Related Experiment Videos
A specific histamine-stimulated phosphoprotein in isolated parietal cells
The Journal of Surgical Research
|April 1, 1987
Summary
Histamine stimulates acid secretion in rabbit parietal cells by phosphorylating a 30,000-Da protein (pp30). This cAMP-dependent protein phosphorylation is crucial for initiating or maintaining gastric acid secretion.
Area of Science:
- Cell biology
- Gastroenterology
- Molecular biology
Background:
- Parietal cells are responsible for gastric acid secretion.
- Histamine is a key stimulant of acid secretion.
- The molecular mechanisms underlying histamine-stimulated acid secretion require further elucidation.
Purpose of the Study:
- To identify specific proteins involved in histamine-stimulated parietal cell secretion.
- To investigate the role of protein phosphorylation in this process.
- To characterize the properties of histamine-stimulated phosphoproteins.
Main Methods:
- Isolated rabbit parietal cells were used.
- Acid secretion was measured by aminopyrine uptake.
- Two-dimensional gel electrophoresis was employed to identify phosphoproteins.
- In vitro phosphorylation assays were performed on parietal cell cytosol.
Main Results:
- Histamine stimulation led to linear acid secretion after 15 minutes.
- A 30,000-Da protein (pp30) was identified, showing prominent histamine-stimulated phosphorylation.
- pp30 has an isoelectric point of 6.0.
- pp30 phosphorylation was demonstrated to be cAMP-dependent in vitro.
Conclusions:
- pp30 is a significant histamine-stimulated, cAMP-dependent phosphoprotein in parietal cells.
- pp30 likely plays a critical role in initiating or maintaining gastric acid secretion.
- Further research into pp30 function could reveal new therapeutic targets for acid-related disorders.