Abstract
Bradykinin (BK) activates phospholipase D (PLD) and induces several responses such as catecholamine secretion, collapse of growth cones, and gene expression in PC12 pheochromocytoma cells. Although two distinct PLD isozymes, PLD1 and PLD2, have been cloned from mammalian cells, the regulatory mechanism for each PLD isozyme by BK is not clear. In our present study, we investigated the activation mechanism of PLD2 by BK in PLD2-overexpressing PC12 cells. BK stimulated PLD2 activity in a concentration-dependent manner within 1 min and this activation was inhibited by pretreatment of the cells with protein kinase C (PKC) inhibitor. PKCα and PKCδ translocated from cytosol to membrane upon BK treatment, and rottlerin potently inhibited the activation of PLD2 by BK. These results suggest that BK activates PLD2 via PKCδ in PC12 cells. Copyright (C) 2000 .
| Original language | English |
|---|---|
| Pages (from-to) | 130-132 |
| Number of pages | 3 |
| Journal | Neuroscience Letters |
| Volume | 294 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 17 Nov 2000 |
Bibliographical note
Funding Information:This work was supported in part by the programs of the National Research Laboratory and Brain Science Research of the Ministry of Science and Technology and by the Center for Cell Signaling Research and the Brain Korea 21 Project of Korea.
Copyright:
Copyright 2006 Elsevier B.V., All rights reserved.
Keywords
- Bradykinin
- PC12 cells
- Phosphatidylbutanol
- Phospholipase D
- Protein kinase C
- Tetracycline
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