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J Insect Physiol. 2012 Apr;58(4):450-8. doi: 10.1016/j.jinsphys.2011.11.015. Epub 2011 Nov 25.

The blowfly salivary gland - a model system for analyzing the regulation of plasma membrane V-ATPase.

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Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Str. 24/25, 14476 Potsdam, Germany.


Vacuolar H(+)-ATPases (V-ATPases) are heteromultimeric proteins that use the energy of ATP hydrolysis for the electrogenic transport of protons across membranes. They are common to all eukaryotic cells and are located in the plasma membrane or in membranes of acid organelles. In many insect epithelia, V-ATPase molecules reside in large numbers in the apical plasma membrane and create an electrochemical proton gradient that is used for the acidification or alkalinization of the extracellular space, the secretion or reabsorption of ions and fluids, the import of nutrients, and diverse other cellular activities. Here, we summarize our results on the functions and regulation of V-ATPase in the tubular salivary gland of the blowfly Calliphora vicina. In this gland, V-ATPase activity energizes the secretion of a KCl-rich saliva in response to the neurohormone serotonin (5-HT). Because of particular morphological and physiological features, 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.

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