A Frequent Tyrosinase Gene Mutation in Classic, Tyrosinase-Negative (Type IA) Oculocutaneous Albinism

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 87; no. 9; pp. 3255 - 3258
• Main Authors: Giebel, Lutz B., Strunk, Kathleen M., King, Richard A., Hanifin, Jon M., Spritz, Richard A.
• Format: Journal Article
• Language: English
• Published: Washington, DC National Academy of Sciences of the United States of America 01.05.1990; National Acad Sciences
• Subjects: albinism; Albinism - enzymology; Albinism - genetics; Alleles; Amino Acid Sequence; Base Sequence; Biological and medical sciences; Catechol Oxidase - genetics; Codon - genetics; Codons; Complementary DNA; Dermatology; Exons; Female; Genes; Genetic Linkage; Genetic mutation; Haplotypes; Heterozygotes; Humans; Introns; Male; Medical sciences; Molecular Sequence Data; Monophenol Monooxygenase - deficiency; Monophenol Monooxygenase - genetics; Mutation; Oculocutaneous albinism; Oligonucleotide Probes; Pedigree; Pigmentary diseases of the skin; Polymerase Chain Reaction; Polymorphism, Restriction Fragment Length; Restriction Mapping; Human; Skin disease; Albinism; Substitution; Nucleotide sequence; Enzyme; Family study; Point mutation; Chromosome DNA; Monophenol monooxygenase; Pigmentation
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.87.9.3255

We have identified a tyrosinase gene mutation in several patients with classic, tyrosinase-negative (type IA) oculocutaneous albinism. This mutation, which results in a proline → leucine substitution at codon 81 of the tyrosinase polypeptide (EC 1.14.18.1), was observed in 20% (6 of 30) of oculocutaneous albinism alleles from independent probands, but it was not observed in any normal individuals. This mutation thus appears to be a frequent cause of tyrosinase-negative oculocutaneous albinism.