Significant morphological and functional alterations of synapses have been described in EAE. Also, it has been shown that antibodies and T cells against the encephalitogenic myelin basic protein (MBP) immunocrossreacts with Synapsin I (Syn), a neuron-specific protein located mainly in the presynaptic terminals. Syn phosphorylation controls its association to synaptic vesicles and actin filaments, playing an important role in the regulation of neurotransmitter release. In this work we study the state of phosphorylation of Syn during the development of EAE induced in Wistar rats. The synaptosomal fractions (P2) were purified from brain, cerebellum and spinal cord of EAE and control animals, and subsequent quantification of total Syn and phosphorylated Syn at Site 1 (phosphoSer9) was done by immunoblot analysis. We found that in the acute and recovery stages of EAE the amount of total Syn was similar in all the tissue samples. However, phosphorylation of Syn was significantly diminished (~40%) in the lumbosacral spinal cords in the acute period but it was restored to normal values after the recovery period. These observations suggest that an alteration on the mechanism of neurotransmitter release could be involved in the development of the clinical signs of EAE.
Significant morphological and functional alterations of synapses have been described in EAE. Also, it has been shown that antibodies and T cells against the encephalitogenic myelin basic protein (MBP) immunocrossreacts with Synapsin I (Syn), a neuron-specific protein located mainly in the presynaptic terminals. Syn phosphorylation controls its association to synaptic vesicles and actin filaments, playing an important role in the regulation of neurotransmitter release. In this work we study the state of phosphorylation of Syn during the development of EAE induced in Wistar rats. The synaptosomal fractions (P2) were purified from brain, cerebellum and spinal cord of EAE and control animals, and subsequent quantification of total Syn and phosphorylated Syn at Site 1 (phosphoSer9) was done by immunoblot analysis. We found that in the acute and recovery stages of EAE the amount of total Syn was similar in all the tissue samples. However, phosphorylation of Syn was significantly diminished (~40%) in the lumbosacral spinal cords in the acute period but it was restored to normal values after the recovery period. These observations suggest that an alteration on the mechanism of neurotransmitter release could be involved in the development of the clinical signs of EAE.
Significant morphological and functional alterations of synapses have been described in EAE. Also, it has been shown that antibodies and T cells against the encephalitogenic myelin basic protein (MBP) immunocrossreacts with Synapsin I (Syn), a neuron-specific protein located mainly in the presynaptic terminals. Syn phosphorylation controls its association to synaptic vesicles and actin filaments, playing an important role in the regulation of neurotransmitter release. In this work we study the state of phosphorylation of Syn during the development of EAE induced in Wistar rats. The synaptosomal fractions (P2) were purified from brain, cerebellum and spinal cord of EAE and control animals, and subsequent quantification of total Syn and phosphorylated Syn at Site 1 (phosphoSer9) was done by immunoblot analysis. We found that in the acute and recovery stages of EAE the amount of total Syn was similar in all the tissue samples. However, phosphorylation of Syn was significantly diminished (~40%) in the lumbosacral spinal cords in the acute period but it was restored to normal values after the recovery period. These observations suggest that an alteration on the mechanism of neurotransmitter release could be involved in the development of the clinical signs of EAE.
