Antilaminin IgG triggers the murine atria phosphoinositide hydrolysis through muscarinic receptor stimulation.

Induction of polyphosphoinositide hydrolysis in cardiac tissue by specific recognition of laminin by antilaminin IgG was assayed. BALB/c mice atria were labelled with the myo-[3H]-inositol precursor and inositol phosphate production was measured in the presence and absence of antilaminin and normal IgG. Antilaminin IgG but not normal IgG specifically increased phosphoinositide (PI) turnover. This increment was blocked by the muscarinic cholinergic antagonist atropine and mimicked by the cholinergic agonist carbachol. The phospholipase C inhibitor diphenylcarbamate (NCDC) also antagonized the stimulatory action of antilaminin IgG on PI turnover. By using an immunofluorescence technique, antilaminin IgG reacted with myocardial cell basement membranes. This antibody fixation was not blocked by atropine. These data suggest that antilaminin IgG specifically recognized myocardial laminin molecules and activated PI turnover through cholinergic stimulation. Even though laminin and cholinergic receptors are different, they probably share common signal transduction systems.