations on association with beta2-microglobulin, intracellular processing, and cell surface expression of the HFE protein in COS-7 cells
    • Waheed A., Parkkila S., Zhou X.Y., Tomatsu S., Tsuchihashi Z., Feder J.N., Schatzman R.C., Britton R.S., Bacon B.R., and Sly W.S. Hereditary hemochromatosis: effects of C282Y and H63D mutations on association with beta2-microglobulin, intracellular processing, and cell surface expression of the HFE protein in COS-7 cells. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 12384-12389
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 12384-12389
    • Waheed, A.1    Parkkila, S.2    Zhou, X.Y.3    Tomatsu, S.4    Tsuchihashi, Z.5    Feder, J.N.6    Schatzman, R.C.7    Britton, R.S.8    Bacon, B.R.9    Sly, W.S.10
  • 9
    • 34248522827 scopus 로고    scopus 로고
    • Overexpression of HFE in HepG2 cells reveals differences in intracellular distribution and co-localization of wt- and mutated forms
    • Pinto J.P., Ramos P., and de Sousa M. Overexpression of HFE in HepG2 cells reveals differences in intracellular distribution and co-localization of wt- and mutated forms. Blood cells mol. diseases 39 (2007) 75-81
    • (2007) Blood cells mol. diseases , vol.39 , pp. 75-81
    • Pinto, J.P.1    Ramos, P.2    de Sousa, M.3
  • 11
    • 26444442450 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress: cell life and death decisions
    • Xu C., Bailly-Maitre B., and Reed J.C. Endoplasmic reticulum stress: cell life and death decisions. J. Clin. Invest. 115 (2005) 2656-2664
    • (2005) J. Clin. Invest. , vol.115 , pp. 2656-2664
    • Xu, C.1    Bailly-Maitre, B.2    Reed, J.C.3
  • 12
    • 0034907531 scopus 로고    scopus 로고
    • Iron-induced oxidative stress up-regulates calreticulin levels in intestinal epithelial (Caco-2) cells
    • Nunez M.T., Osorio A., Tapia V., Vergara A., and Mura C.V. Iron-induced oxidative stress up-regulates calreticulin levels in intestinal epithelial (Caco-2) cells. J. Cell. Biochem. 82 (2001) 660-665
    • (2001) J. Cell. Biochem. , vol.82 , pp. 660-665
    • Nunez, M.T.1    Osorio, A.2    Tapia, V.3    Vergara, A.4    Mura, C.V.5
  • 13
    • 1842523082 scopus 로고    scopus 로고
    • Cytoprotection following endoplasmic reticulum stress protein induction in continuous cell lines
    • Bedard K., MacDonald N., Collins J., and Cribb A. Cytoprotection following endoplasmic reticulum stress protein induction in continuous cell lines. Basic Clin. Pharmacol. Toxicol. 94 (2004) 124-131
    • (2004) Basic Clin. Pharmacol. Toxicol. , vol.94 , pp. 124-131
    • Bedard, K.1    MacDonald, N.2    Collins, J.3    Cribb, A.4
  • 15
    • 0033015485 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress-responsive protein GRP78 protects neurons against excitotoxicity and apoptosis: suppression of oxidative stress and stabilization of calcium homeostasis
    • Yu Z., Luo H., Fu W., and Mattson M.P. The endoplasmic reticulum stress-responsive protein GRP78 protects neurons against excitotoxicity and apoptosis: suppression of oxidative stress and stabilization of calcium homeostasis. Exp. Neurol. 155 (1999) 302-314
    • (1999) Exp. Neurol. , vol.155 , pp. 302-314
    • Yu, Z.1    Luo, H.2    Fu, W.3    Mattson, M.P.4
  • 16
    • 0036169941 scopus 로고    scopus 로고
    • Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin
    • Gao B., Adhikari R., Howarth M., Nakamura K., Gold M.C., Hill A.B., Knee R., Michalak M., and Elliott T. Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin. Immunity 16 (2002) 99-109
    • (2002) Immunity , vol.16 , pp. 99-109
    • Gao, B.1    Adhikari, R.2    Howarth, M.3    Nakamura, K.4    Gold, M.C.5    Hill, A.B.6    Knee, R.7    Michalak, M.8    Elliott, T.9
  • 18
    • 0036381371 scopus 로고    scopus 로고
    • Iron and carcinogenesis: from Fenton reaction to target genes
    • Toyokuni S. Iron and carcinogenesis: from Fenton reaction to target genes. Redox Rep. 7 (2002) 189-197
    • (2002) Redox Rep. , vol.7 , pp. 189-197
    • Toyokuni, S.1
  • 19
    • 0035937721 scopus 로고    scopus 로고
    • Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response
    • Kokame K., Kato H., and Miyata T. Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response. J. Biol. Chem. 276 (2001) 9199-9205
    • (2001) J. Biol. Chem. , vol.276 , pp. 9199-9205
    • Kokame, K.1    Kato, H.2    Miyata, T.3
  • 20
    • 10044241545 scopus 로고    scopus 로고
    • Transcriptional regulation of the human HFE gene indicates high liver expression and erythropoiesis coregulation
    • Mura C., le Gac G., Jacolot S., and Ferec C. Transcriptional regulation of the human HFE gene indicates high liver expression and erythropoiesis coregulation. FASEB J. 18 (2004) 1922-1924
    • (2004) FASEB J. , vol.18 , pp. 1922-1924
    • Mura, C.1    le Gac, G.2    Jacolot, S.3    Ferec, C.4
  • 21
    • 0032866573 scopus 로고    scopus 로고
    • Overexpression of the hereditary hemochromatosis protein, HFE, in HeLa cells induces an iron-deficient phenotype
    • Corsi B., Levi S., Cozzi A., Corti A., Altimare D., Albertini A., and Arosio P. Overexpression of the hereditary hemochromatosis protein, HFE, in HeLa cells induces an iron-deficient phenotype. FEBS Lett. 460 (1999) 149-152
    • (1999) FEBS Lett. , vol.460 , pp. 149-152
    • Corsi, B.1    Levi, S.2    Cozzi, A.3    Corti, A.4    Altimare, D.5    Albertini, A.6    Arosio, P.7
  • 22
    • 0032478524 scopus 로고    scopus 로고
    • Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor
    • Lebrón J.A., Bennett M.J., Vaughn D.E., Chirino A.J., Snow P.M., Mintier G.A., Feder J.N., and Bjorkman P.J. Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor. Cell 93 (1998) 111-123
    • (1998) Cell , vol.93 , pp. 111-123
    • Lebrón, J.A.1    Bennett, M.J.2    Vaughn, D.E.3    Chirino, A.J.4    Snow, P.M.5    Mintier, G.A.6    Feder, J.N.7    Bjorkman, P.J.8
  • 23
    • 0032555601 scopus 로고    scopus 로고
    • Co-trafficking of HFE, a nonclassical major histocompatibility complex class I protein, with the transferrin receptor implies a role in intracellular iron regulation
    • Gross C.N., Irrinki A., Feder J.N., and Enns C.A. Co-trafficking of HFE, a nonclassical major histocompatibility complex class I protein, with the transferrin receptor implies a role in intracellular iron regulation. J. Biol. Chem. 273 (1998) 22068-22074
    • (1998) J. Biol. Chem. , vol.273 , pp. 22068-22074
    • Gross, C.N.1    Irrinki, A.2    Feder, J.N.3    Enns, C.A.4
  • 24
    • 33745808734 scopus 로고    scopus 로고
    • Possible roles of the hereditary hemochromatosis protein, HFE, in regulating cellular iron homeostasis
    • Enns C.A. Possible roles of the hereditary hemochromatosis protein, HFE, in regulating cellular iron homeostasis. Biol. Res. 39 (2006) 105-111
    • (2006) Biol. Res. , vol.39 , pp. 105-111
    • Enns, C.A.1
  • 29
    • 23944438373 scopus 로고    scopus 로고
    • Cellular functions of endoplasmic reticulum chaperones calreticulin, calnexin, and ERp57
    • Bedard K., Szabo E., Michalak M., and Opas M. Cellular functions of endoplasmic reticulum chaperones calreticulin, calnexin, and ERp57. Int. Rev. Cyt. 245 (2005) 91-121
    • (2005) Int. Rev. Cyt. , vol.245 , pp. 91-121
    • Bedard, K.1    Szabo, E.2    Michalak, M.3    Opas, M.4
  • 31
    • 16244405250 scopus 로고    scopus 로고
    • Hepatitis C virus, ER stress, and oxidative stress
    • Tardif K.D., Waris G., and Siddiqui A. Hepatitis C virus, ER stress, and oxidative stress. Trends Microbiol. 13 (2005) 159-163
    • (2005) Trends Microbiol. , vol.13 , pp. 159-163
    • Tardif, K.D.1    Waris, G.2    Siddiqui, A.3
  • 33
    • 0034083227 scopus 로고    scopus 로고
    • Role of oxidative stress in cardiovascular diseases
    • Dhalla N.S., Temsah R.M., and Netticadan T. Role of oxidative stress in cardiovascular diseases. J. Hypertens 18 (2000) 655-673
    • (2000) J. Hypertens , vol.18 , pp. 655-673
    • Dhalla, N.S.1    Temsah, R.M.2    Netticadan, T.3
  • 34
    • 0037378026 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease
    • Jenner P. Oxidative stress in Parkinson's disease. Ann. Neurol. 53 (2003) S26-S36
    • (2003) Ann. Neurol. , vol.53
    • Jenner, P.1
  • 35
    • 0035003439 scopus 로고    scopus 로고
    • Chemistry and biochemistry of oxidative stress in neurodegenerative disease
    • Sayre L.M., Smith M.A., and Perry G. Chemistry and biochemistry of oxidative stress in neurodegenerative disease. Curr. Med. Chem. 8 (2001) 721-738
    • (2001) Curr. Med. Chem. , vol.8 , pp. 721-738
    • Sayre, L.M.1    Smith, M.A.2    Perry, G.3
  • 38
    • 0031002910 scopus 로고    scopus 로고
    • Immunohistochemistry of HLA-H, the protein defective in patients with hereditary hemochromatosis, reveals unique pattern of expression in gastrointestinal tract
    • Parkkila S., Waheed A., Britton R.S., Feder J.N., Tsuchihashi Z., Schatzman R.C., Bacon B.R., and Sly W.S. Immunohistochemistry of HLA-H, the protein defective in patients with hereditary hemochromatosis, reveals unique pattern of expression in gastrointestinal tract. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 2534-2539
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 2534-2539
    • Parkkila, S.1    Waheed, A.2    Britton, R.S.3    Feder, J.N.4    Tsuchihashi, Z.5    Schatzman, R.C.6    Bacon, B.R.7    Sly, W.S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.