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Thiophosphorylation causes Ca2+-independent norepinephrine secretion from permeabilized PC12 cells
1Laboratory of Biochemistry, National Cancer Institute, Bethesda, Maryland 20892.
The Journal of Biological Chemistry
|November 25, 1989
Summary
Phosphorylation regulates norepinephrine secretion in PC12 cells. Adenosine-5'-O-(3-thiotriphosphate) (ATP gamma S) showed that Ca2+-dependent phosphorylation enables ATP-dependent secretion, even without calcium.
Area of Science:
- Neuroscience
- Cell Biology
- Biochemistry
Background:
- Norepinephrine secretion is crucial for neuronal communication.
- Phosphorylation plays a key role in cellular signaling pathways.
- PC12 cells are a widely used model for studying neuronal function.
Purpose of the Study:
- To investigate the role of phosphorylation in regulating norepinephrine secretion from PC12 cells.
- To determine the influence of calcium and ATP on this phosphorylation-dependent process.
Main Methods:
- Utilized digitonin-permeabilized PC12 cells.
- Employed Adenosine-5 -O-(3-thiotriphosphate) (ATP gamma S) to mimic phosphorylation.
- Assessed norepinephrine secretion under varying calcium and ATP conditions.
Main Results:
- ATP gamma S preincubation led to Ca2+-independent norepinephrine secretion.
- This Ca2+-independent secretion remained ATP-dependent.
- Calcium accelerated the phosphorylation process induced by ATP gamma S or ATP.
Conclusions:
- Norepinephrine secretion in PC12 cells is regulated by Ca2+-dependent phosphorylation.
- Phosphorylation, once established, allows for ATP-dependent secretion that is no longer calcium-dependent.