Fragment C of Tetanus Toxin

When Clostridium tetani was discovered and identified as a Gram-positive anaerobic bacterium of the genus Clostridium, the possibility of turning its toxin into a valuable biological carrier to ameliorate neurodegenerative processes was inconceivable. However, the non-toxic carboxy-terminal fragment...

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Detalles Bibliográficos
Autores: Calvo, Ana Cristina|||0000-0001-5193-7782, Oliván, Sara, Manzano Martínez, Raquel|||0000-0002-7477-8742, Zaragoza, Pilar|||0000-0001-5740-0185, Aguilera, José|||0000-0002-9906-8034, Osta, Rosario|||0000-0001-5687-6704
Tipo de recurso: artículo
Fecha de publicación:2012
País:España
Institución:Universitat Autònoma de Barcelona
Repositorio:Dipòsit Digital de Documents de la UAB
Idioma:inglés
OAI Identifier:oai:ddd.uab.cat:147222
Acceso en línea:https://ddd.uab.cat/record/147222
https://dx.doi.org/urn:doi:10.3390/ijms13066883
Access Level:acceso abierto
Palabra clave:Clathrin-mediated pathway
Dynamin
Fragment C
Tetanus toxin
Neurotrophin
Trk receptors
Descripción
Sumario:When Clostridium tetani was discovered and identified as a Gram-positive anaerobic bacterium of the genus Clostridium, the possibility of turning its toxin into a valuable biological carrier to ameliorate neurodegenerative processes was inconceivable. However, the non-toxic carboxy-terminal fragment of the tetanus toxin heavy chain (fragment C) can be retrogradely transported to the central nervous system; therefore, fragment C has been used as a valuable biological carrier of neurotrophic factors to ameliorate neurodegenerative processes. More recently, the neuroprotective properties of fragment C have also been described in vitro and in vivo, involving the activation of Akt kinase and extracellular signal-regulated kinase (ERK) signaling cascades through neurotrophin tyrosine kinase (Trk) receptors. Although the precise mechanism of the molecular internalization of fragment C in neuronal cells remains unknown, fragment C could be internalized and translocated into the neuronal cytosol through a clathrin-mediated pathway dependent on proteins, such as dynamin and AP-2. In this review, the origins, molecular properties and possible signaling pathways of fragment C are reviewed to understand the biochemical characteristics of its intracellular and synaptic transport.