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BioMed Research International
Volume 2013 (2013), Article ID 517570, 15 pages
Novel GUCA1A Mutations Suggesting Possible Mechanisms of Pathogenesis in Cone, Cone-Rod, and Macular Dystrophy Patients
1Department of Cellular Therapy and Regenerative Medicine, Andalusian Centre for Molecular Biology and Regenerative Medicine (CABIMER), ‘Isla Cartuja’, 41092 Seville, Spain
2Department of Genetics, IIS-Jiménez Díaz Foundation, 28040 Madrid, Spain
3Centre for Biomedical Network Research on Rare Diseases (CIBERER), ISCIII, 46010 Valencia, Spain
4Department of Ophthalmology, Hospital ‘Fundación Jiménez Díaz’, 28040 Madrid, Spain
5Department of Genetics, UCL-Institute of Ophthalmology, 11-43 Bath Street, London EC1V 9EL, UK
Received 18 April 2013; Accepted 19 June 2013
Academic Editor: Claudia Gragnoli
Copyright © 2013 Kunka Kamenarova et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- C. P. Hamel, “Cone rod dystrophies,” Orphanet Journal of Rare Diseases, vol. 2, no. 1, article 7, 2007.
- M. Michaelides, A. J. Hardcastle, D. M. Hunt, and A. T. Moore, “Progressive cone and cone-rod dystrophies: phenotypes and underlying molecular genetic basis,” Survey of Ophthalmology, vol. 51, no. 3, pp. 232–258, 2006.
- S. M. Downes, A. M. Payne, R. E. Kelsell et al., “Autosomal dominant cone-rod dystrophy with mutations in the guanylate cyclase 2D gene encoding retinal guanylate cyclase-1,” Archives of Ophthalmology, vol. 119, no. 11, pp. 1667–1673, 2001.
- V. B. D. Kitiratschky, P. Behnen, U. Kellner et al., “Mutations in the GUCA1A gene involved in hereditary cone dystrophies impair calcium-mediated regulation of guanylate cyclase,” Human Mutation, vol. 30, no. 8, pp. E782–E796, 2009.
- M. Michaelides, S. E. Wilkie, S. Jenkins et al., “Mutation in the gene GUCA1A, encoding guanylate cyclase-activating protein 1, causes cone, cone-rod, and macular dystrophy,” Ophthalmology, vol. 112, no. 8, pp. 1442–1447, 2005.
- A. M. Payne, S. M. Downes, D. A. R. Bessant et al., “A mutation in guanylate cyclase activator 1A(GUCA1A) in an autosomal dominant cone dystrophy pedigree mapping to a new locus on chromosome 6p21.1,” Human Molecular Genetics, vol. 7, no. 2, pp. 273–277, 1998.
- L. Jiang, D. Wheaton, G. Bereta et al., “A novel GCAP1(N104K) mutation in EF-hand 3 (EF3) linked to autosomal dominant cone dystrophy,” Vision Research, vol. 48, no. 23-24, pp. 2425–2432, 2008.
- K. M. Nishiguchi, I. Sokal, L. Yang et al., “A novel mutation (I143NT) in guanylate cyclase-activating protein 1 (GCAP1) associated with autosomal dominant cone degeneration,” Investigative Ophthalmology and Visual Science, vol. 45, no. 11, pp. 3863–3870, 2004.
- L. Jiang, B. J. Katz, Z. Yang et al., “Autosomal dominant cone dystrophy caused by a novel mutation in the GCAP1 gene (GUCA1A),” Molecular Vision, vol. 11, pp. 143–151, 2005.
- I. Sokal, W. J. Dupps, M. A. Grassi et al., “A novel GCAP1 missense mutation (L151F) in a large family with autosomal dominant cone-rod dystrophy (adCORD),” Investigative Ophthalmology and Visual Science, vol. 46, no. 4, pp. 1124–1132, 2005.
- S. E. Wilkie, Y. Li, E. C. Deery et al., “Identification and functional consequences of a new mutation (E155G) in the gene for GCAP1 that causes autosomal dominant cone dystrophy,” American Journal of Human Genetics, vol. 69, no. 3, pp. 471–480, 2001.
- N. Cuenca, S. Lopez, K. Howes, and H. Kolb, “The localization of guanylyl cylase-activating proteins in the mammalian retina,” Investigative Ophthalmology and Visual Science, vol. 39, no. 7, pp. 1243–1250, 1998.
- J. J. Falke, S. K. Drake, A. L. Hazard, and O. B. Peersen, “Molecular tuning of ion binding to calcium signaling proteins,” Quarterly Reviews of Biophysics, vol. 27, no. 3, pp. 219–290, 1994.
- K. Palczewski, I. Sokal, and W. Baehr, “Guanylate cyclase-activating proteins: structure, function, and diversity,” Biochemical and Biophysical Research Communications, vol. 322, no. 4, pp. 1123–1130, 2004.
- L. Cartegni, S. L. Chew, and A. R. Krainer, “Listening to silence and understanding nonsense: exonic mutations that affect splicing,” Nature Reviews Genetics, vol. 3, no. 4, pp. 285–298, 2002.
- I. C. Eperon, O. V. Makarova, A. Mayeda et al., “Selection of alternative 5' splice sites: role of U1 snRNP and models for the antagonistic effects of SF2/ASF and hnRNP A1,” Molecular and Cellular Biology, vol. 20, no. 22, pp. 8303–8318, 2000.
- M. Krawczak, N. S. T. Thomas, B. Hundrieser et al., “Single base-pair substitutions in exon-intron junctions of human genes: nature, distribution, and consequences for mRNA splicing,” Human Mutation, vol. 28, no. 2, pp. 150–158, 2007.
- F. Pagani and F. E. Baralle, “Genomic variants in exons and introns: identifying the splicing spoilers,” Nature Reviews Genetics, vol. 5, no. 5, pp. 389–396, 2004.
- S. M. Downes, G. E. Holder, F. W. Fitzke et al., “Autosomal dominant cone and cone-rod dystrophy with mutations in the guanylate cyclase activator 1A gene-encoding guanylate cyclase activating protein-1,” Archives of Ophthalmology, vol. 119, no. 1, pp. 96–105, 2001.
- S. A. Miller, D. D. Dykes, and H. F. Polesky, “A simple salting out procedure for extracting DNA from human nucleated cells,” Nucleic Acids Research, vol. 16, no. 3, p. 1215, 1988.
- K. Hoffmann and T. H. Lindner, “easyLINKAGE-Plus—automated linkage analyses using large-scale SNP data,” Bioinformatics, vol. 21, no. 17, pp. 3565–3567, 2005.
- G. R. Abecasis, S. S. Cherny, W. O. Cookson, and L. R. Cardon, “Merlin—rapid analysis of dense genetic maps using sparse gene flow trees,” Nature Genetics, vol. 30, no. 1, pp. 97–101, 2002.
- I. A. Adzhubei, S. Schmidt, L. Peshkin et al., “A method and server for predicting damaging missense mutations,” Nature Methods, vol. 7, no. 4, pp. 248–249, 2010.
- E. Faraggi, T. Zhang, Y. Yang, L. Kurgan, and Y. Zhou, “SPINE X: improving protein secondary structure prediction by multistep learning coupled with prediction of solvent accessible surface area and backbone torsion angles,” Journal of Computational Chemistry, vol. 33, no. 3, pp. 259–267, 2012.
- L. J. McGuffin, K. Bryson, and D. T. Jones, “The PSIPRED protein structure prediction server,” Bioinformatics, vol. 16, no. 4, pp. 404–405, 2000.
- F. Desmet, D. Hamroun, M. Lalande, G. Collod-Bëroud, M. Claustres, and C. Béroud, “Human Splicing Finder: an online bioinformatics tool to predict splicing signals,” Nucleic Acids Research, vol. 37, no. 9, article e67, 2009.
- L. Cartegni, J. Wang, Z. Zhu, M. Q. Zhang, and A. R. Krainer, “ESEfinder: a web resource to identify exonic splicing enhancers,” Nucleic Acids Research, vol. 31, no. 13, pp. 3568–3571, 2003.
- S. Stamm, J. Riethoven, V. Le Texier et al., “ASD: a bioinformatics resource on alternative splicing.,” Nucleic Acids Research, vol. 34, pp. D46–D55, 2006.
- A. Goren, O. Ram, M. Amit et al., “Comparative analysis identifies exonic splicing regulatory sequences-the complex definition of enhancers and silencers,” Molecular Cell, vol. 22, no. 6, pp. 769–781, 2006.
- W. G. Fairbrother, G. W. Yeo, R. Yeh et al., “RESCUE-ESE identifies candidate exonic splicing enhancers in vertebrate exons,” Nucleic Acids Research, vol. 32, pp. W187–W190, 2004.
- Z. Wang, M. E. Rolish, G. Yeo, V. Tung, M. Mawson, and C. B. Burge, “Systematic identification and analysis of exonic splicing silencers,” Cell, vol. 119, no. 6, pp. 831–845, 2004.
- X. H.-F. Zhang, T. Kangsamaksin, M. S. P. Chao, J. K. Banerjee, and L. A. Chasin, “Exon inclusion is dependent on predictable exonic splicing enhancers,” Molecular and Cellular Biology, vol. 25, no. 16, pp. 7323–7332, 2005.
- W. Humphrey, A. Dalke, and K. Schulten, “VMD: visual molecular dynamics,” Journal of Molecular Graphics, vol. 14, no. 1, pp. 33–38, 1996.
- J. J. C. Van Lith-Verhoeven, C. B. Hoyng, B. Van Den Helm et al., “The benign concentric annular macular dystrophy locus maps to 6p12.3-q16,” Investigative Ophthalmology and Visual Science, vol. 45, no. 1, pp. 30–35, 2004.
- K. Zhang, M. Kniazeva, M. Han et al., “A 5-bp deletion in ELOVL4 is associated with two related forms of autosomal dominant macular dystrophy,” Nature Genetics, vol. 27, no. 1, pp. 89–93, 2001.
- M. Nakazawa, E. Kikawa, Y. Chida, and M. Tamai, “Asn244His mutation of the peripherin/RDS gene causing autosomal dominant cone-rod degeneration,” Human Molecular Genetics, vol. 3, no. 7, pp. 1195–1196, 1994.
- S. Johnson, S. Halford, A. G. Morris et al., “Genomic organisation and alternative splicing of human RIM1, a gene implicated in autosomal dominant cone-rod dystrophy (CORD7),” Genomics, vol. 81, no. 3, pp. 304–314, 2003.
- A. M. Dizhoor, S. G. Boikov, and E. V. Olshevskaya, “Constitutive activation of photoreceptor guanylate cyclase by Y99C mutant of GCAP-1. Possible role in causing human autosomal dominant cone degeneration,” The Journal of Biological Chemistry, vol. 273, no. 28, pp. 17311–17314, 1998.
- E. V. Olshevskaya, P. D. Calvert, M. L. Woodruff et al., “The Y99C mutation in guanylyl cyclase-activating protein 1 increases intracellular Ca2+ and causes photoreceptor degeneration in transgenic mice,” Journal of Neuroscience, vol. 24, no. 27, pp. 6078–6085, 2004.
- J. Zhu, A. Mayeda, and A. R. Krainer, “Exon identity established through differential antagonism between exonic splicing silencer-bound hnRNP A1 and enhancer-bound SR proteins,” Molecular Cell, vol. 8, no. 6, pp. 1351–1361, 2001.
- Y. Yu, P. A. Maroney, J. A. Denker et al., “Dynamic regulation of alternative splicing by silencers that modulate 5' splice site competition,” Cell, vol. 135, no. 7, pp. 1224–1236, 2008.
- T. Sterne-Weiler, J. Howard, M. Mort, D. N. Cooper, and J. R. Sanford, “Loss of exon identity is a common mechanism of human inherited disease,” Genome Research, vol. 21, no. 10, pp. 1563–1571, 2011.
- J. R. Sanford, X. Wang, M. Mort et al., “Splicing factor SFRS1 recognizes a functionally diverse landscape of RNA transcripts,” Genome Research, vol. 19, no. 3, pp. 381–394, 2009.
- C. L. Lorson, E. Hahnen, E. J. Androphy, and B. Wirth, “A single nucleotide in the SMN gene regulates splicing and is responsible for spinal muscular atrophy,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 11, pp. 6307–6311, 1999.
- S. McVety, L. Li, P. H. Gordon, G. Chong, and W. D. Foulkes, “Disruption of an exon splicing enhancer in exon 3 of MLH1 is the cause of HNPCC in a Quebec family,” Journal of Medical Genetics, vol. 43, no. 2, pp. 153–156, 2006.
- K. B. Nielsen, S. Sørensen, L. Cartegni et al., “Seemingly neutral polymorphic variants may confer immunity to splicing-inactivating mutations: a synonymous SNP in exon 5 of MCAD protects from deleterious mutations in a flanking exonic splicing enhancer,” American Journal of Human Genetics, vol. 80, no. 3, pp. 416–432, 2007.
- F. Pagani, C. Stuani, M. Tzetis et al., “New type of disease causing mutations: the example of the composite exonic regulatory elements of splicing in CFTR exon 12,” Human Molecular Genetics, vol. 12, no. 10, pp. 1111–1120, 2003.
- T. Koed Doktor, L. D. Schroeder, A. Vested et al., “SMN2 exon 7 splicing is inhibited by binding of hnRNP A1 to a common ESS motif that spans the 3' splice site,” Human Mutation, vol. 32, no. 2, pp. 220–230, 2011.
- E. Buratti, M. Baralle, and F. E. Baralle, “Defective splicing, disease and therapy: searching for master checkpoints in exon definition.,” Nucleic Acids Research, vol. 34, no. 12, pp. 3494–3510, 2006.
- R. L. Davis, V. M. Homer, P. M. George, and S. O. Brennan, “A deep intronic mutation in FGB creates a consensus exonic splicing enhancer motif that results in afibrinogenemia caused by aberrant mRNA splicing, which can be corrected in vitro with antisense oligonucleotide treatment,” Human Mutation, vol. 30, no. 2, pp. 221–227, 2009.
- K. Homolova, P. Zavadakova, T. K. Doktor, L. D. Schroeder, V. Kozich, and B. S. Andresen, “The deep intronic c.903+469T > C mutation in the MTRR gene creates an SF2/ASF binding exonic splicing enhancer, which leads to pseudoexon activation and causes the cblE type of homocystinuria,” Human Mutation, vol. 31, no. 4, pp. 437–444, 2010.