Phospholipase C-β3 mediates the thrombin-induced Ca2+ response in glial cells

Jong Ik Hwang, Kum Joo Shin, Yong Seok Oh, Jung Woong Choi, Zee Won Lee, Daesoo Kim, Kwon Soo Ha, Hee Sup Shin, Sung Ho Ryu, Pann Ghill Suh

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


Phospholipase C-β (PLC-β) hydrolyses phosphatidylinositol 4,5-bisphosphate and generates inositol 1,4,5-trisphosphate in response to activation of various G protein-coupled receptors (GPCRs). Using glial cells from knock-out mice lacking either PLC-β1 [PLC-β1 (-/-)] or PLC-β3 [PLC-β3 (-/-)], we examined which isotype of PLC- participated in the cellular signaling events triggered by thrombin. Generation of inositol phosphates (IPs) was enhanced by thrombin in PLC-β1 (-/-) cells, but was negligible in PLC-β3 (-/-) cells. Expression of PLC-β in PLC-β(-/-) cells resulted in an increase in pertussis toxin (PTx)-sensitive IPs in response to thrombin as well as to PARI-specific peptide, while expression of PLC-β1 in PLC-β1 (-/-) cells did not have any effect on IP generation. The thrombin-induced [Ca2+]i increase was delayed and attenuated in PLC-β3 (-/-) cells, but normal in PLC-β1 (-/-) cells. Pertussis toxin evoked a delayed [Ca2+], increase in PLC-β3 (-/-) cells as well as in PLC-β1 (-/-) cells. These results suggest that activation of PLC-β3 by pertussis toxin-sensitive G proteins is responsible for the transient [Ca2+], increase in response to thrombin, whereas the delayed [Ca2+], increase may be due to activation of some other PLC, such as PLC-β4, acting via PTx-insensitive G proteins.

Original languageEnglish
Pages (from-to)375-381
Number of pages7
JournalMolecules and cells
Issue number3
Publication statusPublished - 2005
Externally publishedYes


  • Calcium
  • GPCR
  • Glial Cells Inositol Phosphates
  • PLC-β3

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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