Enhancement of ATP-induced Currents by Phospholipase D1 Overexpressed in PC12 Cells.
- Author:
Jin Bong PARK
1
;
Young Rae KIM
;
Byeong Hwa JEON
;
Seung Kiel PARK
;
Sae Ock OH
;
Young Geun KIM
;
Sang Do LEE
;
Kwang Jin KIM
Author Information
1. Department of Physiology, College of Medicine, Chungnam National University, Daejeon, Korea. jinbong@cnu.ac.kr
- Publication Type:Original Article
- Keywords:
Phospholipase D1;
ATP-induced currents;
PC12 cell
- MeSH:
Adenosine Triphosphate;
Animals;
Charybdotoxin;
PC12 Cells*;
Phospholipases*;
Tea
- From:The Korean Journal of Physiology and Pharmacology
2003;7(4):223-230
- CountryRepublic of Korea
- Language:English
-
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.
