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β‐Dystroglycan: Subcellular Localisation in Rat Brain and Detection of a Novel Immunologically Related, Postsynaptic Density‐Enriched Protein
Author(s) -
Mummery Rosemary,
Sessay Abdul,
Lai F. Anthony,
Beesley Philip W.
Publication year - 1996
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1996.66062455.x
Subject(s) - postsynaptic potential , dystrophin , postsynaptic density , forebrain , glycoprotein , biology , molecular mass , biochemistry , synaptic cleft , antiserum , microbiology and biotechnology , chemistry , skeletal muscle , neuroscience , neurotransmission , endocrinology , enzyme , antigen , central nervous system , receptor , genetics
The distribution of a glycoprotein component of the muscle dystrophin complex, β‐dystroglycan, has been determined in subcellular fractions of adult rat forebrain. The results show that β‐dystroglycan is enriched in several membrane fractions, including synaptic membranes, but in marked contrast to dystrophin is not detectable in the postsynaptic density fraction. The antiserum also recognises a second molecular species of apparent molecular mass of 164 kDa which is highly enriched in the postsynaptic density fraction. Preabsorption of the antiserum with the antigen (a 22‐mer peptide corresponding to the C‐terminal sequence of rabbit skeletal muscle β‐dystroglycan) abolished reactivity against both β‐dystroglycan and the 164‐kDa postsynaptic density‐enriched protein, confirming that the two species are immunologically related. Enzymatic removal of N‐linked oligosaccharide lowered the apparent molecular mass of β‐dystroglycan by 3 kDa but did not alter the mass of the 164‐kDa species.