Molecular genetic study of autosomal dominant retinitis pigmentosa in Lithuanian patients

Human Heredity

Volumn 49, Issue 2, 1999, Pages 71-74

  Kučinskas, Vaidutis ^a   Payne, Annette M ^b   Ambrasiene, Daiva ^a   Jurgelevičius, Vaclovas ^a   Steponavičiute, Danguole ^a   Arčiuliene, Julija Vidute ^c   Daktaravičiene, Emilija ^c   Bhattacharya, Shomi ^b  

^a VILNIUS UNIVERSITY   (Lithuania)

^b UNIVERSITY COLLEGE LONDON   (United Kingdom)

^c KAUNAS UNIVERSITY OF MEDICINE   (Lithuania)

Author keywords

Autosomal dominant retinitis pigmentosa; Mutations; Peripherin gene; RDS; RHO; Rhodopsin gene

Indexed keywords

DNA; HETERODUPLEX; PERIPHERIN; RESTRICTION ENDONUCLEASE; RHODOPSIN;

AMINO ACID SUBSTITUTION; ARTICLE; AUTOSOMAL DOMINANT DISORDER; DNA POLYMORPHISM; DNA SEQUENCE; GENE MUTATION; HUMAN; HUMAN CELL; LITHUANIA; MAJOR CLINICAL STUDY; MUTATION RATE; RESTRICTION MAPPING; RETINITIS PIGMENTOSA;

EID: 0344699423     PISSN: 00015652     EISSN: None     Source Type: Journal    
DOI: 10.1159/000022847     Document Type: Article

References (17)

1. Bundey S, Crews SJ: A study of retinitis pigmentosa in the city of Birmingham. II. Clinical and genetic heterogeneity. J Med Genet 1984; 21:421-428.
2. RetNet (Retinal Information Network): The University of Texas Health Science Center, Houston. 1996-1998 (March); http://www.sph. uth.tmc.edu/RetNet/.
3. Sung C-H, Davenport CM, Hennessey JC, Maumenee IH, Jacobson SG, Heckenlively JR, Nowakowski R, Fishman G, Gouras P, Nathans J: Rhodopsin mutations in autosomal dominant retinitis pigmentosa. Proc Natl Acad Sci USA 1991;88:6481-6584.
4. Kojis TL, Heinzmann C, Flodman P, Ngo JT, Sparkes RS, Spence AA, Bateman JB, Heckenlively JR: Map refinement of locus RP13 to human chromosome 17p13.3 in a second family with autosomal dominant retinitis pigmentosa. Am J Hum Genet 1996;58:347-355.
5. Keen TJ, Inglehearn CF: Mutations and polymorphisms in the human peripherin-RDS gene and their involvement in inherited retinal degeneration. Hum Mutat 1996;8:297-303.
6. Miller SA, Dykes DD, Polesky HF: A simple salting out procedure for extracting DNA from human nucleated cells. Nucleic Acids Res 1988;16:215-218.
7. Sambrook J, Fritsch EF, Maniatis A: Molecular Cloning: A Laboratory Manual, ed 2. Cold Spring Harbor, Cold Spring Harbor Laboratory, 1989, vol 1-3.
8. White MB, Carvalho M, Derse D, O'Brien SJ, Dean M: Detecting single base substitutions as heteroduplex polymorphisms. Genomics 1992; 12:301-306.
9. Saiki RK, Gelfand DH, Stoffel S, Scharf SJ, Higuchi R, Horn GT, Mullis KB, Erlich HA: Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase. Science 1988;239:487-491.
10. Rodriguez JA, Herrera CA, Birch DG, Daiger SP: A leucine to arginine amino acid substitution at codon 46 of rhodopsin is responsible for a severe form of autosomal dominant retinitis pigmentosa. Hum Mutat 1993;2:205-213.
11. Grüning G, Millan JM, Meins M, Beneyto M, Caballero M, Apfelstedt-Sylla E, Bosch R, Zrenner E, Prieto F, Gal A: Mutations in the human peripherin/RDS gene associated with autosomal dominant retinitis pigmentosa. Hum Mutat 1994;3:321-323.
12. Glavac D, Dean M: Applications of heteroduplex analysis for mutation detection in disease genes. Hum Mutat 1995;6:281-287.
13. Dryja TP, McGee TL, Reichel E, Hahn LB, Cowley GS, Yandell DW, Sandberg MA, Berson EL: A point mutation of the rhodopsin gene in one from of retinitis pigmentosa. Nature 1990;343:364-366.
14. Berson E, Rosner B, Sandberg MA, Weigel-DiFranco C, Dryja TP: Ocular findings in patients with autosomal dominant retinitis pigmentosa and rhodopsin, proline-347-leucine. Am J Ophthalmol 1991;111:614-623.
15. Al-Maghtheh M, Gregory C, Inglehearn C, Hardcastle A, Bhattacharya S: Rhodopsin mutations in autosomal dominant retinitis pigmentosa. Hum Mutat 1993;2:249-255.
16. Franke RR, Sakmar TP, Oprian DD, Khorana HG: A single amino acid substitution in rhodopsin (Lysine 248 Leucine) prevents activation of transducin. J Biol Chem 1988;263: 2119-2122.
17. Jordan SA, Farrar GJ, Kenna P, Humphries P: Polymorphic variation within 'conserved' sequences at the 3' end of the human RDS gene which results in amino acid substitutions. Hum Mutat 1992;1:240-247.