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Am J Physiol Cell Physiol 276: C930-C937, 1999;
0363-6143/99 $5.00
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Vol. 276, Issue 4, C930-C937, April 1999

Endothelin-B receptors activate Galpha 13

Kenichiro Kitamura1, Naoki Shiraishi2, William D. Singer3, Mary E. Handlogten2, Kimio Tomita1, and R. Tyler Miller2

2 Division of Nephrology, University of Florida, Gainesville, Florida 32610; 3 Department of Pharmacolgy, University of Texas Southwestern Medical School, Dallas, Texas 75235; and 1 Fourth Department of Internal Medicine, Kumamoto University, Kumamoto, Japan

Endothelin (ET) receptors activate heterotrimeric G proteins that are members of the Gi, Gq, and Gs families but may also activate members of other families such as Galpha 12/13. Galpha 13 has multiple complex cellular effects that are similar to those of ET. We studied the ability of ET receptors to activate Galpha 13 using an assay for G protein alpha -chain activation that is based on the fact that an activated (GTP-bound) alpha -chain is resistant to trypsinization compared with an inactive (GDP-bound) alpha -chain. Nonhydrolyzable guanine nucleotides and AlMgF protected Galpha 13 from degradation by trypsin. In membranes from human embryonic kidney 293 cells that coexpress ETB receptors and alpha 13, ET-3 and 5'-guanylylimidodiphosphate [Gpp(NH)p] increased the protection of alpha 13 compared with Gpp(NH)p alone. The specificity of ETB receptor-alpha 13 coupling was documented by showing that beta 2 receptors and isoproterenol or ETA receptors and ET-1 did not activate alpha 13 and that a specific antagonist for ETB receptors blocked ET-3-dependent activation of alpha 13.

G protein; cell signaling; G protein-coupled receptor


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