16 research outputs found
Estudio de la actividad comparativa in vitro de telitromicina en patógenos respiratorios adquiridos en la comunidad en 13 centros clÃnicos chilenos
Evaluación pre-analÃtica de dos métodos de extracción de ADN para la amplificación del gen de la pneumolisina (PLY) de Streptococcus pneumoniae, en muestras de hemocultivo
Actividad comparativa in vitro de cefpodoxima en relación a otros antibióticos de uso frecuente, frente a patógenos respiratorios, urinarios y de infecciones de partes blandas
Colonización bacteriana de piel sana versus quemada de niños bajo 15 años tratados en COANIQUEM, Santiago de Chile
Septicemia fatal causada por Vibrio cholerae no-O1, no-O139 hemolÃtico en Chile: Caso clÃnico
Gastroenteritis aguda causada por Vibrio cholerae no-O1, no-O139 que porta una región homologa a la isla de patogenicidad VpaI-7
Detección de los genes de las exotoxinas pirogénicas SpeA, SpeB y SpeC en cepas chilenas de Streptococcus pyogenes y su asociación con la clÃnica
EpidemiologÃa molecular de un brote de infecciones por Streptococcus pyogenes en una unidad de quemados
Activation of Casein Kinase II and Inhibition of Phosphatase and Tensin Homologue Deleted on Chromosome 10 Phosphatase by Nerve Growth Factor/p75(NTR) Inhibit Glycogen Synthase Kinase-3β and Stimulate Axonal Growth
Axonal elongation and guidance are controlled by extracellular factors such as the neurotrophins. Indeed, nerve growth factor (NGF) seems to promote axon growth through binding to its p75(NTR) receptor and inactivating RhoA. Furthermore, the local inhibition of glycogen synthase kinase (GSK)-3β by NGF also favors microtubule polymerization and axon extension. Inactivation of GSK-3β may be due to the NGF/TrkA-mediated activation of phosphatidylinositol-3 kinase (PI-3 kinase), which increases the levels of phosphatydilinositol 3-phosphate [PI(3)P]. However, we show here that NGF may inactivate GSK-3β through an alternative mechanism. In cultured hippocampal neurons, the capacity of NGF to promote axon elongation is mostly mediated by p75(NTR), and the activation of this pathway leads to the inactivation of GSK-3β. However, the signaling pathway triggered by NGF/p75(NTR) acts through casein kinase II (CK2). NGF/p75(NTR)-activated CK2 phosphorylates the phosphatase and tensin homologue deleted on chromosome 10 (PTEN), thus rendering this phosphatase inactive. Like activation of the PI-3 kinase, PTEN inactivation allows PI(3)P levels to increase, thus favoring GSK-3β inactivation and axon outgrowth. This newly disclosed mechanism may help to extend the repertoire of pharmacological agents that activate CK2 or that inhibit PTEN to stimulate axon regeneration after trauma or disease