ABSTRACT
RESUMEN: Los instrumentos rotatorios utilizados en el tratamiento de conductos dentales necesitan cumplir con ciertas características físicas que le confieran un uso correcto, adecuado y seguro para su uso clínico. En el mercado comercial existen una serie de instrumentos importados que dejan en duda la autenticidad de estos debido a sus bajos costos. En este estudio evaluamos física, química y morfológicamente dos kits de instrumentos rotatorios Protaper universal (Dentsply) mediante análisis de MEB, EDX, microdureza y EDS. Uno de los kits (grupo 1) se adquirió directamente de la casa comercial y otro kit importado que a simple vista no parecía cumplir con los estándares de calidad de un correcto empaquetado (grupo 2). En el análisis de MEB se observaron características morfológicas muy diferentes entre ambos kits, el grupo 2 presentó diversas irregularidades en la superficie de las limas, sin embargo, en el EDS no se encontró diferencia alguna. En cuanto al análisis de microdureza se observó una estadística estadísticamente significativa y en el EDS se observaron mayores picos de intensidad en cuanto a la aleación de Ni-Ti en el grupo 2. Estos resultados sugieren que existen instrumentos rotatorios importados que a pesar de su bajo costo pueden presentar ciertas características muy similares a los kits auténticos, sin embargo, física y químicamente pueden resultar en un riesgo para su uso clínico debido a la diferencia entre estos.
ABSTRACT: Rotatory files are instruments used in the treatment of dental canals roots. These instruments need to comply with certain physical characteristics for a correct, adequate and safe use for clinical use. In the commercial market there are a series of imported instruments that cast doubt on their authenticity due to their low costs. In this study we physically, chemically and morphologically evaluated two Protaper universal rotary instrument kits (Dentsply) using SEM, EDX, microhardness and EDS analysis. One of the kits (group 1) was purchased directly from the commercial house and another imported kit that a simple view did not seem to meet the quality standards of a correct packaging (group 2). In the SEM analysis, very different morphological characteristics were observed between both kits, group 2 presented various irregularities on the surface of the files, however, no difference was found in the EDS. Regarding the microhardness analysis, a statistically significant statistic was observed and in the EDS, higher intensity peaks were observed in terms of the Ni-Ti alloy in group 2. These results suggest that there are imported rotary instruments that despite their low cost can present characteristics very similar to authentic kits, however, physically and chemically they can result in a risk for their clinical use due to the difference between them.
ABSTRACT
BACKGROUND: The olfactomedin-like domain (OLFML) is present in at least four families of proteins, including OLFML2A and OLFML2B, which are expressed in adult rat retina cells. However, no expression of their orthologous has ever been reported in human and baboon. OBJECTIVE: The aim of this study was to investigate the expression of OLFML2A and OLFML2B in ocular tissues of baboons (Papio hamadryas) and humans, as a key to elucidate OLFML function in eye physiology. METHODS: OLFML2A and OLFML2B cDNA detection in ocular tissues of these species was performed by RT-PCR. The amplicons were cloned and sequenced, phylogenetically analyzed and their proteins products were confirmed by immunofluorescence assays. RESULTS: OLFML2A and OLFML2B transcripts were found in human cornea, lens and retina and in baboon cornea, lens, iris and retina. The baboon OLFML2A and OLFML2B ORF sequences have 96% similarity with their human's orthologous. OLFML2A and OLFML2B evolution fits the hypothesis of purifying selection. Phylogenetic analysis shows clear orthology in OLFML2A genes, while OLFML2B orthology is not clear. CONCLUSIONS: Expression of OLFML2A and OLFML2B in human and baboon ocular tissues, including their high similarity, make the baboon a powerful model to deduce the physiological and/or metabolic function of these proteins in the eye.