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J. Biol. Chem., Vol. 265, Issue 35, 21411-21414, 12, 1990
YB Xie, H Wang and DL Segaloff
The lutropin-choriogonadotropin (LH/CG) receptor is a cell surface receptor
comprised of two domains of roughly equivalent size. The amino- terminal
half of the receptor is relatively hydrophilic and is located
extracellularly, whereas the carboxyl-terminal half of the receptor shares
amino acid homology with other receptors that couple to G proteins and is
similarly thought to span the plasma membrane seven times, ending with a
relatively short carboxyl-terminal tail. In order to test the role of the
extracellular domain in binding hormone, we constructed a mutated rat
luteal LH/CG receptor cDNA (termed pCLHR-D2), which encodes for only the
extracellular domain, and used it to transiently transfect human kidney 293
cells. Here we report that the expressed extracellular domain of the LH/CG
receptor is capable of binding human CG with a high affinity, comparable
with that of the full- length receptor. Thus, not only is the extracellular
domain of the glycoprotein hormone receptors involved in binding hormone,
but it alone is capable of conferring high affinity binding. Unexpectedly,
it was also found that this truncated receptor is not secreted into the
culture media but remains trapped within the cells.
Extracellular domain of lutropin/choriogonadotropin receptor expressed in transfected cells binds choriogonadotropin with high affinity
Population Council, New York, New York 10021.
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