Regulation of transmembrane signaling by ganglioside GM1: interaction of anti-GM1 with Neuro2a cells.

摘要: Interaction of antibodies to ganglioside GM1 with Neuro2a cells was studied investigate the role in cell signaling. Binding anti-GM1 induced formation 3H-inositol phosphates (3H-IPs) and elevated intracellular Ca2+ concentration [Ca2+]i. The rise [Ca2+]i due influx from extracellular medium release pools. pathway did not allow permeation Na+ or K+. inhibited by amiloride, a specific blocker T-type channels, whereas nifedipine diltiazem, blockers L-type have any effect. Thus, appears activate channel cells. pretreatment neomycin sulfate, phorbol dibutyrate, pertussis toxin (PTx), which also 3H-IP Addition caffeine neither nor affected anti-GM1-induced rise. data reveal that binding activates phospholipase C via PTx-sensitive G protein, leads IPs inositol trisphosphate-sensitive pool endoplasmic reticulum. Anti-GM1 arrested differentiation culture significantly stimulated their proliferation. This stimulatory effect on proliferation blocked amiloride but PTx, suggesting essentially required for Our suggest regulation transmembrane signaling events growth.