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α‐dystroglycan isoforms are differentially distributed in adult rat retina
Author(s) -
Moukhles Hakima,
Roque Rouel,
Carbonetto Salvatore
Publication year - 2000
Publication title -
journal of comparative neurology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.855
H-Index - 209
eISSN - 1096-9861
pISSN - 0021-9967
DOI - 10.1002/(sici)1096-9861(20000501)420:2<182::aid-cne3>3.0.co;2-2
Subject(s) - biology , outer plexiform layer , retina , microbiology and biotechnology , laminin , inner limiting membrane , dystroglycan , gene isoform , basal lamina , neuroscience , anatomy , biochemistry , extracellular matrix , gene , ultrastructure
Abstract α‐Dystroglycan (α ‐DG) is a laminin/agrin receptor expressed in skeletal muscle as well as in nervous system and other tissues. Glycosylation of the core protein of α‐DG is extensive, variable from tissue to tissue, and functionally relevant. To address differential glycosylation of α‐DG in the retina, we have investigated the distribution of this protein using two different antibodies: 1B7 directed against the core protein of α‐dystroglycan, and IIH6 directed against a carbohydrate moiety (Ervasti and Campbell [1993] J Cell Biol 122:809–823). Monoclonal antibody 1B7 recognizes a broader band than IIH6, which seems to recognize only a subset of α‐DG forms in retina. These data reflect the existence of differentially glycosylated isoforms of α‐DG. Monoclonal antibody 1B7 shows an extensive staining for α‐DG in the inner limiting membrane as well as in the ganglion cell and inner plexiform layers labeling Müller cell processes, whereas monoclonal antibody IIH6 staining is restricted to the inner limiting membrane and blood vessels. Our data indicate that there are distinct isoforms of α‐DG that are localized in apposition to basal lamina in the inner limiting membrane and blood vessels or within the parenchyma of the retina along Müller glia. Both isoforms are expressed in a Müller cell line in culture and coimmunoprecipitate with β‐dystroglycan. These data suggest that DGs may participate in organizing synapses and basement membrane assembly in the retina. J. Comp. Neurol. 420:182–194, 2000. © 2000 Wiley‐Liss, Inc.