JOURNAL ARTICLE
RESEARCH SUPPORT, NON-U.S. GOV'T
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The naturally occurring mutation Y197C does not affect the expression or signaling of the human histamine H 3 receptor.

Neuroscience Letters 2017 Februrary 23
There is evidence for genetic polymorphism within the human histamine H3 receptor (hH3 R), and a Tyr to Cys exchange at position 197 (Y197C), located in the amino terminus of the fifth transmembrane domain, has been reported. In this work we compared the expression and the pharmacological and signaling properties of wild-type (hH3 RWT ) and mutant (hH3 RY197C ) receptors transiently expressed in CHO-K1 cells. The hH3 RY197C cDNA was created by overlap extension PCR amplification. Receptor expression and affinity were assessed by N-α-[methyl-3 H]-histamine binding to cell membranes and intact cells. Receptor function was evaluated by stimulation of [35 S]-GTPγS binding to cell membranes and by inhibition of forskolin-induced cAMP accumulation in intact cells. The hH3 RWT and hH3 RY197C were expressed at similar levels (761±68 and 663±66fmol/mg protein for membranes, and 13,434±1533 and 15,894±1884 receptors per cell, respectively). There were no significant differences in the affinities for H3 R agonists or antagonists/inverse agonists between the hH3 RWT and hH3 RY197C , and the H3 R agonist RAMH was similarly efficacious and potent to stimulate [35 S]-GTPγS binding and to inhibit forskolin-induced cAMP accumulation. These results indicate that the Y197C mutation does not affect the expression, ligand affinity or signaling of the human H3 receptor.

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