2013, Número 6
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Rev Invest Clin 2013; 65 (6)
La glicosilación de los anticuerpos y su efecto patogénico
Olivares N, Hernández-Pando R
Idioma: Español
Referencias bibliográficas: 42
Paginas: 515-523
Archivo PDF: 204.07 Kb.
RESUMEN
Las inmunoglobulinas de clase G (IgG) tienen unida covalentemente
una cadena de azúcares en el fragmento cristalizable
(Fc), estructura que está constituida por complejos glucosídicos
bicatenarios con un alto grado de heterogeneidad que contribuyen
en definir la afinidad de los Ac por sus receptores
específicos, determinando en parte su actividad biológica. Recientemente
se identificó un mecanismo antiinflamatorio mediado
por las IgG con base en las diferentes alternativas de
glicosilación del Fc y su interacción con el receptor de adhesión
específico de células dendríticas (DC-SIGN). Este mecanismo
ha tenido implicaciones clínicas y terapéuticas en los
procesos autoinmunes. El objetivo de esta revisión es describir
la estructura bioquímica de los azúcares asociados al Fc de la
IgG, así como sus variantes en relación con las funciones específicas
que éstas le confieren como factor patogénico en las
enfermedades autoinmunes e infecciosas, particularmente en
la tuberculosis donde también podría tener implicación terapéutica.
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