메뉴 건너뛰기




Volumn 322, Issue 1-2, 2010, Pages 38-43

Genetics and phenomics of hypothyroidism and goiter due to TPO mutations

Author keywords

Hypothyroidism; Iodide; Iodine; Peroxidase; Thyroid

Indexed keywords

IODINE; MESSENGER RNA; THYROID HORMONE; THYROID PEROXIDASE;

EID: 77952876664     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2010.02.008     Document Type: Review
Times cited : (106)

References (50)
  • 2
    • 0025156878 scopus 로고
    • Thyroid peroxidase gene promoter confers TSH responsiveness to heterologous reporter genes in transfection experiments
    • Abramowicz M.J., Vassart G., Christophe D. Thyroid peroxidase gene promoter confers TSH responsiveness to heterologous reporter genes in transfection experiments. Biochem. Biophys. Res. Commun. 1990, 166(3):1257-1264.
    • (1990) Biochem. Biophys. Res. Commun. , vol.166 , Issue.3 , pp. 1257-1264
    • Abramowicz, M.J.1    Vassart, G.2    Christophe, D.3
  • 4
    • 0031025824 scopus 로고    scopus 로고
    • Molecular analysis of mutated thyroid peroxidase detected in patients with total iodide organification defects
    • Bikker H., Baas F., de Vijlder J.J. Molecular analysis of mutated thyroid peroxidase detected in patients with total iodide organification defects. J. Clin. Endocrinol. Metab. 1997, 82(2):649-653.
    • (1997) J. Clin. Endocrinol. Metab. , vol.82 , Issue.2 , pp. 649-653
    • Bikker, H.1    Baas, F.2    de Vijlder, J.J.3
  • 5
    • 0030013089 scopus 로고    scopus 로고
    • Congenital hypothyroidism caused by a premature termination signal in exon 10 of the human thyroid peroxidase gene
    • Bikker H., Waelkens J.J., Bravenboer B., de Vijlder J.J. Congenital hypothyroidism caused by a premature termination signal in exon 10 of the human thyroid peroxidase gene. J. Clin. Endocrinol. Metab. 1996, 81(6):2076-2079.
    • (1996) J. Clin. Endocrinol. Metab. , vol.81 , Issue.6 , pp. 2076-2079
    • Bikker, H.1    Waelkens, J.J.2    Bravenboer, B.3    de Vijlder, J.J.4
  • 8
    • 0021119989 scopus 로고
    • Thyroglobulin and thyroid hormone synthesis
    • Cody V. Thyroglobulin and thyroid hormone synthesis. Endocr. Res. 1984, 10(1):73-88.
    • (1984) Endocr. Res. , vol.10 , Issue.1 , pp. 73-88
    • Cody, V.1
  • 9
    • 0030053759 scopus 로고    scopus 로고
    • Cloning and characterization of the thyroid iodide transporter
    • Dai G., Levy O., Carrasco N. Cloning and characterization of the thyroid iodide transporter. Nature 1996, 379(6564):458-460.
    • (1996) Nature , vol.379 , Issue.6564 , pp. 458-460
    • Dai, G.1    Levy, O.2    Carrasco, N.3
  • 13
    • 0002527566 scopus 로고    scopus 로고
    • Hereditary metabolic disorders causing hypothyroidism
    • Lippincott-Raven, Philadelphia, L.E. Braverman, R.D. Utiger (Eds.)
    • de Vijlder J.J.M., Vulsma T. Hereditary metabolic disorders causing hypothyroidism. Werner and Ingbar's the Thyroid: A Fundamental and Clinical Text 1996, 749-755. Lippincott-Raven, Philadelphia. 7 edn. L.E. Braverman, R.D. Utiger (Eds.).
    • (1996) Werner and Ingbar's the Thyroid: A Fundamental and Clinical Text , pp. 749-755
    • de Vijlder, J.J.M.1    Vulsma, T.2
  • 14
    • 0014217545 scopus 로고
    • Thyroglobulin from human goiters. Effects of iodination on sedimentation and iodoamino acid synthesis
    • DeCrombrugghe B., Edelhoch H., Beckers C., De Visscher M. Thyroglobulin from human goiters. Effects of iodination on sedimentation and iodoamino acid synthesis. J. Biol. Chem. 1967, 242(24):5681-5685.
    • (1967) J. Biol. Chem. , vol.242 , Issue.24 , pp. 5681-5685
    • DeCrombrugghe, B.1    Edelhoch, H.2    Beckers, C.3    De Visscher, M.4
  • 15
    • 0017414240 scopus 로고
    • Biosynthesis of thyroid hormone: basic and clinical aspects
    • DeGroot L.J., Niepomniszcze H. Biosynthesis of thyroid hormone: basic and clinical aspects. Metabolism 1977, 26(6):665-718.
    • (1977) Metabolism , vol.26 , Issue.6 , pp. 665-718
    • DeGroot, L.J.1    Niepomniszcze, H.2
  • 16
    • 33646772555 scopus 로고    scopus 로고
    • Congenital hypothyroidism: from paracelsus to molecular diagnosis
    • Djemli A., Van Vliet G., Delvin E.E. Congenital hypothyroidism: from paracelsus to molecular diagnosis. Clin. Biochem. 2006, 39(5):511-518.
    • (2006) Clin. Biochem. , vol.39 , Issue.5 , pp. 511-518
    • Djemli, A.1    Van Vliet, G.2    Delvin, E.E.3
  • 18
    • 0032055851 scopus 로고    scopus 로고
    • PAX 8 activates the enhancer of the human thyroperoxidase gene
    • Esposito C., Miccadei S., Saiardi A., Civitareale D. PAX 8 activates the enhancer of the human thyroperoxidase gene. Biochem. J. 1998, 331(Pt 1):37-40.
    • (1998) Biochem. J. , vol.331 , Issue.PART 1 , pp. 37-40
    • Esposito, C.1    Miccadei, S.2    Saiardi, A.3    Civitareale, D.4
  • 19
    • 0025305344 scopus 로고
    • Studies on the functional activity of the promoter for the human thyroid peroxidase gene
    • Foti D., Gestautas J., Rapoport B. Studies on the functional activity of the promoter for the human thyroid peroxidase gene. Biochem. Biophys. Res. Commun. 1990, 168(1):281-287.
    • (1990) Biochem. Biophys. Res. Commun. , vol.168 , Issue.1 , pp. 281-287
    • Foti, D.1    Gestautas, J.2    Rapoport, B.3
  • 21
    • 33751052250 scopus 로고    scopus 로고
    • Cloning and characterization of a novel isoform of iodotyrosine dehalogenase 1 (DEHAL1) DEHAL1C from human thyroid: comparisons with DEHAL1 and DEHAL1B
    • Gnidehou S., Lacroix L., Sezan A., Ohayon R., Noel-Hudson M.S., Morand S., Francon J., Courtin F., Virion A., Dupuy C. Cloning and characterization of a novel isoform of iodotyrosine dehalogenase 1 (DEHAL1) DEHAL1C from human thyroid: comparisons with DEHAL1 and DEHAL1B. Thyroid 2006, 16(8):715-724.
    • (2006) Thyroid , vol.16 , Issue.8 , pp. 715-724
    • Gnidehou, S.1    Lacroix, L.2    Sezan, A.3    Ohayon, R.4    Noel-Hudson, M.S.5    Morand, S.6    Francon, J.7    Courtin, F.8    Virion, A.9    Dupuy, C.10
  • 22
    • 33745821178 scopus 로고    scopus 로고
    • Identification of the maturation factor for dual oxidase. Evolution of an eukaryotic operon equivalent
    • Grasberger H., Refetoff S. Identification of the maturation factor for dual oxidase. Evolution of an eukaryotic operon equivalent. J. Biol. Chem. 2006, 281(27):18269-18272.
    • (2006) J. Biol. Chem. , vol.281 , Issue.27 , pp. 18269-18272
    • Grasberger, H.1    Refetoff, S.2
  • 23
    • 34447134181 scopus 로고    scopus 로고
    • A familial thyrotropin (TSH) receptor mutation provides in vivo evidence that the inositol phosphates/Ca2+ cascade mediates TSH action on thyroid hormone synthesis
    • Grasberger H., Van S.J., Hag-Dahood M.A., Tenenbaum-Rakover Y., Refetoff S. A familial thyrotropin (TSH) receptor mutation provides in vivo evidence that the inositol phosphates/Ca2+ cascade mediates TSH action on thyroid hormone synthesis. J. Clin. Endocrinol. Metab. 2007, 92(7):2816-2820.
    • (2007) J. Clin. Endocrinol. Metab. , vol.92 , Issue.7 , pp. 2816-2820
    • Grasberger, H.1    Van, S.J.2    Hag-Dahood, M.A.3    Tenenbaum-Rakover, Y.4    Refetoff, S.5
  • 24
    • 0033323823 scopus 로고    scopus 로고
    • Two novel cysteine substitutions (C1263R and C1995S) of thyroglobulin cause a defect in intracellular transport of thyroglobulin in patients with congenital goiter and the variant type of adenomatous goiter
    • Hishinuma A., Takamatsu J., Ohyama Y., Yokozawa T., Kanno Y., Kuma K., Yoshida S., Matsuura N., Ieiri T. Two novel cysteine substitutions (C1263R and C1995S) of thyroglobulin cause a defect in intracellular transport of thyroglobulin in patients with congenital goiter and the variant type of adenomatous goiter. J. Clin. Endocrinol. Metab. 1999, 84(4):1438-1444.
    • (1999) J. Clin. Endocrinol. Metab. , vol.84 , Issue.4 , pp. 1438-1444
    • Hishinuma, A.1    Takamatsu, J.2    Ohyama, Y.3    Yokozawa, T.4    Kanno, Y.5    Kuma, K.6    Yoshida, S.7    Matsuura, N.8    Ieiri, T.9
  • 25
    • 0021332450 scopus 로고
    • Outcome for congenital hypothyroidism
    • Hulse J.A. Outcome for congenital hypothyroidism. Arch. Dis. Child. 1984, 59(1):23-29.
    • (1984) Arch. Dis. Child. , vol.59 , Issue.1 , pp. 23-29
    • Hulse, J.A.1
  • 26
    • 0024375696 scopus 로고
    • Structure of the human thyroid peroxidase gene: comparison and relationship to the human myeloperoxidase gene
    • Kimura S., Hong Y.S., Kotani T., Ohtaki S., Kikkawa F. Structure of the human thyroid peroxidase gene: comparison and relationship to the human myeloperoxidase gene. Biochemistry 1989, 28(10):4481-4489.
    • (1989) Biochemistry , vol.28 , Issue.10 , pp. 4481-4489
    • Kimura, S.1    Hong, Y.S.2    Kotani, T.3    Ohtaki, S.4    Kikkawa, F.5
  • 27
    • 2042500693 scopus 로고
    • Human thyroid peroxidase: complete cDNA and protein sequence, chromosome mapping, and identification of two alternately spliced mRNAs
    • Kimura S., Kotani T., McBride O.W., Umeki K., Hirai K., Nakayama T., Ohtaki S. Human thyroid peroxidase: complete cDNA and protein sequence, chromosome mapping, and identification of two alternately spliced mRNAs. Proc. Natl. Acad. Sci. U.S.A. 1987, 84(16):5555-5559.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , Issue.16 , pp. 5555-5559
    • Kimura, S.1    Kotani, T.2    McBride, O.W.3    Umeki, K.4    Hirai, K.5    Nakayama, T.6    Ohtaki, S.7
  • 28
    • 0042666816 scopus 로고    scopus 로고
    • Partial iodide organification defect caused by a novel mutation of the thyroid peroxidase gene in three siblings
    • Kotani T., Umeki K., Kawano J., Suganuma T., Hishinuma A., Ieiri T., Harada S. Partial iodide organification defect caused by a novel mutation of the thyroid peroxidase gene in three siblings. Clin. Endocrinol. (Oxf.) 2003, 59(2):198-206.
    • (2003) Clin. Endocrinol. (Oxf.) , vol.59 , Issue.2 , pp. 198-206
    • Kotani, T.1    Umeki, K.2    Kawano, J.3    Suganuma, T.4    Hishinuma, A.5    Ieiri, T.6    Harada, S.7
  • 29
    • 0035920812 scopus 로고    scopus 로고
    • Iodide organification defects resulting from cosegregation of mutated and null thyroid peroxidase alleles
    • Kotani T., Umeki K., Yamamoto I., Ohtaki S., Adachi M., Tachibana K. Iodide organification defects resulting from cosegregation of mutated and null thyroid peroxidase alleles. Mol. Cell. Endocrinol. 2001, 182(1):61-68.
    • (2001) Mol. Cell. Endocrinol. , vol.182 , Issue.1 , pp. 61-68
    • Kotani, T.1    Umeki, K.2    Yamamoto, I.3    Ohtaki, S.4    Adachi, M.5    Tachibana, K.6
  • 31
    • 0023661371 scopus 로고
    • Thyroperoxidase, an auto-antigen with a mosaic structure made of nuclear and mitochondrial gene modules
    • Libert F., Ruel J., Ludgate M., Swillens S., Alexander N., Vassart G., Dinsart C. Thyroperoxidase, an auto-antigen with a mosaic structure made of nuclear and mitochondrial gene modules. EMBO J. 1987, 6(13):4193-4196.
    • (1987) EMBO J. , vol.6 , Issue.13 , pp. 4193-4196
    • Libert, F.1    Ruel, J.2    Ludgate, M.3    Swillens, S.4    Alexander, N.5    Vassart, G.6    Dinsart, C.7
  • 35
    • 0347993689 scopus 로고    scopus 로고
    • Thyroperoxidase gene mutations in congenital goitrous hypothyroidism with total and partial iodide organification defect
    • Nascimento A.C., Guedes D.R., Santos C.S., Knobel M., Rubio I.G., Medeiros-Neto G. Thyroperoxidase gene mutations in congenital goitrous hypothyroidism with total and partial iodide organification defect. Thyroid 2003, 13(12):1145-1151.
    • (2003) Thyroid , vol.13 , Issue.12 , pp. 1145-1151
    • Nascimento, A.C.1    Guedes, D.R.2    Santos, C.S.3    Knobel, M.4    Rubio, I.G.5    Medeiros-Neto, G.6
  • 36
    • 0043122919 scopus 로고    scopus 로고
    • SIFT: predicting amino acid changes that affect protein function
    • Ng P.C., Henikoff S. SIFT: predicting amino acid changes that affect protein function. Nucleic Acids Res. 2003, 31(13):3812-3814.
    • (2003) Nucleic Acids Res. , vol.31 , Issue.13 , pp. 3812-3814
    • Ng, P.C.1    Henikoff, S.2
  • 37
    • 0030691075 scopus 로고    scopus 로고
    • Human thyroperoxidase in its alternatively spliced form (TPO2) is enzymatically inactive and exhibits changes in intracellular processing and trafficking
    • Niccoli P., Fayadat L., Panneels V., Lanet J., Franc J.L. Human thyroperoxidase in its alternatively spliced form (TPO2) is enzymatically inactive and exhibits changes in intracellular processing and trafficking. J. Biol. Chem. 1997, 272(47):29487-29492.
    • (1997) J. Biol. Chem. , vol.272 , Issue.47 , pp. 29487-29492
    • Niccoli, P.1    Fayadat, L.2    Panneels, V.3    Lanet, J.4    Franc, J.L.5
  • 39
    • 18844400822 scopus 로고    scopus 로고
    • Genetics of congenital hypothyroidism
    • Park S.M., Chatterjee V.K. Genetics of congenital hypothyroidism. J. Med. Genet. 2005, 42(5):379-389.
    • (2005) J. Med. Genet. , vol.42 , Issue.5 , pp. 379-389
    • Park, S.M.1    Chatterjee, V.K.2
  • 40
    • 0031594239 scopus 로고    scopus 로고
    • Thyrotropin chronically regulates the pool of thyroperoxidase and its intracellular distribution: a quantitative confocal microscopic study
    • Penel C., Gruffat D., Alquier C., Benoliel A.M., Chabaud O. Thyrotropin chronically regulates the pool of thyroperoxidase and its intracellular distribution: a quantitative confocal microscopic study. J. Cell. Physiol. 1998, 174(2):160-169.
    • (1998) J. Cell. Physiol. , vol.174 , Issue.2 , pp. 160-169
    • Penel, C.1    Gruffat, D.2    Alquier, C.3    Benoliel, A.M.4    Chabaud, O.5
  • 41
    • 0036713510 scopus 로고    scopus 로고
    • Human non-synonymous SNPs: server and survey
    • Ramensky V., Bork P., Sunyaev S. Human non-synonymous SNPs: server and survey. Nucleic Acids Res. 2002, 30(17):3894-3900.
    • (2002) Nucleic Acids Res. , vol.30 , Issue.17 , pp. 3894-3900
    • Ramensky, V.1    Bork, P.2    Sunyaev, S.3
  • 42
    • 33750017623 scopus 로고    scopus 로고
    • Molecular advances in thyroglobulin disorders
    • Rivolta C.M., Targovnik H.M. Molecular advances in thyroglobulin disorders. Clin. Chim. Acta 2006, 374(1-2):8-24.
    • (2006) Clin. Chim. Acta , vol.374 , Issue.1-2 , pp. 8-24
    • Rivolta, C.M.1    Targovnik, H.M.2
  • 43
    • 38949195105 scopus 로고    scopus 로고
    • Messenger RNA regulation: to translate or to degrade
    • Shyu A.B., Wilkinson M.F., van H.A. Messenger RNA regulation: to translate or to degrade. EMBO J. 2008, 27(3):471-481.
    • (2008) EMBO J. , vol.27 , Issue.3 , pp. 471-481
    • Shyu, A.B.1    Wilkinson, M.F.2    van, H.A.3
  • 45
    • 0014724834 scopus 로고
    • Thyroid peroxidase and thyroxine biosynthesis
    • Taurog A. Thyroid peroxidase and thyroxine biosynthesis. Recent Prog. Horm. Res. 1970, 26:189-247.
    • (1970) Recent Prog. Horm. Res. , vol.26 , pp. 189-247
    • Taurog, A.1
  • 47
    • 0042652185 scopus 로고    scopus 로고
    • Thyroid disease in newborns, infants and children
    • Oxford University Press, J.A. Wass, S.M. Shalet (Eds.)
    • Vulsma T., de Vijlder J.J.M. Thyroid disease in newborns, infants and children. Oxford Textbook of Endocrinology and Diabetes 2002, 532-544. Oxford University Press. J.A. Wass, S.M. Shalet (Eds.).
    • (2002) Oxford Textbook of Endocrinology and Diabetes , pp. 532-544
    • Vulsma, T.1    de Vijlder, J.J.M.2
  • 48
    • 0004645898 scopus 로고
    • The inhibitory action of iodide upon organic binding of iodine by the normal thyroid gland
    • Wolff J., Chaikoff I.L. The inhibitory action of iodide upon organic binding of iodine by the normal thyroid gland. J. Biol. Chem. 1948, 172(2):855.
    • (1948) J. Biol. Chem. , vol.172 , Issue.2 , pp. 855
    • Wolff, J.1    Chaikoff, I.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.