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J Biol Chem, Vol. 273, Issue 31, 19431-19436, July 31, 1998

G₁₄ and G_q Mediate the Response to Trypsin in Xenopus Oocytes

Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel-Aviv University, Ramat Aviv 69978, Israel and ^§ National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Rockville, Maryland 20850

Xenopus oocytes respond to trypsin with a characteristic chloride current, virtually indistinguishable from responses mediated by a large number of native and expressed G protein-coupled receptors. We studied the involvement of G proteins of the G_q family as possible mediators of this and other G protein-coupled receptor-mediated responses in Xenopus oocytes. We have cloned the third member of the G_q family, Xenopus G₁₄, in addition to the previously cloned Xenopus G_q and G₁₁ (Shapira, H., Way, J., Lipinsky, D., Oron, Y., and Battey, J. F. (1994) FEBS Lett. 348, 89-92). Amphibian G₁₄ is 354 amino acids long and is 93% identical to its mammalian counterpart. Based on the G₁₄ cDNA sequence, we designed a specific antisense DNA oligonucleotide (antiG₁₄) that, together with antiG_q and antiG₁₁, was used in antisense depletion experiments. 24 h after injection into oocytes, either antiG_q or antiG₁₄ reduced the response to 1 µg/ml trypsin by 70%, whereas antiG₁₁ had no effect. A mixture of antiG_q and antiG₁₄ virtually abolished the response. These data strongly suggest that G_q and G₁₄ are the exclusive mediators of the trypsin-evoked response in Xenopus oocytes. Similar experiments with the expressed gastrin-releasing peptide receptor and muscarinic m1 receptor revealed the coupling of G_q and G₁₁, but not G₁₄, to these receptors in oocytes. These results confirm the hypothesis that endogenous members of the Gq family discriminate among different native receptors in vivo.

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