메뉴 건너뛰기




Volumn 91, Issue 2, 2007, Pages 148-156

Pleiotropic effects and compensation mechanisms determine tissue specificity in mitochondrial myopathy and sideroblastic anemia (MLASA)

Author keywords

Expression; Microarray; Myopathy; Oxidative phosphorylation disorder; Pseudouridylation; Sideroblastic anemia

Indexed keywords

ARTICLE; CLINICAL ARTICLE; CONTROLLED STUDY; DNA TRANSCRIPTION; FEMALE; GENE EXPRESSION; GENE MUTATION; HUMAN; HUMAN CELL; IRON METABOLISM; MALE; METAL BINDING; MICROARRAY ANALYSIS; MITOCHONDRIAL MYOPATHY; MITOCHONDRIAL MYOPATHY AND SIDEROBLASTIC ANEMIA; NUCLEOTIDE SEQUENCE; PATHOGENESIS; PHENOTYPE; PLEIOTROPY; PRIORITY JOURNAL; REAL TIME POLYMERASE CHAIN REACTION; SIDEROBLASTIC ANEMIA; TISSUE SPECIFICITY; TRANSCRIPTION REGULATION;

EID: 34249008188     PISSN: 10967192     EISSN: 10967206     Source Type: Journal    
DOI: 10.1016/j.ymgme.2007.02.006     Document Type: Article
Times cited : (15)

References (43)
  • 1
    • 1442308549 scopus 로고    scopus 로고
    • Mitochondrial myopathy and sideroblastic anemia
    • Casas K.A., and Fischel-Ghodsian N. Mitochondrial myopathy and sideroblastic anemia. Am. J. Med. Genet. A125 (2004) 201-204
    • (2004) Am. J. Med. Genet. , vol.A125 , pp. 201-204
    • Casas, K.A.1    Fischel-Ghodsian, N.2
  • 2
    • 2442691791 scopus 로고    scopus 로고
    • Missense mutation in pseudouridine synthase 1 (PUS1) causes mitochondrial myopathy and sideroblastic anemia (MLASA)
    • Bykhovskaya Y., Casas K.A., Mengesha E., Inbal A., and Fischel-Ghodsian N. Missense mutation in pseudouridine synthase 1 (PUS1) causes mitochondrial myopathy and sideroblastic anemia (MLASA). Am. J. Hum. Genet. 74 (2004) 1303-1308
    • (2004) Am. J. Hum. Genet. , vol.74 , pp. 1303-1308
    • Bykhovskaya, Y.1    Casas, K.A.2    Mengesha, E.3    Inbal, A.4    Fischel-Ghodsian, N.5
  • 3
    • 21244449941 scopus 로고    scopus 로고
    • Mitochondrial myopathy and sideroblastic anemia (MLASA): missense mutation in the pseudouridine synthase 1 (PUS1) gene is associated with the loss of tRNA pseudouridylation
    • Patton J.R., Bykhovskaya Y., Mengesha E., Bertolotto C., and Fischel-Ghodsian N. Mitochondrial myopathy and sideroblastic anemia (MLASA): missense mutation in the pseudouridine synthase 1 (PUS1) gene is associated with the loss of tRNA pseudouridylation. J. Biol. Chem. 280 (2005) 19823-19828
    • (2005) J. Biol. Chem. , vol.280 , pp. 19823-19828
    • Patton, J.R.1    Bykhovskaya, Y.2    Mengesha, E.3    Bertolotto, C.4    Fischel-Ghodsian, N.5
  • 4
    • 0037972522 scopus 로고    scopus 로고
    • Mitochondrial respiratory-chain diseases
    • DiMauro S., and Schon E.A. Mitochondrial respiratory-chain diseases. N. Engl. J. Med. 348 (2003) 2656-2668
    • (2003) N. Engl. J. Med. , vol.348 , pp. 2656-2668
    • DiMauro, S.1    Schon, E.A.2
  • 5
    • 10644231741 scopus 로고    scopus 로고
    • The many faces of mitochondrial diseases
    • DiMauro S. The many faces of mitochondrial diseases. Mitochondrion 4 (2004) 799-807
    • (2004) Mitochondrion , vol.4 , pp. 799-807
    • DiMauro, S.1
  • 6
    • 33744752749 scopus 로고    scopus 로고
    • The molecular basis for tissue specificity of the oxidative phosphorylation deficiencies in patients with mutations in the mitochondrial translation factor EFG1
    • Antonicka H., Sasarman F., Kennaway N.G., and Shoubridge E.A. The molecular basis for tissue specificity of the oxidative phosphorylation deficiencies in patients with mutations in the mitochondrial translation factor EFG1. Hum. Mol. Genet. 15 (2006) 1835-1846
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1835-1846
    • Antonicka, H.1    Sasarman, F.2    Kennaway, N.G.3    Shoubridge, E.A.4
  • 7
    • 33746504845 scopus 로고    scopus 로고
    • A previously unidentified activity of yeast and mouse RNA:pseudouridine synthases 1 (Pus1p) on tRNAs
    • Behm-Ansmant I., Massenet S., Immel F., Patton J.R., Motorin Y., and Branlant C. A previously unidentified activity of yeast and mouse RNA:pseudouridine synthases 1 (Pus1p) on tRNAs. RNA 12 (2006) 1583-1593
    • (2006) RNA , vol.12 , pp. 1583-1593
    • Behm-Ansmant, I.1    Massenet, S.2    Immel, F.3    Patton, J.R.4    Motorin, Y.5    Branlant, C.6
  • 8
    • 4344573761 scopus 로고    scopus 로고
    • Regulation of nuclear receptor activity by a pseudouridine synthase through posttranscriptional modification of steroid receptor RNA activator
    • Zhao X., Patton J.R., Davis S.L., Florence B., Ames S.J., and Spanjaard R.A. Regulation of nuclear receptor activity by a pseudouridine synthase through posttranscriptional modification of steroid receptor RNA activator. Mol. Cell 15 (2004) 549-558
    • (2004) Mol. Cell , vol.15 , pp. 549-558
    • Zhao, X.1    Patton, J.R.2    Davis, S.L.3    Florence, B.4    Ames, S.J.5    Spanjaard, R.A.6
  • 9
    • 3242656131 scopus 로고    scopus 로고
    • Mouse dyskerin mutations affect accumulation of telomerase RNA and small nucleolar RNA, telomerase activity, and ribosomal RNA processing
    • Mochizuki Y., He J., Kulkarni S., Bessler M., and Masonl P.J. Mouse dyskerin mutations affect accumulation of telomerase RNA and small nucleolar RNA, telomerase activity, and ribosomal RNA processing. Proc. Natl. Acad. Sci. USA 101 (2004) 10756-10761
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10756-10761
    • Mochizuki, Y.1    He, J.2    Kulkarni, S.3    Bessler, M.4    Masonl, P.J.5
  • 10
    • 0033518188 scopus 로고    scopus 로고
    • A telomerase component is defective in the human disease dyskeratosis congenita
    • Mitchell J.R., Wood E., and Collins K. A telomerase component is defective in the human disease dyskeratosis congenita. Nature 402 (1999) 551-555
    • (1999) Nature , vol.402 , pp. 551-555
    • Mitchell, J.R.1    Wood, E.2    Collins, K.3
  • 11
    • 0033754823 scopus 로고    scopus 로고
    • Dyskeratosis congenita in all its forms
    • Dokal I. Dyskeratosis congenita in all its forms. Br. J. Haematol. 110 (2000) 768-779
    • (2000) Br. J. Haematol. , vol.110 , pp. 768-779
    • Dokal, I.1
  • 13
    • 33845906332 scopus 로고    scopus 로고
    • Utilization of lymphoblastoid cell lines as a system for the molecular modeling of autism
    • Baron C.A., Liu S.Y., Hicks C., and Gregg J.P. Utilization of lymphoblastoid cell lines as a system for the molecular modeling of autism. J. Autism. Dev. Disord. 36 (2006) 973-982
    • (2006) J. Autism. Dev. Disord. , vol.36 , pp. 973-982
    • Baron, C.A.1    Liu, S.Y.2    Hicks, C.3    Gregg, J.P.4
  • 14
    • 33745905328 scopus 로고    scopus 로고
    • Identification of genes modulated in rheumatoid arthritis using complementary DNA microarray analysis of lymphoblastoid B cell lines from disease-discordant monozygotic twins
    • Haas C.S., Creighton C.J., Pi X., Maine I., Koch A.E., Haines G.K., Ling S., Chinnaiyan A.M., and Holoshitz J. Identification of genes modulated in rheumatoid arthritis using complementary DNA microarray analysis of lymphoblastoid B cell lines from disease-discordant monozygotic twins. Arthritis Rheum 54 (2006) 2047-2060
    • (2006) Arthritis Rheum , vol.54 , pp. 2047-2060
    • Haas, C.S.1    Creighton, C.J.2    Pi, X.3    Maine, I.4    Koch, A.E.5    Haines, G.K.6    Ling, S.7    Chinnaiyan, A.M.8    Holoshitz, J.9
  • 16
    • 0026352757 scopus 로고
    • Epstein-Barr virus transformation of cryopreserved lymphocytes: prolonged experience with technique
    • Pressman S., and Rotter J.I. Epstein-Barr virus transformation of cryopreserved lymphocytes: prolonged experience with technique. Am. J. Hum. Genet. 49 (1991) 467
    • (1991) Am. J. Hum. Genet. , vol.49 , pp. 467
    • Pressman, S.1    Rotter, J.I.2
  • 22
    • 33646543044 scopus 로고    scopus 로고
    • Impaired control of IRES-mediated translation in X-linked dyskeratosis congenita
    • Yoon A., Peng G., Brandenburger Y., Zollo O., Xu W., Rego E., and Ruggero D. Impaired control of IRES-mediated translation in X-linked dyskeratosis congenita. Science 312 (2006) 902-906
    • (2006) Science , vol.312 , pp. 902-906
    • Yoon, A.1    Peng, G.2    Brandenburger, Y.3    Zollo, O.4    Xu, W.5    Rego, E.6    Ruggero, D.7
  • 23
    • 0028618244 scopus 로고
    • Pseudouridine formation in small nuclear RNAs
    • Patton J.R. Pseudouridine formation in small nuclear RNAs. Biochimie 76 (1994) 1129-1132
    • (1994) Biochimie , vol.76 , pp. 1129-1132
    • Patton, J.R.1
  • 24
    • 0029945504 scopus 로고    scopus 로고
    • Pseudouridine synthases: four families of enzymes containing a putative uridine-binding motif also conserved in dUTPases and dCTP deaminases
    • Koonin E.V. Pseudouridine synthases: four families of enzymes containing a putative uridine-binding motif also conserved in dUTPases and dCTP deaminases. Nucleic Acids Res. 24 (1996) 2411-2415
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2411-2415
    • Koonin, E.V.1
  • 25
    • 0002425959 scopus 로고    scopus 로고
    • Posttranscriptional modifications in the U small nuclear RNAs
    • Grosjean H., and Benne R. (Eds), ASM Press, Washington, DC
    • Massenet S., Mougin A., and Branlant C. Posttranscriptional modifications in the U small nuclear RNAs. In: Grosjean H., and Benne R. (Eds). The Modification and Editing of RNA (1998), ASM Press, Washington, DC 201-228
    • (1998) The Modification and Editing of RNA , pp. 201-228
    • Massenet, S.1    Mougin, A.2    Branlant, C.3
  • 26
    • 0033935223 scopus 로고    scopus 로고
    • Pseudouridine in RNA: what, where, how, and why
    • Charette M., and Gray M.W. Pseudouridine in RNA: what, where, how, and why. IUBMB Life 49 (2000) 341-351
    • (2000) IUBMB Life , vol.49 , pp. 341-351
    • Charette, M.1    Gray, M.W.2
  • 27
    • 0037029086 scopus 로고    scopus 로고
    • Ribosomal RNA pseudouridines and pseudouridine synthases
    • Ofengand J. Ribosomal RNA pseudouridines and pseudouridine synthases. FEBS Lett. 514 (2002) 17-25
    • (2002) FEBS Lett. , vol.514 , pp. 17-25
    • Ofengand, J.1
  • 28
    • 0031870753 scopus 로고    scopus 로고
    • The yeast tRNA:pseudouridine synthase Pus1p displays a multisite substrate specificity
    • Motorin Y., Keith G., Simon C., Foiret D., Simos G., Hurt E., and Grosjean H. The yeast tRNA:pseudouridine synthase Pus1p displays a multisite substrate specificity. RNA 4 (1998) 856-869
    • (1998) RNA , vol.4 , pp. 856-869
    • Motorin, Y.1    Keith, G.2    Simon, C.3    Foiret, D.4    Simos, G.5    Hurt, E.6    Grosjean, H.7
  • 29
    • 0033046012 scopus 로고    scopus 로고
    • Pseudouridine mapping in the Saccharomyces cerevisiae spliceosomal U small nuclear RNAs (snRNAs) reveals that pseudouridine synthase Pus1p exhibits a dual substrate specificity for U2 snRNA and tRNA
    • Massenet S., Motorin Y., Lafontaine D.L., Hurt E.C., Grosjean H., and Branlant C. Pseudouridine mapping in the Saccharomyces cerevisiae spliceosomal U small nuclear RNAs (snRNAs) reveals that pseudouridine synthase Pus1p exhibits a dual substrate specificity for U2 snRNA and tRNA. Mol. Cell. Biol. 19 (1999) 2142-2154
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2142-2154
    • Massenet, S.1    Motorin, Y.2    Lafontaine, D.L.3    Hurt, E.C.4    Grosjean, H.5    Branlant, C.6
  • 30
    • 0142147324 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae U2 snRNA:pseudouridine-synthase Pus7p is a novel multisite-multisubstrate RNA:{Psi}-synthase also acting on tRNAs
    • Behm-Ansmant I., Urban A., Ma X., Yu Y.-T., Motorin Y., and Branlant C. The Saccharomyces cerevisiae U2 snRNA:pseudouridine-synthase Pus7p is a novel multisite-multisubstrate RNA:{Psi}-synthase also acting on tRNAs. RNA 9 (2003) 1371-1382
    • (2003) RNA , vol.9 , pp. 1371-1382
    • Behm-Ansmant, I.1    Urban, A.2    Ma, X.3    Yu, Y.-T.4    Motorin, Y.5    Branlant, C.6
  • 31
    • 0034528502 scopus 로고    scopus 로고
    • Mouse pseudouridine synthase 1: gene structure and alternative splicing of pre-mRNA
    • Chen J., and Patton J.R. Mouse pseudouridine synthase 1: gene structure and alternative splicing of pre-mRNA. Biochem J. 352 (2000) 465-473
    • (2000) Biochem J. , vol.352 , pp. 465-473
    • Chen, J.1    Patton, J.R.2
  • 32
    • 0035312526 scopus 로고    scopus 로고
    • A developmental transition in definitive erythropoiesis: erythropoietin expression is sequentially regulated by retinoic acid receptors and HNF4
    • Makita T., Hernandez-Hoyos G., Chen T.H., Wu H., Rothenberg E.V., and Sucov H.M. A developmental transition in definitive erythropoiesis: erythropoietin expression is sequentially regulated by retinoic acid receptors and HNF4. Genes Dev. 15 (2001) 889-901
    • (2001) Genes Dev. , vol.15 , pp. 889-901
    • Makita, T.1    Hernandez-Hoyos, G.2    Chen, T.H.3    Wu, H.4    Rothenberg, E.V.5    Sucov, H.M.6
  • 33
    • 0031018874 scopus 로고    scopus 로고
    • Regulation of cellular iron metabolism by erythropoiet
    • Activation of iron-regulatory protein and upregulation of transferrin receptor expression in erythroid cells
    • Weiss G., Houston T., Kastner S., Johrer K., Grunewald K., and Brock J.H. Regulation of cellular iron metabolism by erythropoiet. Activation of iron-regulatory protein and upregulation of transferrin receptor expression in erythroid cells. Blood 89 (1997) 680-687
    • (1997) Blood , vol.89 , pp. 680-687
    • Weiss, G.1    Houston, T.2    Kastner, S.3    Johrer, K.4    Grunewald, K.5    Brock, J.H.6
  • 34
    • 0030763793 scopus 로고    scopus 로고
    • Complex regulation of transferrin receptors during erythropoietin-induced differentiation of J2E erythroid cells-elevated transcription and mRNA stabilisation produce only a modest rise in protein content
    • Busfield S.J., Tilbrook P.A., Callus B.A., Spadaccini A., Kuhn L., and Klinken S.P. Complex regulation of transferrin receptors during erythropoietin-induced differentiation of J2E erythroid cells-elevated transcription and mRNA stabilisation produce only a modest rise in protein content. Eur. J. Biochem. 249 (1997) 77-84
    • (1997) Eur. J. Biochem. , vol.249 , pp. 77-84
    • Busfield, S.J.1    Tilbrook, P.A.2    Callus, B.A.3    Spadaccini, A.4    Kuhn, L.5    Klinken, S.P.6
  • 35
    • 0036037048 scopus 로고    scopus 로고
    • Erythroid 5-aminolevulinate synthase, ferrochelatase and DMT1 expression in erythroid progenitors: differential pathways for erythropoietin and iron-dependent regulation
    • Zoller H., Decristoforo C., and Weiss G. Erythroid 5-aminolevulinate synthase, ferrochelatase and DMT1 expression in erythroid progenitors: differential pathways for erythropoietin and iron-dependent regulation. Br. J. Haematol. 118 (2002) 619-626
    • (2002) Br. J. Haematol. , vol.118 , pp. 619-626
    • Zoller, H.1    Decristoforo, C.2    Weiss, G.3
  • 36
    • 0027479724 scopus 로고
    • A double life: cytosolic aconitase as a regulatory RNA binding protein
    • Klausner R.D., and Rouault T.A. A double life: cytosolic aconitase as a regulatory RNA binding protein. Mol. Biol. Cell 4 (1993) 1-5
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1-5
    • Klausner, R.D.1    Rouault, T.A.2
  • 37
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • Hentze M.W., and Kuhn L.C. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc. Natl. Acad. Sci. USA 93 (1996) 8175-8182
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kuhn, L.C.2
  • 38
    • 0031028178 scopus 로고    scopus 로고
    • Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanisms in erythroid cells
    • Ponka P. Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanisms in erythroid cells. Blood 89 (1997) 1-25
    • (1997) Blood , vol.89 , pp. 1-25
    • Ponka, P.1
  • 40
    • 0032832182 scopus 로고    scopus 로고
    • Regulation of erythroid 5-aminolevulinate synthase expression during erythropoiesis
    • Sadlon T.J., Dell'Oso T., Surinya K.H., and May B.K. Regulation of erythroid 5-aminolevulinate synthase expression during erythropoiesis. Int. J. Biochem. Cell Biol. 31 (1999) 1153-1167
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 1153-1167
    • Sadlon, T.J.1    Dell'Oso, T.2    Surinya, K.H.3    May, B.K.4
  • 41
    • 0024819020 scopus 로고
    • Iron regulation of transferrin receptor mRNA levels requires iron-responsive elements and a rapid turnover determinant in the 3′ untranslated region of the mRNA
    • Casey J.L., Koeller D.M., Ramin V.C., Klausner R.D., and Harford J.B. Iron regulation of transferrin receptor mRNA levels requires iron-responsive elements and a rapid turnover determinant in the 3′ untranslated region of the mRNA. EMBO J. 8 (1989) 3693-3699
    • (1989) EMBO J. , vol.8 , pp. 3693-3699
    • Casey, J.L.1    Koeller, D.M.2    Ramin, V.C.3    Klausner, R.D.4    Harford, J.B.5
  • 42
    • 0025248551 scopus 로고
    • Regulation of ferritin and transferrin receptor mRNAs
    • Theil E.C. Regulation of ferritin and transferrin receptor mRNAs. J. Biol. Chem. 265 (1990) 4771-4774
    • (1990) J. Biol. Chem. , vol.265 , pp. 4771-4774
    • Theil, E.C.1
  • 43
    • 33746820269 scopus 로고    scopus 로고
    • Alternative splicing of the first intron of the steroid receptor RNA activator (SRA) participates in the generation of coding and noncoding RNA isoforms in breast cancer cell lines
    • Hube F., Guo J., Chooniedass-Kothari S., Cooper C., Hamedani M.K., Dibrov A.A., Blanchard A.A., Wang X., Deng G., Myal Y., and Leygue E. Alternative splicing of the first intron of the steroid receptor RNA activator (SRA) participates in the generation of coding and noncoding RNA isoforms in breast cancer cell lines. DNA Cell Biol. 25 (2006) 418-428
    • (2006) DNA Cell Biol. , vol.25 , pp. 418-428
    • Hube, F.1    Guo, J.2    Chooniedass-Kothari, S.3    Cooper, C.4    Hamedani, M.K.5    Dibrov, A.A.6    Blanchard, A.A.7    Wang, X.8    Deng, G.9    Myal, Y.10    Leygue, E.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.