Forskolin stimulation of water and cation permeability in aquaporin 1 water channels

Andrea J. Yool, W. Daniel Stamer, John W Regan

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Aquaporin1, a six-transmembrane domain protein, is a water channel present in many fluid-secreting and -absorbing cells. In Xenopus oocytes injected with aquaporin 1 complementary RNA, the application of forskolin or cyclic 8-bromo-adenosine 3',5'-monophosphate increased membrane permeability to water and triggered a cationic conductance. The cationic conductance was also induced by direct injection of protein kinase A (PKA) catalytic subunit, reduced by the kinase inhibitor H7, and blocked by HgCl2, an inhibitor of aquaporin 1. The cationic permeability of the aquaporin 1 channel is activated by a cyclic adenosine monophosphate-dependent mechanism that may involve direct or indirect phosphorylation by PKA.

Original languageEnglish (US)
Pages (from-to)1216-1218
Number of pages3
Issue number5279
Publication statusPublished - 1996


ASJC Scopus subject areas

  • General

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