cAMP regulates plasma membrane vacuolar-type H+-ATPase assembly and activity in blowfly salivary glands.

@article{Dames2006cAMPRP,
  title={cAMP regulates plasma membrane vacuolar-type H+-ATPase assembly and activity in blowfly salivary glands.},
  author={Petra Dames and Bernhard Zimmermann and Ruth Schmidt and Julia Rein and Martin Voss and Bettina Schewe and Bernd Walz and Otto Baumann},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2006},
  volume={103 10},
  pages={
          3926-31
        }
}
  • P. Dames, B. Zimmermann, +5 authors O. Baumann
  • Published 2006
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
Reversible assembly of the V0V1 holoenzyme from V0 and V1 subcomplexes is a widely used mechanism for regulation of vacuolar-type H+-ATPases (V-ATPases) in animal cells. In the blowfly (Calliphora vicina) salivary gland, V-ATPase is located in the apical membrane of the secretory cells and energizes the secretion of a KCl-rich saliva in response to the hormone serotonin. We have examined whether the cAMP pathway, known to be activated by serotonin, controls V-ATPase assembly and activity… Expand
Hormone-induced assembly and activation of V-ATPase in blowfly salivary glands is mediated by protein kinase A.
TLDR
It is concluded that cAMP exerts its effects on V-ATPase via PKA, the cAMP target proteins that are present within the salivary glands. Expand
The blowfly salivary gland - a model system for analyzing the regulation of plasma membrane V-ATPase.
TLDR
The blowfly salivary glands are a superior and exemplary system for the analysis of the intracellular signaling pathways and mechanisms that modulate V-ATPase activity and solute transport in an insect epithelium. Expand
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TLDR
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TLDR
Findings suggest a role for phospho-moesin, a linker between actin filaments and membrane components, in apical membrane morphogenesis in blowfly secretory cells. Expand
Stimulus-induced Phosphorylation of Vacuolar H+-ATPase by Protein Kinase A*
TLDR
Salivary glands of the blowfly Calliphora vicina are used to suggest that subunit C binds to and serves as a substrate for protein kinase A and that this phosphorylation may be a regulatory switch for the formation of the active V1V0 holoenzyme. Expand
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TLDR
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Fluorescence measurements of serotonin-induced V-ATPase-dependent pH changes at the luminal surface in salivary glands of the blowfly Calliphora vicina
TLDR
Ratiometric measurements of HAF fluorescence provide an elegant method for monitoring V-ATPase-dependent H+ transport in the blowfly salivary gland in vivo and for analysing the spatiotemporal pattern of pH changes at the luminal surface. Expand
Regulation of V-ATPase activity.
TLDR
V-ATPases are ATP-driven proton pumps present in both intracellular and cell surface membranes of eukaryotes that function in many normal and disease processes and differential expression of genes encoding V- ATPases subunits occurs in a number of contexts, including cancer. Expand
Intracellular pH homeostasis and serotonin-induced pH changes in Calliphora salivary glands: the contribution of V-ATPase and carbonic anhydrase
TLDR
It is concluded that V-ATPase and CA contribute to steady-state pHi regulation and 5-HT-induced outward H+ pumping does not cause an alkalinization of pHi because of cytosolic H+ accumulation attributable to stimulated cellular respiration and AE activity, masking the alkalizing effect of V- ATPase-mediated acid extrusion. Expand
A vacuolar-type H+-ATPase and a Na+/H+ exchanger contribute to intracellular pH regulation in cockroach salivary ducts
TLDR
It is concluded that the apical V-ATPase and a basolateral Na+/H+ exchange play a minor role in steady-state pHi regulation but contribute both to H+ extrusion after an acute dopamine- or NH4Cl-induced acid load. Expand
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