RESUMEN

Mutations in the gene encoding fukutin protein cause Fukuyama muscular dystrophy, a severe congenital disorder that occurs mainly in Japan. A major consequence of the mutation is reduced glycosylation of alpha-dystroglycan, which is also a feature of other forms of congenital and limb-girdle muscular dystrophy. Immunodetection of endogenous fukutin in cells and tissues has been difficult and this has hampered progress in understanding fukutin function and disease pathogenesis. Using a new panel of monoclonal antibodies which bind to different defined sites on the fukutin molecule, we now show that fukutin has the predicted size for a protein without extensive glycosylation and is present at the Golgi apparatus at very low levels. These antibodies should enable more rapid future progress in understanding the molecular function of fukutin.

Asunto(s)

Anticuerpos Monoclonales , Proteínas de la Membrana/análisis , Síndrome de Walker-Warburg/diagnóstico , Secuencia de Aminoácidos , Animales , Mapeo Epitopo , Glicosilación , Aparato de Golgi/metabolismo , Células HeLa , Humanos , Hibridomas , Epítopos Inmunodominantes/análisis , Epítopos Inmunodominantes/genética , Epítopos Inmunodominantes/inmunología , Proteínas de la Membrana/genética , Proteínas de la Membrana/inmunología , Ratones , Ratones Endogámicos BALB C , Datos de Secuencia Molecular , Biblioteca de Péptidos , Síndrome de Walker-Warburg/genética , Síndrome de Walker-Warburg/metabolismo