Morphological and functional characterization of the thoracic portion of blowfly salivary glands

Rotte, Cathleen; Baumann, Otto

doi:10.1016/j.asd.2008.01.003

Cited by 6 publications

(6 citation statements)

References 27 publications

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“…To determine the structural reorganization of the apical membrane domain during cell differentiation, cryosections through salivary glands at various developmental stages were labelled with fluorophore-tagged phalloidin. Since microplicae have actin filaments in their interior, staining with the F-actin probe phalloidin visualizes the entire apical membrane of fully differentiated secretory cells in the adult salivary gland (Zimmermann, 2000;Zimmermann et al, 2003;Rotte et al, 2008).…”

Section: Structural Differentiation Of the Apical Plasma Membranementioning

confidence: 99%

“…Subsequently, glands were chemically fixed, cryosectioned and immunostained as described in detail previously (Dames et al, 2006;Rotte et al, 2008). Fluorescence images were recorded with a Zeiss LSM 510 or a Zeiss LSM 710 confocal laser scanning microscope (Carl Zeiss Microscopy, Jena, Germany).…”

Section: Immunofluorescence Microscopymentioning

confidence: 99%

“…The salivary glands are a pair of tubules that extend through the entire abdomen and the thorax and unite and open into the oesophagus (Oschman and Berridge, 1970;Rotte et al, 2008). The abdominal region of the salivary gland, i.e.…”

Section: Introductionmentioning

confidence: 99%

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Development of apical membrane organization and V-ATPase regulation in blowfly salivary glands

Baumann

Bauer

2013

Journal of Experimental Biology

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Section: Structural Differentiation Of the Apical Plasma Membranementioning

confidence: 99%

Section: Immunofluorescence Microscopymentioning

confidence: 99%

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Development of apical membrane organization and V-ATPase regulation in blowfly salivary glands

Baumann

Bauer

2013

Journal of Experimental Biology

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“…Blowfly salivary glands are blind-ending tubules of uniformly differentiated cells arranged in a single-layered epithelium. The apical membrane, visualized by staining for actin (Zimmermann 2000;Rotte et al 2008), is deeply invaginated and forms canaliculi. Anti-PKA-RII immunoreactivity and anti-PKA-C immunoreactivity had a similar distribution in non-stimulated cells (Fig.…”

Section: Resultsmentioning

confidence: 99%

Stimulus-induced translocation of the protein kinase A catalytic subunit to the apical membrane in blowfly salivary glands

2008

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Secretion in blowfly (Calliphora vicina) salivary glands is regulated by the neurohormone serotonin (5-HT), which activates the InsP(3)/Ca(2+) pathway and the cAMP/protein kinase A (PKA) pathway in the secretory cells. The latter signaling cascade induces the activation of a vacuolar H(+)-ATPase on the apical membrane. Here, we have determined the distribution of PKA by using antibodies against the PKA regulatory subunit-II (PKA-RII) and the PKA catalytic subunit (PKA-C) of Drosophila. PKA is present in high concentrations within the secretory cells. PKA-RII and PKA-C co-distribute in non-stimulated glands, being enriched in the basal portion of the secretory cells. Exposure to 8-CPT-cAMP or 5-HT induces the translocation of PKA-C to the apical membrane, whereas the PKA-RII distribution remains unchanged. The recruitment of PKA-C to the apical membrane corroborates our hypothesis that vacuolar H(+)-ATPase, which is enriched in this membrane domain, is a target protein for PKA.

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“…Blowfly salivary glands are long tubules of a single layer of uniform epithelial cells (Oschman and Berridge, 1970;Rotte et al, 2008). Exposure of isolated glands to 5-HT induces a reversible acidification of the luminal compartment ( Fig.…”

Section: Resultsmentioning

confidence: 99%

V‐ATPase deactivation in blowfly salivary glands is mediated by protein phosphatase 2C

Voß

Blenau

Baumann

2009

Arch Insect Biochem Physiol

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The activity of vacuolar H(+)-ATPase (V-ATPase) in the apical membrane of blowfly (Calliphora vicina) salivary glands is regulated by the neurohormone serotonin (5-HT). 5-HT induces, via protein kinase A, the phosphorylation of V-ATPase subunit C and the assembly of V-ATPase holoenzymes. The protein phosphatase responsible for the dephosphorylation of subunit C and V-ATPase inactivation is not as yet known. We show here that inhibitors of protein phosphatases PP1 and PP2A (tautomycin, ocadaic acid) and PP2B (cyclosporin A, FK-506) do not prevent V-ATPase deactivation and dephosphorylation of subunit C. A decrease in the intracellular Mg(2+) level caused by loading secretory cells with EDTA-AM leads to the activation of proton pumping in the absence of 5-HT, prolongs the 5-HT-induced response in proton pumping, and inhibits the dephosphorylation of subunit C. Thus, the deactivation of V-ATPase is most probably mediated by a protein phosphatase that is insensitive to okadaic acid and that requires Mg(2+), namely, a member of the PP2C protein family. By molecular biological techniques, we demonstrate the expression of at least two PP2C protein family members in blowfly salivary glands.

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Morphological and functional characterization of the thoracic portion of blowfly salivary glands

Cited by 6 publications

References 27 publications

Development of apical membrane organization and V-ATPase regulation in blowfly salivary glands

Development of apical membrane organization and V-ATPase regulation in blowfly salivary glands

Stimulus-induced translocation of the protein kinase A catalytic subunit to the apical membrane in blowfly salivary glands

V‐ATPase deactivation in blowfly salivary glands is mediated by protein phosphatase 2C

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