Korean J Physiol Pharmacol.  2003 Aug;7(4):223-230.

Enhancement of ATP-induced Currents by Phospholipase D1 Overexpressed in PC12 Cells

Affiliations
  • 1Department of Physiology, College of Medicine, Chungnam National University, Daejeon, Korea. jinbong@cnu.ac.kr
  • 2Department of Biochemistry, College of Medicine, Chungnam National University, Daejeon, Korea.

Abstract

Using phospholipase D1 (PLD1) -overexpressing PC12 (PLD1-PC12) cells, the regulatory roles of PLD1 on ATP-induced currents were investigated. In control and PLD1-PC12 cells, ATP increased PLD activity in an external Ca2+ dependent manner. PLD activity stimulated by ATP was substantially larger in PLD1-PC12 cells than in control cells. In whole-cell voltage-clamp mode, ATP induced transient inward and outward currents. The outward currents inhibited by TEA or charybdotoxin were significantly larger in PLD1-PC12 cells than in control cells. The inward currents known as Ca2+ permeable nonselective cation currents were also larger in PLD1-PC12 cells than in control cells. However, the difference between the two groups of cells disappeared in Ca2+ -free external solution, where ATP did not activate PLD. Finally, ATP-induced 45Ca uptakes were also larger in PLD1-PC12 cells than in control cells. These results suggest that PLD enhances ATP-induced Ca2+ influx via Ca2+ permeable nonselective cation channels and increases subsequent Ca2+ -activated K+ currents in PC12 cells.

Keyword

Phospholipase D1; ATP-induced currents; PC12 cell

MeSH Terms

Adenosine Triphosphate
Animals
Charybdotoxin
PC12 Cells*
Phospholipases*
Tea
Adenosine Triphosphate
Charybdotoxin
Phospholipases
Tea
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