Dystroglycan is a ubiquitous protein that links the extracellular matrix to the cytoskeleton and is the central unit of the dystrophin glycoprotein complex (DGC), a membrane complex that connects the cytoskeleton to the extracellular matrix (ECM). Dystroglycan is composed of two subunits that are tightly but non-covalently linked. alpha Dystroglycan (alpha DG) is located extracellularly and it is the only component of the DGC linked to the ECM, while beta Dystroglycan (beta DG) spans the plasma membrane and has both an extracellular and a cytoplasmic domain. The DGC is involved in skeletal muscle maintenance and viability, and in the organization and stabilization of the neuromuscular junction, but its function in brain is poorly understood. DGC components are target of several protein kinases, indicating that they are involved in cell signalling pathways. The finding of new dystroglycan interacting proteins could help to obtain some insights in its function in brain tissues. Previous immunoprecipitation and pull down experiments have been used to identify proteins interacting with the cytoplasmic tail of beta DG in brain tissues. Here, we attempt to extend the use of these techniques by using pull down experiments performed with the Glutathione-S-transferase (GST) fusion expression system as a tool for the proteomic analysis of Dystroglycan interacting proteins in the brain.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.82287 |
| Date | January 2005 |
| Creators | Marazzo, Elena |
| Publisher | McGill University |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | English |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Format | application/pdf |
| Coverage | Master of Science (Department of Biology.) |
| Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| Relation | alephsysno: 002226985, proquestno: AAIMR12498, Theses scanned by UMI/ProQuest. |
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