The role of canonical transient receptor potential 7 in B-cell receptor-activated channels

Jean Philippe Lievremont, Takuro Numaga, Guillermo Vazquez, Loïc Lemonnier, Yuji Hara, Emiko Mori, Mohamed Trebak, Stephen E. Moss, Gary S. Bird, Yasuo Mori, James W. Putney

Research output: Contribution to journalArticlepeer-review

55 Scopus citations


Phospholipase C signaling stimulates Ca2+ entry across the plasma membrane through multiple mechanisms. Ca2+ store depletion stimulates store-operated Ca2+-selective channels, or alternatively, other phospholipase C-dependent events activate Ca2+-permeable non-selective cation channels. Transient receptor potential 7 (TRPC7) is a non-selective cation channel that can be activated by both mechanisms when ectopically expressed, but the regulation of native TRPC7 channels is not known. We knocked out TRPC7 in DT40 B-cells, which expresses both forms of Ca 2+ entry. No difference in the store-operated current I crac was detected between TRPC7-/- and wild-type cells. Wild-type cells demonstrated non-store-operated cation entry and currents in response to activation of the B-cell receptor or protease-activated receptor 2, intracellular dialysis with GTPγS, or application of the synthetic diacylglycerol oleyl-acetyl-glycerol. These responses were absent in TRPC7 -/- cells but could be restored by transfection with human TRPC7. In conclusion, in B-lymphocytes, TRPC7 appeared to participate in the formation of ion channels that could be activated by phospholipase C-linked receptors. This represents the first demonstration of a physiological function for endogenous TRPC7 channels.

Original languageEnglish (US)
Pages (from-to)35346-35351
Number of pages6
JournalJournal of Biological Chemistry
Issue number42
StatePublished - Oct 21 2005

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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