Skip to main content
PMC home page
Journal of Medical Genetics logoLink to Journal of Medical Genetics
. 1991 Jul;28(7):464–467. doi: 10.1136/jmg.28.7.464

A nonsense mutation in the tyrosinase gene of Afghan patients with tyrosinase negative (type IA) oculocutaneous albinism.

L B Giebel 1, M A Musarella 1, R A Spritz 1
PMCID: PMC1016956  PMID: 1832718

Abstract

We detected a nonsense mutation in the tyrosinase gene of two Afghan sibs with classical tyrosinase negative (type IA) oculocutaneous albinism. The mutation, a single base substitution at codon 178, creates an amber termination codon that truncates the 529 amino acid tyrosinase polypeptide at this position. The patients' parents are first cousins, and the patients are therefore homoallelic for this mutation.

Full text

PDF
464

Images in this article

466Image
on p.466
466Image
on p.466

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Barton D. E., Kwon B. S., Francke U. Human tyrosinase gene, mapped to chromosome 11 (q14----q21), defines second region of homology with mouse chromosome 7. Genomics. 1988 Jul;3(1):17–24. doi: 10.1016/0888-7543(88)90153-x. [DOI] [PubMed] [Google Scholar]
  2. Bouchard B., Fuller B. B., Vijayasaradhi S., Houghton A. N. Induction of pigmentation in mouse fibroblasts by expression of human tyrosinase cDNA. J Exp Med. 1989 Jun 1;169(6):2029–2042. doi: 10.1084/jem.169.6.2029. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Giebel L. B., Spritz R. A. RFLP for MboI in the human tyrosinase (TYR) gene detected by PCR. Nucleic Acids Res. 1990 May 25;18(10):3103–3103. doi: 10.1093/nar/18.10.3103-a. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Giebel L. B., Strunk K. M., King R. A., Hanifin J. M., Spritz R. A. A frequent tyrosinase gene mutation in classic, tyrosinase-negative (type IA) oculocutaneous albinism. Proc Natl Acad Sci U S A. 1990 May;87(9):3255–3258. doi: 10.1073/pnas.87.9.3255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Giebel L. B., Strunk K. M., Spritz R. A. Organization and nucleotide sequences of the human tyrosinase gene and a truncated tyrosinase-related segment. Genomics. 1991 Mar;9(3):435–445. doi: 10.1016/0888-7543(91)90409-8. [DOI] [PubMed] [Google Scholar]
  6. Kikuchi H., Hara S., Ishiguro S., Tamai M., Watanabe M. Detection of point mutation in the tyrosinase gene of a Japanese albino patient by a direct sequencing of amplified DNA. Hum Genet. 1990 Jun;85(1):123–124. doi: 10.1007/BF00276337. [DOI] [PubMed] [Google Scholar]
  7. Kikuchi H., Miura H., Yamamoto H., Takeuchi T., Dei T., Watanabe M. Characteristic sequences in the upstream region of the human tyrosinase gene. Biochim Biophys Acta. 1989 Dec 22;1009(3):283–286. doi: 10.1016/0167-4781(89)90115-2. [DOI] [PubMed] [Google Scholar]
  8. King R. A., Summers C. G. Albinism. Dermatol Clin. 1988 Apr;6(2):217–228. [PubMed] [Google Scholar]
  9. Kwon B. S., Haq A. K., Pomerantz S. H., Halaban R. Isolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus. Proc Natl Acad Sci U S A. 1987 Nov;84(21):7473–7477. doi: 10.1073/pnas.84.21.7473. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Saiki R. K., Gelfand D. H., Stoffel S., Scharf S. J., Higuchi R., Horn G. T., Mullis K. B., Erlich H. A. Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase. Science. 1988 Jan 29;239(4839):487–491. doi: 10.1126/science.2448875. [DOI] [PubMed] [Google Scholar]
  11. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Shibahara S., Tomita Y., Tagami H., Müller R. M., Cohen T. Molecular basis for the heterogeneity of human tyrosinase. Tohoku J Exp Med. 1988 Dec;156(4):403–414. doi: 10.1620/tjem.156.403. [DOI] [PubMed] [Google Scholar]
  13. Spritz R. A., Strunk K. M., Giebel L. B., King R. A. Detection of mutations in the tyrosinase gene in a patient with type IA oculocutaneous albinism. N Engl J Med. 1990 Jun 14;322(24):1724–1728. doi: 10.1056/NEJM199006143222407. [DOI] [PubMed] [Google Scholar]
  14. Spritz R. A., Strunk K. M., Hsieh C. L., Sekhon G. S., Francke U. Homozygous tyrosinase gene mutation in an American black with tyrosinase-negative (type IA) oculocutaneous albinism. Am J Hum Genet. 1991 Feb;48(2):318–324. [PMC free article] [PubMed] [Google Scholar]
  15. Tomita Y., Takeda A., Okinaga S., Tagami H., Shibahara S. Human oculocutaneous albinism caused by single base insertion in the tyrosinase gene. Biochem Biophys Res Commun. 1989 Nov 15;164(3):990–996. doi: 10.1016/0006-291x(89)91767-1. [DOI] [PubMed] [Google Scholar]
  16. Wittbjer A., Dahlbäck B., Odh G., Rosengren A. M., Rosengren E., Rorsman H. Isolation of human tyrosinase from cultured melanoma cells. Acta Derm Venereol. 1989;69(2):125–131. [PubMed] [Google Scholar]

Articles from Journal of Medical Genetics are provided here courtesy of BMJ Publishing Group

RESOURCES