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Participation of cytoskeleton in the effect of antilaminin IgG on cardiac cholinoceptors
Author(s) -
Bacman Sandra,
Borda Enri,
Denduchis Berta,
Lustig Livia,
SterinBorda Leonor
Publication year - 1994
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.1994.tb14055.x
Subject(s) - muscarinic acetylcholine receptor , contractility , cholinergic , endocrinology , medicine , agonist , biology , nocodazole , microbiology and biotechnology , cytoskeleton , receptor , chemistry , biochemistry , cell
1 We have previously demonstrated a molecular relationship between laminin and cardiac cholinoceptors. 2 We have now explored the participation of cytoskeletal proteins in the interaction between an antilaminin IgG with cardiac cholinoceptors. 3 Antilaminin IgG, whilst it specifically reacts with laminin molecules was able to induce cardiac cholinoceptor activation; acting like an agonist, decreasing cyclic AMP concentrations, reducing heart contractility and increasing phosphoinositide turnover. 4 Antilaminin IgG also interfered with the binding of a radiolabelled muscarinic antagonist, [ 3 H]‐quinuclidinyl benzilate. Colchicine and cytochalasin B, drugs that are able to prevent microfilament and microtubule polimerization, impaired the binding of antilaminin IgG to muscarinic cholinoceptors. 5 Cytochalasin B but not colchicine modified the muscarinic cholinoceptor effects mediated by regulatory G proteins (cyclic AMP and contractility) induced by antilaminin IgG. 6 It was demonstrated, by immunofluorescence, that none of these disrupting drugs altered the specific recognition of the antibody by its antigen. 7 These data indirectly suggest the participation of the cytoskeleton in the laminin and cholinergic receptor association.