Novel deletion spanning RCC1-like domain of RPGR in Japanese X-linked retinitis pigmentosa family

Molecular Vision

Volumn 11, Issue , 2005, Pages 535-541

  Jin, Zi Bing ^a,b   Liu, Xiao Qiang ^a,b   Uchida, Asuka ^a   Vervoort, Raf ^c   Morishita, Kazuhiro ^a   Hayakawa, Matsuko ^d   Murakami, Akira ^d   Matsumoto, Naomichi ^e   Niikawa, Norio ^e   Nao I, Nobuhisa ^a  

^a UNIVERSITY OF MIYAZAKI   (Japan)

^b WENZHOU MEDICAL UNIVERSITY   (China)

^c UNIVERSITY OF LEUVEN   (Belgium)

^d JUNTENDO UNIVERSITY   (Japan)

^e NAGASAKI UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

GENOMIC DNA; REGULATOR PROTEIN; RETINITIS PIGMENTOSA GUANOSINE TRIPHOSPHATASE REGULATOR PROTEIN; UNCLASSIFIED DRUG;

ADULT; AGED; ARTICLE; CLINICAL ARTICLE; CONTROLLED STUDY; DETERIORATION; DNA DETERMINATION; DNA EXTRACTION; DNA FLANKING REGION; EXON; FAMILY; FEMALE; GENE AMPLIFICATION; GENE DELETION; HUMAN; JAPAN; MALE; NUCLEOTIDE SEQUENCE; PATHOGENESIS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; RETINITIS PIGMENTOSA; SOUTHERN BLOTTING; TRANSLATION INITIATION; VISUAL SYSTEM EXAMINATION; X CHROMOSOME LINKED DISORDER;

ADULT; AGE OF ONSET; AGED; BLOTTING, SOUTHERN; CELL CYCLE PROTEINS; ELECTRORETINOGRAPHY; EXONS; EYE PROTEINS; FEMALE; GENE DELETION; GENETIC DISEASES, X-LINKED; GUANINE NUCLEOTIDE EXCHANGE FACTORS; HUMANS; JAPAN; MALE; MIDDLE AGED; NUCLEAR PROTEINS; PEDIGREE; POLYMERASE CHAIN REACTION; RETINITIS PIGMENTOSA; VISUAL FIELDS;

EID: 26244436676     PISSN: 10900535     EISSN: 10900535     Source Type: Journal    
DOI: None     Document Type: Article

References (28)

1. Vervoort R, Lennon A, Bird AC, Tulloch B, Axton R, Miano MG, Meindl A, Meitinger T, Ciccodicola A, Wright AF. Mutational hot spot within a new RPGR exon in X-linked retinitis pigmentosa. Nat Genet 2000; 25:462-6.
2. Breuer DK, Yashar BM, Filippova E, Hiriyanna S, Lyons RH, Mears AJ, Asaye B, Acar C, Vervoort R, Wright AF, Musarella MA, Wheeler P, MacDonald I, Iannaccone A, Birch D, Hoffman DR, Fishman GA, Heckenlively JR, Jacobson SG, Sieving PA, Swaroop A. A comprehensive mutation analysis of RP2 and RPGR in a North American cohort of families with X-linked retinitis pigmentosa. Am J Hum Genet 2002; 70:1545-54.
3. Sharon D, Sandberg MA, Rabe VW, Stillberger M, Dryja TP, Berson EL. RP2 and RPGR mutations and clinical correlations in patients with X-linked retinitis pigmentosa. Am J Hum Genet 2003; 73:1131-46.
4. Meindl A, Dry K, Herrmann K, Manson F, Ciccodicola A, Edgar A, Carvalho MR, Achatz H, Hellebrand H, Lennon A, Migliaccio C, Porter K, Zrenner E, Bird A, Jay M, Lorenz B, Wittwer B, D'Urso M, Meitinger T, Wright A. A gene (RPGR) with homology to the RCC1 guanine nucleotide exchange factor is mutated in X-linked retinitis pigmentosa (RP3). Nat Genet 1996; 13:35-42.
5. Roepman R, van Duijnhoven G, Rosenberg T, Pinckers AJ, Bleeker-Wagemakers LM, Bergen AA, Post J, Beck A, Reinhardt R, Ropers HH, Cremers FP, Berger W. Positional cloning of the gene for X-linked retinitis pigmentosa 3: homology with the guanine-nucleotide-exchange factor RCC1. Hum Mol Genet 1996; 5:1035-41.
6. Gorlich D, Mattaj IW. Nucleocytoplasmic transport. Science 1996; 271:1513-8.
7. Linari M, Ueffing M, Manson F, Wright A, Meitinger T, Becker J. The retinitis pigmentosa GTPase regulator, RPGR, interacts with the delta subunit of rod cyclic GMP phosphodiesterase. Proc Natl Acad Sci U S A 1999; 96:1315-20.
8. Boylan JP, Wright AF. Identification of a novel protein interacting with RPGR. Hum Mol Genet 2000; 9:2085-93.
9. Dryja TP, Adams SM, Grimsby JL, McGee TL, Hong DH, Li T, Andreasson S, Berson EL. Null RPGRIP1 alleles in patients with Leber congenital amaurosis. Am J Hum Genet 2001; 68:1295-8.
10. Mutsuko H, Keiko F, Akira N. A family exhibiting X-linked retinitis pigmentosa. Folia Ophthalmologica Japonica 1985; 36:1087-92.
11. Kirschner R, Rosenberg T, Schultz-Heienbrok R, Lenzner S, Feil S, Roepman R, Cremers FP, Ropers HH, Berger W. RPGR transcription studies in mouse and human tissues reveal a retina-specific isoform that is disrupted in a patient with X-linked retinitis pigmentosa. Hum Mol Genet 1999; 8:1571-8.
12. Bader I, Brandau O, Achatz H, Apfelstedt-Sylla E, Hergersberg M, Lorenz B, Wissinger B, Wittwer B, Rudolph G, Meindl A, Meitinger T. X-linked retinitis pigmentosa: RPGR mutations in most families with definite X linkage and clustering of mutations in a short sequence stretch of exon ORF15. Invest Ophthalmol Vis Sci 2003; 44:1458-63.
13. Yan D, Swain PK, Breuer D, Tucker RM, Wu W, Fujita R, Rehemtulla A, Burke D, Swaroop A. Biochemical characterization and subcellular localization of the mouse retinitis pigmentosa GTPase regulator (mRpgr). J Biol Chem 1998; 273:19656-63.
14. Kirschner R, Erturk D, Zeitz C, Sahin S, Ramser J, Cremers FP, Ropers HH, Berger W. DNA sequence comparison of human and mouse retinitis pigmentosa GTPase regulator (RPGR) identifies tissue-specific exons and putative regulatory elements. Hum Genet 2001; 109:271-8.
15. Hong DH, Li T. Complex expression pattern of RPGR reveals a role for purine-rich exonic splicing enhancers. Invest Ophthalmol Vis Sci 2002; 43:3373-82.
16. Gillespie PG, Prusti RK, Apel ED, Beavo JA. A soluble form of bovine rod photoreceptor phosphodiesterase has a novel 15-kDa subunit. J Biol Chem 1989; 264:12187-93.
17. Roepman R, Bernoud-Hubac N, Schick DE, Maugeri A, Berger W, Ropers HH, Cremers FP, Ferreira PA. The retinitis pigmentosa GTPase regulator (RPGR) interacts with novel transport-like proteins in the outer segments of rod photoreceptors. Hum Mol Genet 2000; 9:2095-105.
18. Hong DH, Yue G, Adamian M, Li T. Retinitis pigmentosa GTPase regulator (RPGRr)-interacting protein is stably associated with the photoreceptor ciliary axoneme and anchors RPGR to the connecting cilium. J Biol Chem 2001; 276:12091-9.
19. Gerber S, Perrault I, Hanein S, Barbet F, Ducroq D, Ghazi I, Martin-Coignard D, Leowski C, Homfray T, Dufier JL, Munnich A, Kaplan J, Rozet JM. Complete exon-intron structure of the RPGR-interacting protein (RPGRIP1) gene allows the identification of mutations underlying Leber congenital amaurosis. Eur J Hum Genet 2001; 9:561-71.
20. Antonarakis SE. Recommendations for a nomenclature system for human gene mutations. Nomenclature Working Group. Hum Mutat 1998; 11:1-3.
21. den Dunnen JT, Paalman MH. Standardizing mutation nomenclature: why bother? Hum Mutat 2003; 22:181-2.
22. den Dunnen JT, Antonarakis SE. Mutation nomenclature extensions and suggestions to describe complex mutations: a discussion. Hum Mutat 2000; 15:7-12. Erratum in: Hum Mutat 2002; 20:403.
23. den Dunnen JT, Antonarakis SE. Nomenclature for the description of human sequence variations. Hum Genet 2001; 109:121-4.
24. Carter PE, Duponchel C, Tosi M, Fothergill JE. Complete nucleotide sequence of the gene for human C1 inhibitor with an unusually high density of Alu elements. Eur J Biochem 1991; 197:301-8.
25. Maltais LJ, Blake JA, Chu T, Lutz CM, Eppig JT, Jackson I. Rules and guidelines for mouse gene, allele, and mutation nomenclature: a condensed version. Genomics 2002; 79:471-4.
26. Beutler E, McKusick VA, Motulsky AG, Scriver CR, Hutchinson F. Mutation nomenclature: nicknames, systematic names, and unique identifiers. Hum Mutat 1996; 8:203-6.
27. Update on nomenclature for human gene mutations. Ad Hoc Committee on Mutation Nomenclature. Hum Mutat 1996; 8:197-202.
28. Antonarakis SE, McKusick VA. Discussion on mutation nomenclature. Hum Mutat 1994; 4:166.