메뉴 건너뛰기




Volumn 256, Issue 1, 1998, Pages 221-228

Preferential pre-mRNA utilisation of an upstream cryptic 5' splice site created by a single base deletion mutation in exon 37 of the FBN-1 gene

Author keywords

Cryptic splicing; Exon mutation; Fibrillin; Marfan syndrome

Indexed keywords

FIBRILLIN; MESSENGER RNA;

EID: 0032529150     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2560221.x     Document Type: Article
Times cited : (4)

References (40)
  • 1
    • 0023002893 scopus 로고
    • Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils
    • Sakai, L. Y., Keene, D. R. & Engvall, E. (1986) Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils, J. Cell Biol. 103, 2499-2509.
    • (1986) J. Cell Biol. , vol.103 , pp. 2499-2509
    • Sakai, L.Y.1    Keene, D.R.2    Engvall, E.3
  • 2
    • 0029115657 scopus 로고
    • Fibrillin-containing microfibrils: Structure and function in health and disease
    • Kielty, C. M. & Shuttleworth, C. A. (1995) Fibrillin-containing microfibrils: Structure and function in health and disease, Int. J. Biochem. Cell Biol. 7, 747-760.
    • (1995) Int. J. Biochem. Cell Biol. , vol.7 , pp. 747-760
    • Kielty, C.M.1    Shuttleworth, C.A.2
  • 3
    • 0002212848 scopus 로고    scopus 로고
    • Elastic tissue, elastin and elastin-associated microfibrils
    • (Comper, W. D., ed.) Harwood Academic Publishers, Amsterdam
    • Cleary, E. G. & Gibson, M. A. (1996) Elastic tissue, elastin and elastin-associated microfibrils, in Extracellular matrix, (Comper, W. D., ed.) vol. 2, pp. 95-140, Harwood Academic Publishers, Amsterdam..
    • (1996) Extracellular Matrix , vol.2 , pp. 95-140
    • Cleary, E.G.1    Gibson, M.A.2
  • 4
    • 0028626352 scopus 로고
    • Marfan syndrome and other microfibrillar diseases
    • (Harris, H. & Hirschhorn, K., eds) Plenum Press, New York
    • Dietz, H. C., Ramirez, F. & Sakai, L. Y. (1994) Marfan syndrome and other microfibrillar diseases, in Advances in human genetics (Harris, H. & Hirschhorn, K., eds) vol. 22, pp. 153-186, Plenum Press, New York.
    • (1994) Advances in Human Genetics , vol.22 , pp. 153-186
    • Dietz, H.C.1    Ramirez, F.2    Sakai, L.Y.3
  • 5
    • 0028852659 scopus 로고
    • Mutations in the human gene tor fibrillin-1 (FBN1) in the Marfan syndrome and related disorders
    • Dietz, H. C. & Pyeritz, R. E. (1995) Mutations in the human gene tor fibrillin-1 (FBN1) in the Marfan syndrome and related disorders, Hum. Mol. Genet. 4, 1799-1809.
    • (1995) Hum. Mol. Genet. , vol.4 , pp. 1799-1809
    • Dietz, H.C.1    Pyeritz, R.E.2
  • 6
    • 0029665565 scopus 로고    scopus 로고
    • Fibrillin mutations in Marfan syndrome and related phenotypes
    • Ramirez, F. (1996) Fibrillin mutations in Marfan syndrome and related phenotypes, Curr. Opin. Genet. Dev. 6, 309-315.
    • (1996) Curr. Opin. Genet. Dev. , vol.6 , pp. 309-315
    • Ramirez, F.1
  • 8
    • 0029745110 scopus 로고    scopus 로고
    • Characterisation of four novel fibrillin-1 (FBN1) mutations in Marfan syndrome
    • Ades, L. C., Haan, E. A., Colley, A. F. & Richard, R. I. (1996) Characterisation of four novel fibrillin-1 (FBN1) mutations in Marfan syndrome, J. Med. Genet. 33, 665-671.
    • (1996) J. Med. Genet. , vol.33 , pp. 665-671
    • Ades, L.C.1    Haan, E.A.2    Colley, A.F.3    Richard, R.I.4
  • 9
    • 0028335388 scopus 로고
    • Mutation in the fibrillin gene responsible for dominant ectopia lentis and neonatal Marfan syndrome
    • Kainulainen, K., Karttunen, L., Puhakka, L., Sakai, L. Y. & Peltonen, L. (1994) Mutation in the fibrillin gene responsible for dominant ectopia lentis and neonatal Marfan syndrome, Nat. Genet. 6, 64-69.
    • (1994) Nat. Genet. , vol.6 , pp. 64-69
    • Kainulainen, K.1    Karttunen, L.2    Puhakka, L.3    Sakai, L.Y.4    Peltonen, L.5
  • 10
    • 0029797761 scopus 로고    scopus 로고
    • Mutant fibrillin-1 monomers lacking EGF-like domains disrupt microfibril assembly and cause severe Marfan syndrome
    • Lui, W., Qian, C., Comeau, K., Brenn, T., Furthmayr, H. & Francke, U. (1996) Mutant fibrillin-1 monomers lacking EGF-like domains disrupt microfibril assembly and cause severe Marfan syndrome, Hum. Mol. Genet. 5, 1581-1587.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1581-1587
    • Lui, W.1    Qian, C.2    Comeau, K.3    Brenn, T.4    Furthmayr, H.5    Francke, U.6
  • 11
    • 0027379305 scopus 로고
    • Mutation screening of complete fibrillin-1 coding sequence: Report of five new mutations, including two in 8-cysteine domains
    • Tynan, K., Comeau, K., Pearson, M., Wilgenbus, P., Levitt, D., Gasner, C., Berg, M. A., Miller, D. C. & Francke, U. (1993) Mutation screening of complete fibrillin-1 coding sequence: report of five new mutations, including two in 8-cysteine domains, Hum. Mol. Genet. 2, 1813-1821.
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 1813-1821
    • Tynan, K.1    Comeau, K.2    Pearson, M.3    Wilgenbus, P.4    Levitt, D.5    Gasner, C.6    Berg, M.A.7    Miller, D.C.8    Francke, U.9
  • 13
    • 0029962419 scopus 로고    scopus 로고
    • Delineation of the Marfan phenotype associated with mutations in exons 23-32 of the FBN1 gene
    • Putman, E. A., Cho, M., Zinn, A. B., Towbin, J. A., Byers, P. H. & Milewicz, D. M. (1996) Delineation of the Marfan phenotype associated with mutations in exons 23-32 of the FBN1 gene, Am. J. Med. Genet. 62, 233-242.
    • (1996) Am. J. Med. Genet. , vol.62 , pp. 233-242
    • Putman, E.A.1    Cho, M.2    Zinn, A.B.3    Towbin, J.A.4    Byers, P.H.5    Milewicz, D.M.6
  • 15
    • 0028828221 scopus 로고
    • Fibrillin-2 (FBN2) mutations result in the Marfan-like disorder, congenital contractual arachnodactyly
    • Putman, E. A., Zhang, H., Ramirez, F. & Milewicz, D. M. (1995) Fibrillin-2 (FBN2) mutations result in the Marfan-like disorder, congenital contractual arachnodactyly, Nat. Genet. 11, 456-457.
    • (1995) Nat. Genet. , vol.11 , pp. 456-457
    • Putman, E.A.1    Zhang, H.2    Ramirez, F.3    Milewicz, D.M.4
  • 16
    • 0029908699 scopus 로고    scopus 로고
    • Familial occurrence of typical and severe lethal congenital contractural arachnodactyly caused by missplicing of exon 34 of fibrillin-2
    • Wang, M., Clericuzio, C. L. & Godfrey, M. (1996) Familial occurrence of typical and severe lethal congenital contractural arachnodactyly caused by missplicing of exon 34 of fibrillin-2, Am. J. Hum. Genet. 59, 1027-1034.
    • (1996) Am. J. Hum. Genet. , vol.59 , pp. 1027-1034
    • Wang, M.1    Clericuzio, C.L.2    Godfrey, M.3
  • 17
    • 0028988069 scopus 로고
    • Quantitation of fibrillin immunofluorescence in fibroblast cultures in the Marfan syndrome
    • Schaefer, G. B. & Godfrey, M. (1995) Quantitation of fibrillin immunofluorescence in fibroblast cultures in the Marfan syndrome, Clin. Genet. 47, 144-149.
    • (1995) Clin. Genet. , vol.47 , pp. 144-149
    • Schaefer, G.B.1    Godfrey, M.2
  • 18
    • 0028220980 scopus 로고
    • Abnormal fibrillin assembly by dermal fibroblasts from two patients with Marfan syndrome
    • Kielty, C. M. & Shuttleworth, C. A. (1994) Abnormal fibrillin assembly by dermal fibroblasts from two patients with Marfan syndrome, J. Cell Biol. 124, 997-1004.
    • (1994) J. Cell Biol. , vol.124 , pp. 997-1004
    • Kielty, C.M.1    Shuttleworth, C.A.2
  • 19
    • 0026585419 scopus 로고
    • Marfan syndrome: Defective synthesis, secretion, and extracellular matrix formation of fibrillin by cultured dermal fibroblasts
    • McGookey-Milewicz, D., Pyeritz, R. E., Crawford, E. S. & Byers, P. H. (1992) Marfan syndrome: defective synthesis, secretion, and extracellular matrix formation of fibrillin by cultured dermal fibroblasts, J. Clin. Invest. 89, 79-86.
    • (1992) J. Clin. Invest. , vol.89 , pp. 79-86
    • McGookey-Milewicz, D.1    Pyeritz, R.E.2    Crawford, E.S.3    Byers, P.H.4
  • 20
    • 0027738563 scopus 로고
    • Missense mutations impair intracellular processing of fibrillin and microfibril assembly in Marfan syndrome
    • Aoyama, T., Tynan, K., Dietz, H. C. Francke, U. & Furthmayr, H. (1993) Missense mutations impair intracellular processing of fibrillin and microfibril assembly in Marfan syndrome, Hum. Mol. Genet. 12, 2135-2140.
    • (1993) Hum. Mol. Genet. , vol.12 , pp. 2135-2140
    • Aoyama, T.1    Tynan, K.2    Dietz, H.C.3    Francke, U.4    Furthmayr, H.5
  • 21
    • 0029037449 scopus 로고
    • Truncated profibrillin of a Marfan patient is of apparent similar size as fibrillin: Intracellular retention leads to over-N-glycosylation
    • Raghunath, M., Kielty, C. M. & Steinmann, B. (1995) Truncated profibrillin of a Marfan patient is of apparent similar size as fibrillin: intracellular retention leads to over-N-glycosylation, J. Mol. Biol. 248, 901-909.
    • (1995) J. Mol. Biol. , vol.248 , pp. 901-909
    • Raghunath, M.1    Kielty, C.M.2    Steinmann, B.3
  • 22
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. & Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction, Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 23
    • 0024021305 scopus 로고
    • Reactivity of cytosine and thymine in single-base-pair mismatches with hydroxylamine and osmium tetroxide and its application to the study of mutations
    • Cotton, R. G., Rodrigues, N. R. & Campbell, R. D. (1988) Reactivity of cytosine and thymine in single-base-pair mismatches with hydroxylamine and osmium tetroxide and its application to the study of mutations, Proc. Natl Acad. Sci. USA 85, 4397-4401.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4397-4401
    • Cotton, R.G.1    Rodrigues, N.R.2    Campbell, R.D.3
  • 24
    • 0024605060 scopus 로고
    • Direct detection of point mutations by mismatch analysis: Application to haemophilia B
    • Montandon, A. J., Green, P. M., Giannelli, F. & Bentley, D. R. (1989) Direct detection of point mutations by mismatch analysis: application to haemophilia B, Nucleic Acids Res. 17, 3347-3358.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 3347-3358
    • Montandon, A.J.1    Green, P.M.2    Giannelli, F.3    Bentley, D.R.4
  • 25
    • 0028857166 scopus 로고
    • Bovine latent transforming growth factor beta 1-binding protein 2: Molecular cloning, identification of tissue isoforms, and immunolocalization to elastin-associated microfibrils
    • Gibson, M. A., Hatzinikolas, G., Davis, E. C., Baker, E., Sutherland, G. R. & Mecham, R. P. (1995) Bovine latent transforming growth factor beta 1-binding protein 2: molecular cloning, identification of tissue isoforms, and immunolocalization to elastin-associated microfibrils, Mol. Cell. Biol. 15, 6932-6942.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6932-6942
    • Gibson, M.A.1    Hatzinikolas, G.2    Davis, E.C.3    Baker, E.4    Sutherland, G.R.5    Mecham, R.P.6
  • 26
    • 0030696781 scopus 로고    scopus 로고
    • Immunohistochemical and ultrastructural localization of MP78/70 (βig-h3) in extracellular matrix of developing and mature bovine tissues
    • Gibson, M. A., Kumaratilake, J. S. & Clean, E. G. (1997) Immunohistochemical and ultrastructural localization of MP78/70 (βig-h3) in extracellular matrix of developing and mature bovine tissues, J. Histochem. Cytochem. 45, 1683-1696.
    • (1997) J. Histochem. Cytochem. , vol.45 , pp. 1683-1696
    • Gibson, M.A.1    Kumaratilake, J.S.2    Clean, E.G.3
  • 27
    • 0023019066 scopus 로고
    • The major antigen of elastin-associated microfibrils is a 31-kDa glycoprotein
    • Gibson, M. A., Hughes, J. L., Fanning, J. C. & Cleary, E. G. (1986) The major antigen of elastin-associated microfibrils is a 31-kDa glycoprotein, J. Biol. Chem. 261, 11429-11436.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11429-11436
    • Gibson, M.A.1    Hughes, J.L.2    Fanning, J.C.3    Cleary, E.G.4
  • 28
    • 0029845144 scopus 로고
    • Evidence that the decay of nucleus-associated nonsense mRNA for human triosephosphate isomerase involves nonsense codon recognition after splicing
    • Zhang, J. & Maquat, L. H. (1995) Evidence that the decay of nucleus-associated nonsense mRNA for human triosephosphate isomerase involves nonsense codon recognition after splicing, RNA 2, 235-243.
    • (1995) RNA , vol.2 , pp. 235-243
    • Zhang, J.1    Maquat, L.H.2
  • 29
    • 0029835707 scopus 로고    scopus 로고
    • Defects in RNA splicing and the consequence of shortened translational reading frames
    • Maquat, L. E. (1996) Defects in RNA splicing and the consequence of shortened translational reading frames, Am. J. Hum. Genet. 59, 279-286.
    • (1996) Am. J. Hum. Genet. , vol.59 , pp. 279-286
    • Maquat, L.E.1
  • 30
    • 0023651307 scopus 로고
    • RNA splice junctions of different classes of eukaryotes: Sequence statistics and functional implications in gene expression
    • Shapiro, M. B. & Senapathy, 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    Senapathy, P.2
  • 31
    • 0028895417 scopus 로고
    • Exon recognition in vertebrate splicing
    • Berget, S. M. (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
  • 32
    • 0025098474 scopus 로고
    • Exon definition may facilitate splice site selection in RNAs with multiple exons
    • Robberson, B. L., Cote, G. J. & Berget, S. M. (1990) Exon definition may facilitate splice site selection in RNAs with multiple exons, Mol. Cell. Biol. 10, 84-94.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 84-94
    • Robberson, B.L.1    Cote, G.J.2    Berget, S.M.3
  • 33
    • 0027937274 scopus 로고
    • A 5′ splice site mutation affecting the pre-mRNA splicing of two upstream exons in the collagen COL1A1 gene
    • Bateman, J. F., Chan, D., Moeller, I., Hannagan, M. & Cole, W. G. (1994) A 5′ splice site mutation affecting the pre-mRNA splicing of two upstream exons in the collagen COL1A1 gene, Biochem. J. 302, 729-735.
    • (1994) Biochem. J. , vol.302 , pp. 729-735
    • Bateman, J.F.1    Chan, D.2    Moeller, I.3    Hannagan, M.4    Cole, W.G.5
  • 34
    • 0025245371 scopus 로고
    • Effect of 5′ splice site mutations on splicing of the preceding intron
    • Talerico, M. & Berget, S. M. (1990) Effect of 5′ splice site mutations on splicing of the preceding intron, Mol. Cell. Biol. 10, 6299-6305.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6299-6305
    • Talerico, M.1    Berget, S.M.2
  • 35
    • 0023658298 scopus 로고
    • 5′ cleavage site in eukaryotic pre-mRNA splicing is determined by the overall 5′ splice region, not by the conserved 5′ GU
    • Aebi, M., Hornig, H. & Weissman, C. (1987) 5′ cleavage site in eukaryotic pre-mRNA splicing is determined by the overall 5′ splice region, not by the conserved 5′ GU, Cell 50, 237-246.
    • (1987) Cell , vol.50 , pp. 237-246
    • Aebi, M.1    Hornig, H.2    Weissman, C.3
  • 36
    • 0026316732 scopus 로고
    • Occurrence of multiple aberrantly spliced mRNAs upon a donor splice site mutation that causes familial lipoprotein lipase deficiency
    • Gotoda, T., Yamada, N., Murase, T., Inaba, T., Ishibashi, S., Shimano, H., Koga, S., Yasaki, Y. Furuichi, Y. & Takaku, F. (1991) Occurrence of multiple aberrantly spliced mRNAs upon a donor splice site mutation that causes familial lipoprotein lipase deficiency, J. Biol. Chem. 266, 24757-24762.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24757-24762
    • Gotoda, T.1    Yamada, N.2    Murase, T.3    Inaba, T.4    Ishibashi, S.5    Shimano, H.6    Koga, S.7    Yasaki, Y.8    Furuichi, Y.9    Takaku, F.10
  • 37
    • 0028136599 scopus 로고
    • Maintenance of an open reading frame as an additional level of scrutiny during splice site selection
    • Dietz, H. C. & Kendzior, R. J. (1994) Maintenance of an open reading frame as an additional level of scrutiny during splice site selection, Nat. Genet. 8, 183-188.
    • (1994) Nat. Genet. , vol.8 , pp. 183-188
    • Dietz, H.C.1    Kendzior, R.J.2
  • 38
    • 0024349521 scopus 로고
    • Nonsense mutations in the dihydrofolate reductase gene affect RNA processing
    • Urlaub, G., Mitchell, P. J., Ciudad, C. J. & Chasin, L. A. (1989) Nonsense mutations in the dihydrofolate reductase gene affect RNA processing, Mol. Cell. Biol. 9, 2868-2880.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2868-2880
    • Urlaub, G.1    Mitchell, P.J.2    Ciudad, C.J.3    Chasin, L.A.4
  • 40
    • 15844406352 scopus 로고    scopus 로고
    • Nonsense mutations inhibit RNa splicing in a cell-free system: Recognition of mutant codon is independent of protein synthesis
    • Aoufouchi, S., Yelamos, J. & Milstein, C. (1996) Nonsense mutations inhibit RNA splicing in a cell-free system: recognition of mutant codon is independent of protein synthesis, Cell 85, 415-422.
    • (1996) Cell , vol.85 , pp. 415-422
    • Aoufouchi, S.1    Yelamos, J.2    Milstein, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.