Endothelin-B receptors activate Gα13

Kenichiro Kitamura, Naoki Shiraishi, William D. Singer, Mary E. Handlogten, Kimio Tomita, R. Tyler Miller

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


Endothelin (ET) receptors activate heterotrimeric G proteins that are members of the G(i), G(q), and G(s) families but may also activate members of other families such as Gα(12/13). Gα13 has multiple complex cellular effects that are similar to those of ET. We studied the ability of ET receptors to activate Gα13 using an assay for G protein α-chain activation that is based on the fact that an activated (GTP-bound) α-chain is resistant to trypsinization compared with an inactive (GDP-bound) α- chain. Nonhydrolyzable guanine nucleotides and AlMgF protected Gα13 from degradation by trypsin. In membranes from human embryonic kidney 293 cells that coexpress ET(B) receptors and α13, ET-3 and 5'- guanylylimidodiphosphate [Gpp(NH)p] increased the protection of α13 compared with Gpp(NH)p alone. The specificity of ET(B) receptor-α13 coupling was documented by showing that β2 receptors and isoproterenol or ET(A) receptors and ET-1 did not activate α13 and that a specific antagonist for ET(B) receptors blocked ET-3-dependent activation of α13.

Original languageEnglish (US)
Pages (from-to)C930-C937
JournalAmerican Journal of Physiology - Cell Physiology
Issue number4 45-4
StatePublished - 1999


  • Cell signaling
  • G protein
  • G protein-coupled receptor

ASJC Scopus subject areas

  • Physiology
  • Cell Biology


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