Immunodetection of partially glycosylated isoforms of alpha-dystroglycan by a new monoclonal antibody against its beta-dystroglycan-binding epitope |
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Authors: | Pavoni Ernesto Sciandra Francesca Barca Stefano Giardina Bruno Petrucci Tamara Corinna Brancaccio Andrea |
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Institution: | CNR, Istituto di Chimica del Riconoscimento Molecolare c/o Istituto di Biochimica e Biochimica Clinica, Università Cattolica del Sacro Cuore, Largo F. Vito 1, 00168 Roma, Italy. |
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Abstract: | The alpha/beta dystroglycan (DG) complex links the extracellular matrix to the actin cytoskeleton. The extensive glycosylation of alpha-DG is believed to be crucial for the interaction with its extracellular matrix-binding partners. We characterized a monoclonal antibody, directed against the beta-DG-binding epitope ( approximately positions 550-565), which recognizes preferentially hypoglycosylated alpha-DG. In Western blot, the antibody was able to detect a number of partially glycosylated alpha-DG isoforms from rat brain and chicken skeletal muscle tissue samples. In addition, we demonstrated its inhibitory effect on the interaction between alpha- and beta-DG in vitro and preliminary immunostaining experiments suggest that such hypoglycosylated alpha-DG isoforms could play a role within cells. |
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Keywords: | Dystroglycan Monoclonal antibody Isoform Glycosylation |
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