RESUMEN
BACKGROUND: Oral white sponge nevus (WSN) is a rare autosomal dominant benign condition, characterized by asymptomatic spongy white plaques. Mutations in Keratin 4 (KRT4) and 13 (KRT13) have been shown to cause WSN. Familial cases are uncommon due to irregular penetrance. Thus, the aim of the study was: a) to demonstrate the clinical and histopathological features of a three-generation Turkish family with oral WSN b) to determine whether KRT4 or KRT13 gene mutation was the molecular basis of WSN. MATERIAL AND METHODS: Out of twenty members of the family ten were available for assessment. Venous blood samples from six affected and five unaffected members and 48 healthy controls were obtained for genetic mutational analysis. Polymerase chain reaction was used to amplify all exons within KRT4 and KRT13 genes. These products were sequenced and the data was examined for mutations and polymorphisms. RESULTS: Varying presentation and severity of clinical features were observed. Analysis of the KRT13 gene revealed the sequence variant Y118D as the disease-causing mutation. One patient revealed several previously unreported polymorphisms including a novel mutation in exon 1 of the KRT13 gene and a heterozygous deletion in exon 1 of KRT4. This deletion in the KRT4 gene was found to be a common polymorphism reflecting a high allele frequency of 31.25% in the Turkish population. CONCLUSIONS: Oral WSN may manifest variable clinical features. The novel mutation found in the KRT13 gene is believed to add evidence for a mutational hotspot in the mucosal keratins. Molecular genetic analysis is required to establish correct diagnosis and appropriate genetic consultation.
Asunto(s)
Queratina-13/genética , Queratina-4/genética , Leucoqueratosis Mucosa Hereditaria/diagnóstico , Leucoqueratosis Mucosa Hereditaria/genética , Adolescente , Adulto , Estudios de Casos y Controles , Niño , Análisis Citogenético , Humanos , Masculino , Persona de Mediana Edad , Mutación , Linaje , Turquía , Adulto JovenRESUMEN
Xenobiotic metabolizing enzymes in the olfactory epithelium have been suggested to catalyse inactivation and facilitate elimination of odorants. We report here the molecular cloning and functional characterization of a human olfactory UDP-glucuronosyltransferase (UGT). The cloned protein is composed of 527 amino acids with an identity of 87% with a rat olfactory UGT and of 43-62% with other human UGT isoforms. Based on the sequence homology, it has been designated hUGT2A1. The gene was mapped to chromosome 4q13 by fluorescence in situ hybridization. The expression appeared to be specific for the olfactory tissue. The substrate specificity of this isoform was assessed using Chinese hamster V79 cells stably transfected with the isolated cDNA. The expressed enzyme showed a broad substrate spectrum including a range of phenolic compounds as well as aliphatic and monoterpenoid alcohols, among them many odorants. Furthermore, some steroids, especially androgens, some drugs and carcinogens were conjugated. The results support a role of the enzyme in olfactory perception and in protection of the neural system against airborne hazardous chemicals.
Asunto(s)
Glucuronosiltransferasa/genética , Bulbo Olfatorio/enzimología , Alcoholes/metabolismo , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Línea Celular , Cromosomas Humanos Par 4/genética , Clonación Molecular , Cricetinae , Cricetulus , Glucuronosiltransferasa/química , Glucuronosiltransferasa/metabolismo , Humanos , Isoenzimas/química , Isoenzimas/genética , Datos de Secuencia Molecular , Especificidad de Órganos , Fenoles/metabolismo , Filogenia , ARN Mensajero/análisis , ARN Mensajero/genética , ARN Mensajero/metabolismo , Ratas , Análisis de Secuencia de ADN , Homología de Secuencia de Aminoácido , Esteroides/metabolismo , Especificidad por Sustrato , TransfecciónRESUMEN
This study was performed to determine how preapplication of unfilled resin and subsequent saliva contamination would affect the shear strength of the etched-metal resin-bonded retainer. There was no significant difference in the shear strength of the metal-resin bond among experimental groups when the metal retainer was bonded in the routine manner, when unfilled resin was applied and allowed to polymerize before bonding of filled resin, or when saliva contamination occurred before the addition of filled resin. Preapplication of unfilled resin to etched metal retainers may serve as a means of protecting the etched metal surface for routine try-in of "Maryland bridges" before final cementation.