메뉴 건너뛰기




Volumn 113, Issue 2, 2003, Pages 140-148

Disruption of exon definition produces a dominant-negative growth hormone isoform that causes somatotroph death and IGHD II

Author keywords

[No Author keywords available]

Indexed keywords

GROWTH HORMONE;

EID: 0037897328     PISSN: 03406717     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00439-003-0949-x     Document Type: Article
Times cited : (54)

References (35)
  • 1
    • 0036235583 scopus 로고    scopus 로고
    • Regulation of alternative splicing by SRrp86 through co-activation and repression of specific SR proteins
    • Barnard D, Li J, Peng R, Patton JG (2002) Regulation of alternative splicing by SRrp86 through co-activation and repression of specific SR proteins. RNA 8:526-533
    • (2002) RNA , vol.8 , pp. 526-533
    • Barnard, D.1    Li, J.2    Peng, R.3    Patton, J.G.4
  • 2
    • 0028895417 scopus 로고
    • Exon recognition in vertebrate splicing
    • Berget SM (1995) Exon recognition in vertebrate splicing. J Biol Chem 270:2411-2414
    • (1995) J Biol Chem , vol.270 , pp. 2411-2414
    • Berget, S.M.1
  • 3
    • 0028955078 scopus 로고
    • Screening for growth hormone (GH) gene splice-site mutations in sporadic cases with severe isolated GH deficiency using ectopic transcript analysis
    • Binder G, Ranke M (1995) Screening for growth hormone (GH) gene splice-site mutations in sporadic cases with severe isolated GH deficiency using ectopic transcript analysis. J Clin Endocrinol Metab 80:1247-52
    • (1995) J Clin Endocrinol Metab , vol.80 , pp. 1247-1252
    • Binder, G.1    Ranke, M.2
  • 4
    • 0029839542 scopus 로고    scopus 로고
    • Mechanisms responsible for dominant expression of human growth hormone gene mutations
    • Binder G, Brown M, Parks J (1996) Mechanisms responsible for dominant expression of human growth hormone gene mutations. J Clin Endocrinol Metab 81:4047-50
    • (1996) J Clin Endocrinol Metab , vol.81 , pp. 4047-4050
    • Binder, G.1    Brown, M.2    Parks, J.3
  • 6
    • 0029382603 scopus 로고
    • Finding splice sites within a wilderness of RNA
    • Black DL (1995) Finding splice sites within a wilderness of RNA. RNA 1:763-771
    • (1995) RNA , vol.1 , pp. 763-771
    • Black, D.L.1
  • 7
    • 0034161419 scopus 로고    scopus 로고
    • Exonic splicing enhancers: Mechanism of action, diversity and role in human genetic disease
    • Blencowe BJ (2000) Exonic splicing enhancers: Mechanism of action, diversity and role in human genetic disease. Trends Biol Sci 25:106-110
    • (2000) Trends Biol Sci , vol.25 , pp. 106-110
    • Blencowe, B.J.1
  • 8
    • 0033780676 scopus 로고    scopus 로고
    • Long-term follow-up evaluation of magnetic resonance imaging in the prognosis of permanent GH deficiency
    • Bozzola M, Mengarda F, Sartirana P, Tato L, Chaussain JL (2000) Long-term follow-up evaluation of magnetic resonance imaging in the prognosis of permanent GH deficiency. Eur J Endocrinol 143:493-496
    • (2000) Eur J Endocrinol , vol.143 , pp. 493-496
    • Bozzola, M.1    Mengarda, F.2    Sartirana, P.3    Tato, L.4    Chaussain, J.L.5
  • 9
    • 0036207384 scopus 로고    scopus 로고
    • Listening to silence and understanding nonsense: Exonic mutations that affect splicing
    • Cartegni L, Chew SL, Krainer AR (2002) Listening to silence and understanding nonsense: Exonic mutations that affect splicing. Nat Rev Genet 3:285-298
    • (2002) Nat Rev Genet , vol.3 , pp. 285-298
    • Cartegni, L.1    Chew, S.L.2    Krainer, A.R.3
  • 12
    • 0028989162 scopus 로고
    • Run-around PCR: A novel way to create duplications using polymerase chain reaction
    • Coolidge CJ, Patton JG (1995) Run-around PCR: A novel way to create duplications using polymerase chain reaction. Biotechniques 18:763-764
    • (1995) Biotechniques , vol.18 , pp. 763-764
    • Coolidge, C.J.1    Patton, J.G.2
  • 13
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • De Vos A, Ultsch M, Kossiakoff A (1992) Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex. Science 255:306-312
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.1    Ultsch, M.2    Kossiakoff, A.3
  • 14
    • 0034885411 scopus 로고    scopus 로고
    • Autosomal dominant GH deficiency due to an Arg183His GH-1 gene mutation: Clinical and molecular evidence of impaired regulated GH secretion
    • Deladoey J, Stocker P, Mullis P (2001) Autosomal dominant GH deficiency due to an Arg183His GH-1 gene mutation: Clinical and molecular evidence of impaired regulated GH secretion. J Clin Endocrinol Metab 86:3941-3947
    • (2001) J Clin Endocrinol Metab , vol.86 , pp. 3941-3947
    • Deladoey, J.1    Stocker, P.2    Mullis, P.3
  • 15
    • 0002792844 scopus 로고    scopus 로고
    • Molecular heterogeneity of familial isolated growth hormone deficiency, type II: A novel IVS3+2 T→C splicing mutation in the GH-1 gene
    • Fofanova O, Evgrafov O, Polyakov A, Polltouraus A, Peterkova V, Dedov I (2000) Molecular heterogeneity of familial isolated growth hormone deficiency, type II: A novel IVS3+2 T→C splicing mutation in the GH-1 gene. Horm Res 53S2:56A
    • (2000) Horm Res , vol.53 , Issue.S2
    • Fofanova, O.1    Evgrafov, O.2    Polyakov, A.3    Polltouraus, A.4    Peterkova, V.5    Dedov, I.6
  • 16
    • 0032538791 scopus 로고    scopus 로고
    • A systematic analysis of the factors that determine the strength of pre-mRNA splicing enhancers
    • Graveley BR, Hertel KJ, Maniatis T (1998) A systematic analysis of the factors that determine the strength of pre-mRNA splicing enhancers. EMBO J 17:6747-6756
    • (1998) EMBO J , vol.17 , pp. 6747-6756
    • Graveley, B.R.1    Hertel, K.J.2    Maniatis, T.3
  • 17
    • 0034764940 scopus 로고    scopus 로고
    • Misfolded growth hormone causes fragmentation of the Golgi apparatus and disrupts endoplasmic reticulum-to-Golgi traffic
    • Graves TK, Patel S, Dannies PS, Hinkle PM (2001) Misfolded growth hormone causes fragmentation of the Golgi apparatus and disrupts endoplasmic reticulum-to-Golgi traffic. J Cell Sci 114:3685-3694
    • (2001) J Cell Sci , vol.114 , pp. 3685-3694
    • Graves, T.K.1    Patel, S.2    Dannies, P.S.3    Hinkle, P.M.4
  • 19
    • 0033304919 scopus 로고    scopus 로고
    • Inhibition of growth hormone (GH) secretion by a mutant GH-I gene product in neuroendocrine cells containing secretory granules: An implication for isolated GH deficiency inherited in an autosomal dominant manner
    • Hayashi Y, Yamamoto M, Ohmori S, Kamijo T, Ogawa M, Seo H (1999b) Inhibition of growth hormone (GH) secretion by a mutant GH-I gene product in neuroendocrine cells containing secretory granules: An implication for isolated GH deficiency inherited in an autosomal dominant manner. J Clin Endocrinol Metab 84:2134-2139
    • (1999) J Clin Endocrinol Metab , vol.84 , pp. 2134-2139
    • Hayashi, Y.1    Yamamoto, M.2    Ohmori, S.3    Kamijo, T.4    Ogawa, M.5    Seo, H.6
  • 20
    • 0028806064 scopus 로고
    • The human growth hormone gene is regulated by a multicomponent locus control region
    • Jones B, Monks B, Liebhaber S, Cooke N (1995) The human growth hormone gene is regulated by a multicomponent locus control region. Mol Cell Biol 15:7010-7021
    • (1995) Mol Cell Biol , vol.15 , pp. 7010-7021
    • Jones, B.1    Monks, B.2    Liebhaber, S.3    Cooke, N.4
  • 21
    • 0036792889 scopus 로고    scopus 로고
    • A general role for splicing enhancers in exon definition
    • Lam B, Hertel K (2002) A general role for splicing enhancers in exon definition. RNA 8:1233-1241
    • (2002) RNA , vol.8 , pp. 1233-1241
    • Lam, B.1    Hertel, K.2
  • 22
    • 0034465474 scopus 로고    scopus 로고
    • Autosomal dominant growth hormone (GH) deficiency type II: The Del32-71-GH deletion mutant suppresses secretion of wild-type GH*
    • Lee M, Wajnrajch M, Kim S, Plotnick L, Wang J, Gertner J, Leibel R, Dannies P (2000) Autosomal dominant growth hormone (GH) deficiency type II: The Del32-71-GH deletion mutant suppresses secretion of wild-type GH*. Endocrinology 141:883-890
    • (2000) Endocrinology , vol.141 , pp. 883-890
    • Lee, M.1    Wajnrajch, M.2    Kim, S.3    Plotnick, L.4    Wang, J.5    Gertner, J.6    Leibel, R.7    Dannies, P.8
  • 24
    • 0025145822 scopus 로고
    • The 20,000 Da variant of human growth hormone does not bind to growth hormone receptors in human liver
    • McCarter J, Shaw M, Winer L, Baumann G (1990) The 20,000 Da variant of human growth hormone does not bind to growth hormone receptors in human liver. Mol Cell Endocrinol 73:11-14
    • (1990) Mol Cell Endocrinol , vol.73 , pp. 11-14
    • McCarter, J.1    Shaw, M.2    Winer, L.3    Baumann, G.4
  • 26
    • 0031468346 scopus 로고    scopus 로고
    • Two different 5′ splice site mutations in the growth hormone gene causing autosomal dominant growth hormone deficiency
    • Missarelli C, Herrera L, Merica V, Carvallo P (1997) Two different 5′ splice site mutations in the growth hormone gene causing autosomal dominant growth hormone deficiency. Hum Genet 101:113-117
    • (1997) Hum Genet , vol.101 , pp. 113-117
    • Missarelli, C.1    Herrera, L.2    Merica, V.3    Carvallo, P.4
  • 28
    • 0027982794 scopus 로고
    • Genetic basis of endocrine disease. 6. Molecular basis of familial human growth hormone deficiency
    • Phillips III JA, Cogan J (1994) Genetic basis of endocrine disease. 6. Molecular basis of familial human growth hormone deficiency. J Clin Endocrinol Metab 78:11-6
    • (1994) J Clin Endocrinol Metab , vol.78 , pp. 11-16
    • Phillips J.A. III1    Cogan, J.2
  • 30
    • 0031682082 scopus 로고    scopus 로고
    • The molecular genetics of growth hormone deficiency
    • Procter A, Phillips III JA, Cooper D (1998) The molecular genetics of growth hormone deficiency. Hum Genet 103:255-272
    • (1998) Hum Genet , vol.103 , pp. 255-272
    • Procter, A.1    Phillips J.A. III2    Cooper, D.3
  • 31
    • 0023651307 scopus 로고
    • RNA splice junctions of different classes of eukaryotes: Sequence statistics and functional implications in gene expression
    • Shapiro MB, Senepathy P (1987) RNA splice junctions of different classes of eukaryotes: Sequence statistics and functional implications in gene expression. Nucleic Acids Res 15:7155-7174
    • (1987) Nucleic Acids Res , vol.15 , pp. 7155-7174
    • Shapiro, M.B.1    Senepathy, P.2
  • 32
    • 0034256020 scopus 로고    scopus 로고
    • Alternative pre-mRNA splicing: The logic of combinatorial control
    • Smith CWJ, Valcarcel J (2000) Alternative pre-mRNA splicing: The logic of combinatorial control. Trends Biol Sci 25:381-388
    • (2000) Trends Biol Sci , vol.25 , pp. 381-388
    • Smith, C.W.J.1    Valcarcel, J.2
  • 33
    • 0026506815 scopus 로고
    • An evaluation of the functions of the 22-kilodalton (kDa), the 20-kDa, and the N-terminal polypeptide forms of human growth hormone using transgenic mice
    • Stewart T, Clift S, Pitts-Meek S, Martin L, Terrell T, Liggitt D, Oakley H (1992) An evaluation of the functions of the 22-kilodalton (kDa), the 20-kDa, and the N-terminal polypeptide forms of human growth hormone using transgenic mice. Endocrinology 130:405-414
    • (1992) Endocrinology , vol.130 , pp. 405-414
    • Stewart, T.1    Clift, S.2    Pitts-Meek, S.3    Martin, L.4    Terrell, T.5    Liggitt, D.6    Oakley, H.7
  • 34
    • 0034677895 scopus 로고    scopus 로고
    • The human growth hormone gene cluster locus control region supports position-independent pituitary- and placenta-specific expression in the transgenic mouse
    • Su Y, Liebhaber SA, Cooke NE (2000) The human growth hormone gene cluster locus control region supports position-independent pituitary- and placenta-specific expression in the transgenic mouse. J Biol Chem 275:7902-7909
    • (2000) J Biol Chem , vol.275 , pp. 7902-7909
    • Su, Y.1    Liebhaber, S.A.2    Cooke, N.E.3
  • 35
    • 0031893308 scopus 로고    scopus 로고
    • The 20-kilodalton (kDa) human growth hormone (hGH) differs from the 22-kDa hGH in the complex formation with cell surface hGH receptor and hGH-binding protein circulating in human plasma
    • Wada M, Uchida H, Ikeda M, Tsunekawa B, Naito N, Banba S, Tanaka E, Hashimoto Y, Honjo M (1998) The 20-kilodalton (kDa) human growth hormone (hGH) differs from the 22-kDa hGH in the complex formation with cell surface hGH receptor and hGH-binding protein circulating in human plasma. Mol Endocrinol 12:146-156
    • (1998) Mol Endocrinol , vol.12 , pp. 146-156
    • Wada, M.1    Uchida, H.2    Ikeda, M.3    Tsunekawa, B.4    Naito, N.5    Banba, S.6    Tanaka, E.7    Hashimoto, Y.8    Honjo, M.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.