RESUMEN
OBJECTIVE: The study was performed to analyze the oropharynx airway and examine the influence of age and gender on the oropharynx volume configuration using cone beam computed tomography. MATERIALS AND METHODS: This study examined the cone beam computed tomographic images of 51 patients 25 male and 26 females, group matched for age and gender. The oropharynx airway volume and area between the posterior nasal spine and top of the epiglottis were measured and compared. RESULTS: The statistical measurements of 51 cone beam computed tomography images showed a nonsignificant difference found between male and female regarding the age (the mean age for female 40.15 y. and for male32.72 y). Male subjects had greater oropharynx volume, a high significant difference ( P =0.005) in oropharynx volume between the 3 age groups. A significant difference was found between the smallest age group with the larger age groups. CONCLUSION: The study data revealed that the changes in measurements of oropharynx airway are age-dependent in addition to gender effect.
Asunto(s)
Tomografía Computarizada de Haz Cónico Espiral , Humanos , Masculino , Femenino , Imagenología Tridimensional/métodos , Orofaringe/diagnóstico por imagen , Tomografía Computarizada de Haz Cónico/métodos , Epiglotis , Cefalometría/métodos , FaringeRESUMEN
The purpose of the present work was to identify the catalytic activity of AGXT2L1 and AGXT2L2, two closely related, putative pyridoxal-phosphate-dependent enzymes encoded by vertebrate genomes. The existence of bacterial homologues (40-50% identity with AGXT2L1 and AGXT2L2) forming bi- or tri-functional proteins with a putative kinase belonging to the family of aminoglycoside phosphotransferases suggested that AGXT2L1 and AGXT2L2 acted on phosphorylated and aminated compounds. Vertebrate genomes were found to encode a homologue (AGPHD1) of these putative bacterial kinases, which was therefore likely to phosphorylate an amino compound bearing a hydroxyl group. These and other considerations led us to hypothesize that AGPHD1 corresponded to 5-hydroxy-L-lysine kinase and that AGXT2L1 and AGXT2L2 catalyzed the pyridoxal-phosphate-dependent breakdown of phosphoethanolamine and 5-phosphohydroxy-L-lysine. The three recombinant human proteins were produced and purified to homogeneity. AGPHD1 was indeed found to catalyze the GTP-dependent phosphorylation of 5-hydroxy-L-lysine. The phosphorylation product made by this enzyme was metabolized by AGXT2L2, which converted it to ammonia, inorganic phosphate, and 2-aminoadipate semialdehyde. AGXT2L1 catalyzed a similar reaction on phosphoethanolamine, converting it to ammonia, inorganic phosphate, and acetaldehyde. AGPHD1 and AGXT2L2 are likely to be the mutated enzymes in 5-hydroxylysinuria and 5-phosphohydroxylysinuria, respectively. The high level of expression of AGXT2L1 in human brain, as well as data in the literature linking AGXT2L1 to schizophrenia and bipolar disorders, suggest that these diseases may involve a perturbation of brain phosphoethanolamine metabolism. AGXT2L1 and AGXT2L2, the first ammoniophospholyases to be identified, belong to a family of aminotransferases acting on ω-amines.