Expresión de tuftelina en gérmenes dentales humanos / Expression of tuftelin in human dental germs

La tuftelina es una proteína secretada en la matriz adamantina en desarrollo durante la formación del esmalte. Su función continúa sin esclarecerse, aunque se presume que juega un papel importante en la biomineralización de esmalte y dentina, así como en el desarrollo del órgano dental. Con el presente estudio se identificó su localización en las diferentes estructuras de gérmenes dentales de fetos humanos, conforme a los resultados se observó su expresión en el estadio pre-secretor observándose en el citoplasma de los ameloblastos, retículo estrellado, papila dental, así como en el estrato intermedio; en el secretor se identificó principalmente en la unión amelodentinaria, y en la superficie externa del esmalte, observando una marcada expresión de la proteína en la porción basal del proceso odontoblástico, pero no en la matriz extracelular de la dentina. De acuerdo a los resultados obtenidos se puede considerar que su expresión se presenta tanto en la amelogénesis, como en la odontogénesis en tejidos sin mineralizar.

The tuftelin is a secreted protein in the adamantine matrix in developing during the enamel formation. Its function continues unclarified, although it plays a role in the biomineralization of the dental organ. With the present studio the location was identified in the different structures of dental germs from human fetuses, according to the results it was observed the expression in the pre-secretor stage being observed in the cytoplasm of ameloblasts, stellate reticulum, dental papilla, also in the intermediate stratum; in the secretor it was mainly identified in the amelodentinal junction and in the outer surface of enamel, observing a marked expression of the protein in the basal portion of the odontoblastic process, but not in the extracellular matrix of the dentine. According to the results obtained it can be considered that its expression occurs in both amelogenesis and odontegenesis in unmineralized tissues.

role of smooth-ended ameloblasts in enamel protein degradation in the rat incisor pigmentation

Rats were perfused with glutaraldehyde. The lower incisors were dissected free. Mid-sagittal slice was cut through the entire incisor, deimneralized. The pigmentation zone was isolated and further sliced into cross sections. These sections were incubated for CMPase. CMPase reaction product were associated with the lateral cell memberane of subclass II and Subclass III. This localization confirm the role of extracellular space of SM as a route of enamel proteins during maturation