Colchicine blocks beta adrenoceptor and class I antigen-specific interactions.

Previously we have demonstrated a molecular relationship between H-2 class I antigens and beta adrenoceptors from cardiac tissue. Here we show this type of interaction taking place with beta adrenoceptors from splenic cells and their purified membranes and the participation of cytoskeletal proteins in the phenomenon. Alloimmune, as well as anti-class I but not anti-class II, antibodies were able to inhibit in a competitive manner the binding of (-)-[3H]dihydroalprenolol to splenic lymphocytes and their purified membranes, and to increase cyclic AMP levels in intact cells as a consequence of beta adrenoceptor activation. Furthermore, colchicine (a microtubule disrupting drug), but not cytochalasin B (a microfilament disrupting drug), was able to abrogate alloimmune antibody inhibition over the beta radioligand binding to its receptor on both intact splenocytes and their membranes. Alloantibody actions were significantly diminished by peripheral protein solubilization in purified spleen cell membranes. These data pointed indirectly to the participation of a colchicine binding protein in class I antigen hormone-receptor associations.