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Related Experiment Videos

Endoplasmic reticulum Ca(2+)-ATPase inhibitors stimulate membrane guanylate cyclase in pancreatic acinar cells.

A S Gukovskaya1, S Gukovsky, S J Pandol

  • 1Departments of Medicine, Veterans Affairs Greater Los Angeles Healthcare System and University of California, Los Angeles, California 90073, USA. agukovsk@ucla.edu

American Journal of Physiology. Cell Physiology
|February 9, 2000
PubMed
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Particulate guanylate cyclase (GC) in rat pancreatic acinar cells is activated by ER Ca(2+)-ATPase inhibitors, suggesting a link between ER Ca(2+)-ATPase and GC activity.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Gastroenterology

Background:

  • Particulate guanylate cyclase (GC) plays a role in cellular signaling.
  • The localization and regulation of GC in pancreatic acinar cells are not fully understood.

Purpose of the Study:

  • To investigate the presence and localization of particulate GC in rat pancreatic acinar cells.
  • To explore the relationship between ER Ca(2+)-ATPase and particulate GC activity.

Main Methods:

  • Western blot analysis to identify GC isoforms.
  • Treatment of pancreatic acini with ER Ca(2+)-ATPase inhibitors (thapsigargin, BHQ, CPA).
  • Co-immunoprecipitation assays to assess enzyme interactions.

Main Results:

Related Experiment Videos

  • Particulate GC, specifically the GC-A isoform, is found in rat pancreatic acinar cell membranes and ER.
  • ER Ca(2+)-ATPase inhibitors activate particulate GC and induce its dephosphorylation.
  • ER Ca(2+)-ATPase and GC show co-immunoprecipitation, indicating a physical association.

    • Conclusions:

    • ER Ca(2+)-ATPase activity is linked to the activation of particulate GC in pancreatic acinar cells.
    • Inhibitors of ER Ca(2+)-ATPase likely activate GC through interaction with ER Ca(2+)-ATPase, though direct effects on GC are possible.