@misc{BaumannWalz2012,
  author    = {Baumann, Otto and Walz, Bernd},
  title     = {The blowfly salivary gland - A model system for analyzing the regulation of plasma membrane V-ATPase},
  series = {Journal of insect physiology},
  volume    = {58},
  journal   = {Journal of insect physiology},
  number    = {4},
  publisher = {Elsevier},
  address   = {Oxford},
  issn      = {0022-1910},
  doi       = {10.1016/j.jinsphys.2011.11.015},
  pages     = {450 -- 458},
  year      = {2012},
  abstract  = {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.},
  language  = {en}
}
@article{ScheweBlenauWalz2012,
  author    = {Schewe, Bettina and Blenau, Wolfgang and Walz, Bernd},
  title     = {Intracellular pH regulation in unstimulated Calliphora salivary glands is Na+ dependent and requires V-ATPase activity},
  series = {The journal of experimental biology},
  volume    = {215},
  journal   = {The journal of experimental biology},
  number    = {8},
  publisher = {Company of Biologists Limited},
  address   = {Cambridge},
  issn      = {0022-0949},
  doi       = {10.1242/jeb.063172},
  pages     = {1337 -- 1345},
  year      = {2012},
  abstract  = {Salivary gland cells of the blowfly Calliphora vicina have a vacuolar-type H+-ATPase (V-ATPase) that lies in their apical membrane and energizes the secretion of a KCl-rich primary saliva upon stimulation with serotonin (5-hydroxytryptamine). Whether and to what extent V-ATPase contributes to intracellular pH (pH(i)) regulation in unstimulated gland cells is unknown. We used the fluorescent dye BCECF to study intracellular pH(i) regulation microfluorometrically and show that: (1) under resting conditions, the application of Na+-free physiological saline induces an intracellular alkalinization attributable to the inhibition of the activity of a Na+-dependent glutamate transporter; (2) the maintenance of resting pHi is Na+, Cl-, concanamycin A and DIDS sensitive; (3) recovery from an intracellular acid load is Na+ sensitive and requires V-ATPase activity; (4) the Na+/H+ antiporter is not involved in pHi recovery after a NH4Cl prepulse; and (5) at least one Na+-dependent transporter and the V-ATPase maintain recovery from an intracellular acid load. Thus, under resting conditions, the V-ATPase and at least one Na+-dependent transporter maintain normal pH(i) values of pH.7.5. We have also detected the presence of a Na+-dependent glutamate transporter, which seems to act as an acid loader. Despite this not being a common pH(i)-regulating transporter, its activity affects steady-state pH(i) in C. vicina salivary gland cells.},
  language  = {en}
}
@article{HeindorffBlenauWalzetal.2012,
  author    = {Heindorff, Kristoffer and Blenau, Wolfgang and Walz, Bernd and Baumann, Otto},
  title     = {Characterization of a Ca2+/calmodulin-dependent AC1 adenylyl cyclase in a non-neuronal tissue, the blowfly salivary gland},
  series = {Cell calcium},
  volume    = {52},
  journal   = {Cell calcium},
  number    = {2},
  publisher = {Churchill Livingstone},
  address   = {Edinburgh},
  issn      = {0143-4160},
  doi       = {10.1016/j.ceca.2012.04.016},
  pages     = {103 -- 112},
  year      = {2012},
  abstract  = {Crosstalk between intracellular signalling pathways is a functionally important and widespread phenomenon in cell physiology across phyla. In the salivary gland of the blowfly, serotonin induces fluid secretion via parallel activation of both the InsP(3)/Ca2+ and the cAMP/PKA signalling pathways, which interact on multiple levels. We have determined the molecular identity of a link between both pathways that mediates a Ca2+-dependent rise of intracellular cAMP. Whereas hydrolysis of cAMP via phosphodiesterases is largely independent of Ca2+, cAMP synthesis by adenylyl cyclases (AC) is potentiated in a Ca2+/calmodulin (Ca2+/CaM)-dependent manner. The existence of a Ca2+/CaM-dependent AC is supported by physiological data and a molecular approach. We have cloned Cv rutabaga cDNA, encoding the first blowfly AC, and confirmed its expression in the salivary gland via reverse transcription followed by polymerase chain reaction. The putative gene product of Cv rutabaga is a Ca2+/CaM-dependent type I AC and shows highest homology to Rutabaga from Drosophila. Thus, a Ca2+/CaM-dependent AC serves as a link between the InsP(3)/Ca2+ and the cAMP/PKA signalling pathways in the salivary gland of the blowfly and might be important for the amplification and optimization of the secretory response.},
  language  = {en}
}