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Submitted on November 14, 2003
Accepted on January 5, 2004
Department of Chemistry, University of Kentucky, Lexington, KY 40506-0055 and School of Biotechnology and Biomedical Science, InJe Univeristy, GimHae, Korea
* To whom correspondence should be addressed. E-mail: tji{at}uky.edu.
Previously, we reported that a liganded LH receptor is capable of activating it (cis-activation) as well as other nonliganded LH receptors to induce cAMP (trans-activation). Trans-activation of the LH receptor raises two crucial questions. Is trans-activation unique to LHR or common to other G protein coupled receptors? Does trans-activation stimulate phospholipase C
as it does adenylyl cyclase? To address these questions, two types of novel FSH receptors were constructed, one defective in hormone binding and the other defective in signal generation. The FSH receptor, a G protein coupled receptor, comprises two major domains, the N-terminal extracellular exodomain that binds the hormone and the membrane associated endodomain that generates the hormone signals. For signal defective receptors, the exodomain was attached to glycosyl phosphatidylinositol (ExoGPI) or the transmemebrane domain of CD8 immune receptor (ExoCD). ExoGPI and ExoCD can trans-activate another nonliganded FSH. Surprisingly, the trans-activation generates a signal to activate either adenylyl cyclase or phospholipase C, but not both. These results indicate that trans-activation in these mutant receptors is selective and limited in signal generation, thus providing new approaches to investigating the generation of different hormone signals and a novel means to selectively generate a particular hormone signal. Our data also suggests that the FSH receptor's exodomain could not trans-activate LH receptor.
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