Production of antibodies against rhodopsin after immunization with .beta..gamma.-subunits of transducin: evidence for interaction of .beta..gamma.-subunits of guanosine 5'-triphosphate binding proteins with receptor

Autor: Martha Vaughan, Robert Sohn, Patrick P. Chang, Joel Moss, Su Chen Tsai, Y Kanaho, Jane L. Halpern, Ronald Adamik
Rok vydání: 1987
Předmět:
Zdroj: Biochemistry. 26:1655-1658
ISSN: 1520-4995
0006-2960
Popis: The light-detecting system of retinal rod outer segments is regulated by a guanyl nucleotide binding (G) protein, transducin, which is composed of alpha-, beta-, and gamma-subunits. Transducin couples rhodopsin to the intracellular effector enzyme, a cGMP phosphodiesterase. The beta gamma complex (T beta gamma) is required for the alpha-subunit (T alpha) to interact effectively with the photon receptor rhodopsin. It is not clear, however, whether T beta gamma binds directly to rhodopsin or promotes T alpha binding to rhodopsin only by binding to T alpha. We have found that serum from rabbits immunized with T beta gamma contained a population of antibodies that were reactive against rhodopsin. These antibodies could be separated from T beta gamma antibodies by absorbing the latter on immobilized transducin. Binding of purified rhodopsin antibodies was inhibited by T beta gamma, suggesting that the rhodopsin antibodies and T beta gamma bound to the same site on rhodopsin. We propose that the rhodopsin antibodies act both as antiidiotypic antibodies against the idiotypic T beta gamma antibodies and as antibodies against rhodopsin. This hypothesis is consistent with the conclusion that T beta gamma interacts directly with the receptor. It is probable that in an analogous way, G beta gamma interacts directly with receptors of the adenylate cyclase system.
Databáze: OpenAIRE