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Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
Published on: March 10, 2010
El distroglicano-alfa, una glicoproteína asociada a la distrofina, es un receptor de agrina funcional
S H Gee1, F Montanaro, M H Lindenbaum
1Centre for Research in Neuroscience, McGill University, Montreal General Hospital Research Institute, Quebec, Canada.
Cell
|June 3, 1994
Resumen
El distroglicano-alfa se une a la agrina, una proteína crucial para la agregación del receptor de acetilcolina (AChR) en las fibras musculares. Esta unión, parte de un complejo de receptores de distrofina, es esencial para el agrupamiento de AChR.
Área de la Ciencia:
- Biología muscular Biología muscular.
- La adhesión celular es la adhesión celular.
- La neurociencia es la neurociencia.
Sus antecedentes:
- Se cree que Agrin, una proteína de la lámina basal, media la agregación del receptor de acetilcolina (AChR) en las fibras del músculo esquelético.
- Las similitudes estructurales entre la agrina y la laminina sugieren una posible interacción con el distroglicano alfa, un receptor de la laminina dentro del complejo receptor de la distrofina.
Objetivo del estudio:
- Para investigar si el distroglicano-alfa se une al agrin.
- Determinar el papel del distroglicano alfa y de la proteína relacionada con la distrofina (DRP/utrofina) en la agregación de la AChR inducida por la agrina.
Principales métodos:
- Ensayos de unión in vitro utilizando proteínas purificadas.
- Microscopía de inmunofluorescencia para detectar la localización de proteínas en los miotubos C2 y las células S27.
- Estudios de inhibición mediante el uso de anticuerpos monoclonales (MAb IIH6), heparina, laminina y fibronectina.
- Evaluación de la agregación de AChR inducida por agrina en presencia de MAb IIH6.6.
Principales resultados:
- El distroglicano-alfa y el DRP/utrofina se encontraron concentrados en agregados de AChR en miotubos C2.
- Agrin se une específicamente al distroglicano-alfa in vitro, una interacción dependiente del calcio inhibida por el MAb IIH6, la heparina y la laminina.
- La unión de la agrina y la laminina al distroglicano alfa se redujo significativamente en las células S27, que carecen de agregación espontánea de la AChR.
- MAb IIH6 inhibió sustancialmente la agregación de AChR inducida por agrina en las células C2.
Conclusiones:
- El distroglicano-alfa funciona como una proteína que se une a la agrina.
- El distroglicano-alfa, como parte de un complejo de receptores de distrofina, juega un papel importante en la agregación de los receptores de acetilcolina en la unión neuromuscular.
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