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Volumn 90, Issue 2, 2007, Pages 140-147

Mitochondrial vitamin B12-binding proteins in patients with inborn errors of cobalamin metabolism

Author keywords

Cobalamin; Complementation analysis; Homocysteine; Homocystinuria; Methylmalonic acid; Methylmalonic aciduria; Mitochondria; Vitamin B12; Vitamin B12 binding proteins

Indexed keywords

COBALAMIN; COBALT 57; METHYLMALONYL COENZYME A MUTASE; VITAMIN BINDING PROTEIN; COBAMAMIDE; CYANOCOBALAMIN; DRUG DERIVATIVE; ENZYME; MECOBALAMIN; MITOCHONDRIAL PROTEIN; TRANSCOBALAMIN;

EID: 33846265402     PISSN: 10967192     EISSN: 10967206     Source Type: Journal    
DOI: 10.1016/j.ymgme.2006.08.014     Document Type: Article
Times cited : (13)

References (33)
  • 1
    • 0016836319 scopus 로고
    • Genetic complementation in heterokaryons of human fibroblasts defective in cobalamin metabolism
    • Gravel R.A., Mahoney M.J., Ruddle F.H., and Rosenberg L.E. Genetic complementation in heterokaryons of human fibroblasts defective in cobalamin metabolism. Proc. Natl. Acad. Sci. USA 72 (1975) 3181-3185
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 3181-3185
    • Gravel, R.A.1    Mahoney, M.J.2    Ruddle, F.H.3    Rosenberg, L.E.4
  • 2
    • 0017821131 scopus 로고
    • Genetic complementation among inherited deficiencies of methylmalonyl-CoA mutase activity: evidence for a new class of human cobalamin mutant
    • Willard H.F., Mellman I.S., and Rosenberg L.E. Genetic complementation among inherited deficiencies of methylmalonyl-CoA mutase activity: evidence for a new class of human cobalamin mutant. Am. J. Hum. Genet. 30 (1978) 1-13
    • (1978) Am. J. Hum. Genet. , vol.30 , pp. 1-13
    • Willard, H.F.1    Mellman, I.S.2    Rosenberg, L.E.3
  • 3
    • 0023029805 scopus 로고
    • 12: a new complementation group causing methylmalonic aciduria (cblF)
    • 12: a new complementation group causing methylmalonic aciduria (cblF). Am. J. Hum. Genet. 39 (1986) 404-408
    • (1986) Am. J. Hum. Genet. , vol.39 , pp. 404-408
    • Watkins, D.1    Rosenblatt, D.S.2
  • 4
    • 0023884198 scopus 로고    scopus 로고
    • Genetic heterogeneity among patients with methylcobalamin deficiency. Definition of two complementation groups, cblE and cblG
    • Watkins D., and Rosenblatt D.S. Genetic heterogeneity among patients with methylcobalamin deficiency. Definition of two complementation groups, cblE and cblG. J. Clin. Invest. 81 (1998) 1690-1694
    • (1998) J. Clin. Invest. , vol.81 , pp. 1690-1694
    • Watkins, D.1    Rosenblatt, D.S.2
  • 5
    • 0033938389 scopus 로고    scopus 로고
    • Complementation studies in the cblA class of inborn error of cobalamin metabolism: evidence for interallelic complementation and for a new complementation class (cblH)
    • Watkins D., Matiaszuk N., and Rosenblatt D.S. Complementation studies in the cblA class of inborn error of cobalamin metabolism: evidence for interallelic complementation and for a new complementation class (cblH). J. Med. Genet. 37 (2000) 510-513
    • (2000) J. Med. Genet. , vol.37 , pp. 510-513
    • Watkins, D.1    Matiaszuk, N.2    Rosenblatt, D.S.3
  • 6
    • 0037180440 scopus 로고    scopus 로고
    • 12-responsive methylmalonic acidemia based on analysis of prokaryotic gene arrangements
    • 12-responsive methylmalonic acidemia based on analysis of prokaryotic gene arrangements. Proc. Natl. Acad. Sci. USA 99 (2002) 15554-15559
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15554-15559
    • Dobson, C.M.1    Wai, T.2    Leclerc, D.3
  • 8
    • 5644298359 scopus 로고    scopus 로고
    • The cblD defect causes either isolated or combined deficiency of methylcobalamin and adenosylcobalamin synthesis
    • Suormala T., Baumgartner M.R., Coelho D., et al. The cblD defect causes either isolated or combined deficiency of methylcobalamin and adenosylcobalamin synthesis. J. Biol. Chem. 279 (2004) 42742-42749
    • (2004) J. Biol. Chem. , vol.279 , pp. 42742-42749
    • Suormala, T.1    Baumgartner, M.R.2    Coelho, D.3
  • 9
    • 0020539836 scopus 로고
    • The natural history of the inherited methylmalonic acidemias
    • Matsui S.M., Mahoney M.J., and Rosenberg L.E. The natural history of the inherited methylmalonic acidemias. N. Engl. J. Med. 308 (1983) 857-861
    • (1983) N. Engl. J. Med. , vol.308 , pp. 857-861
    • Matsui, S.M.1    Mahoney, M.J.2    Rosenberg, L.E.3
  • 10
    • 0001912321 scopus 로고    scopus 로고
    • Inherited disorders of folate and cobalamin transport and metabolism
    • Scriver C.R., Sly W.S., Childs B., Beaudet A.L., Valle D., Kinzler K.W., and Vogelstein B. (Eds), McGraw-Hill, New York
    • Rosenblatt D.S., and Fenton W.A. Inherited disorders of folate and cobalamin transport and metabolism. In: Scriver C.R., Sly W.S., Childs B., Beaudet A.L., Valle D., Kinzler K.W., and Vogelstein B. (Eds). The Metabolic and Molecular Bases of Inherited Disease (2001), McGraw-Hill, New York 3897-3933
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 3897-3933
    • Rosenblatt, D.S.1    Fenton, W.A.2
  • 11
    • 0017184537 scopus 로고
    • Rapid prenatal and postnatal detection of inborn errors of propionate. Methylmalonate, and cobalamin metabolism: a sensitive assay using cultured cells
    • Willard H.F., Ambani L.M., Hart A.C., Mahoney M.J., and Rosenberg L.E. Rapid prenatal and postnatal detection of inborn errors of propionate. Methylmalonate, and cobalamin metabolism: a sensitive assay using cultured cells. Hum. Genet. 34 (1976) 227-283
    • (1976) Hum. Genet. , vol.34 , pp. 227-283
    • Willard, H.F.1    Ambani, L.M.2    Hart, A.C.3    Mahoney, M.J.4    Rosenberg, L.E.5
  • 13
    • 10544249877 scopus 로고    scopus 로고
    • Human methionine synthase: cDNA cloning and identification of mutations in patients of the cblG complementation group of folate/cobalamin disorders
    • Leclerc D., Campeau E., Goyette P., et al. Human methionine synthase: cDNA cloning and identification of mutations in patients of the cblG complementation group of folate/cobalamin disorders. Hum. Mol. Genet. 5 (1996) 1867-1874
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1867-1874
    • Leclerc, D.1    Campeau, E.2    Goyette, P.3
  • 14
    • 0029803594 scopus 로고    scopus 로고
    • Defects in human methionine synthase in cblG patients
    • Gulati S., Baker P., Li Y.N., et al. Defects in human methionine synthase in cblG patients. Hum. Mol. Genet. 5 (1996) 1859-1865
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1859-1865
    • Gulati, S.1    Baker, P.2    Li, Y.N.3
  • 16
    • 13144282730 scopus 로고    scopus 로고
    • Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria
    • Leclerc D., Wilson A., Dumas R., et al. Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria. Proc. Natl. Acad. Sci. USA 95 (1998) 3059-3064
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3059-3064
    • Leclerc, D.1    Wilson, A.2    Dumas, R.3
  • 18
    • 0024831226 scopus 로고
    • Functional methionine synthase deficiency (cblE and cblG): clinical and biochemical heterogeneity
    • Watkins D., and Rosenblatt D.S. Functional methionine synthase deficiency (cblE and cblG): clinical and biochemical heterogeneity. Am. J. Med. Genet. 34 (1989) 427-434
    • (1989) Am. J. Med. Genet. , vol.34 , pp. 427-434
    • Watkins, D.1    Rosenblatt, D.S.2
  • 20
    • 0025881389 scopus 로고
    • Lysosomal cobalamin accumulation in fibroblasts from a patient with an inborn error of cobalamin metabolism (cblF complementation group): visualization by electron microscope radioautography
    • Vassiliadis A., Rosenblatt D.S., Cooper B.A., and Bergeron J.J. Lysosomal cobalamin accumulation in fibroblasts from a patient with an inborn error of cobalamin metabolism (cblF complementation group): visualization by electron microscope radioautography. Exp. Cell Res. 195 (1991) 295-302
    • (1991) Exp. Cell Res. , vol.195 , pp. 295-302
    • Vassiliadis, A.1    Rosenblatt, D.S.2    Cooper, B.A.3    Bergeron, J.J.4
  • 21
    • 0006975297 scopus 로고    scopus 로고
    • Recognition of two intracellular cobalamin binding proteins and their identification as methylmalonyl-CoA mutase and methionine synthetase
    • Kolhouse J.F., and Allen R.H. Recognition of two intracellular cobalamin binding proteins and their identification as methylmalonyl-CoA mutase and methionine synthetase. Proc. Natl. Acad. Sci. USA 74 (1997) 921-925
    • (1997) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 921-925
    • Kolhouse, J.F.1    Allen, R.H.2
  • 22
    • 4544315119 scopus 로고    scopus 로고
    • Human SCO1 and SCO2 have independent, cooperative functions in copper delivery to cytochrome C oxidase
    • Leary S.C., Kaufman B.A., Pellecchia G., et al. Human SCO1 and SCO2 have independent, cooperative functions in copper delivery to cytochrome C oxidase. Hum. Mol. Genet. 13 (2004) 1839-1848
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1839-1848
    • Leary, S.C.1    Kaufman, B.A.2    Pellecchia, G.3
  • 23
    • 0031036839 scopus 로고    scopus 로고
    • The IdhA gene encoding the fermentative lactate dehydrogenase of Escerichia coli
    • Bunch P.K., Mat-Jan F., Lee N., and Clark D.P. The IdhA gene encoding the fermentative lactate dehydrogenase of Escerichia coli. Microbiology 143 (1997) 187-195
    • (1997) Microbiology , vol.143 , pp. 187-195
    • Bunch, P.K.1    Mat-Jan, F.2    Lee, N.3    Clark, D.P.4
  • 24
    • 0014059118 scopus 로고
    • An electron-transport system associated with the outer membrane of liver mitochondria. A biochemical and morphological study
    • Sottocasa G.L., Kuylenstierna B., Ernster L., and Bergstrand A. An electron-transport system associated with the outer membrane of liver mitochondria. A biochemical and morphological study. J. Cell. Biol. 32 (1967) 415-438
    • (1967) J. Cell. Biol. , vol.32 , pp. 415-438
    • Sottocasa, G.L.1    Kuylenstierna, B.2    Ernster, L.3    Bergstrand, A.4
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 72 (1976) 248-254
    • (1976) Anal Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 0018242326 scopus 로고
    • Cobalamin binding and cobalamin-dependent enzyme activity in normal and mutant human fibroblasts
    • Mellman I., Willard H.F., and Rosenberg L.E. Cobalamin binding and cobalamin-dependent enzyme activity in normal and mutant human fibroblasts. J. Clin. Invest. 62 (1978) 952-960
    • (1978) J. Clin. Invest. , vol.62 , pp. 952-960
    • Mellman, I.1    Willard, H.F.2    Rosenberg, L.E.3
  • 27
    • 0011756284 scopus 로고
    • Intracellular binding of radioactive hydroxocobalamin to cobalamin-dependent apoenzymes in rat liver
    • Mellman I.S., Youngdahl-Turner P., Willard H.F., and Rosenberg L.E. Intracellular binding of radioactive hydroxocobalamin to cobalamin-dependent apoenzymes in rat liver. Proc. Natl. Acad. Sci. USA 74 (1977) 916-920
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 916-920
    • Mellman, I.S.1    Youngdahl-Turner, P.2    Willard, H.F.3    Rosenberg, L.E.4
  • 28
    • 1842791547 scopus 로고    scopus 로고
    • MeaB is a component of the methylmalonyl-CoA mutase complex required for protection of the enzyme from inactivation
    • Korotkova N., and Lidstrom M.E. MeaB is a component of the methylmalonyl-CoA mutase complex required for protection of the enzyme from inactivation. J. Biol. Chem. 279 (2004) 13558-13652
    • (2004) J. Biol. Chem. , vol.279 , pp. 13558-13652
    • Korotkova, N.1    Lidstrom, M.E.2
  • 29
    • 9144272719 scopus 로고    scopus 로고
    • Human ATP: Cob(I)alamin adenosyltransferase and its interaction with methionine synthase reductase
    • Leal N.A., Olteanu H., Banerjee R., and Bobik T.A. Human ATP: Cob(I)alamin adenosyltransferase and its interaction with methionine synthase reductase. J. Biol. Chem. 279 (2004) 47536-47542
    • (2004) J. Biol. Chem. , vol.279 , pp. 47536-47542
    • Leal, N.A.1    Olteanu, H.2    Banerjee, R.3    Bobik, T.A.4
  • 30
    • 0024165935 scopus 로고
    • 12 -responsive megaloblastic anemia, homocystinuria, and transient methylmalonic aciduria in cblE disease
    • 12 -responsive megaloblastic anemia, homocystinuria, and transient methylmalonic aciduria in cblE disease. J. Pediatr. 113 (1988) 1052-1056
    • (1988) J. Pediatr. , vol.113 , pp. 1052-1056
    • Tuchman, M.1    Kelly, P.2    Watkins, D.3    Rosenblatt, D.S.4


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