Characterization of a putative Ca2+-transporting Ca2+-ATPase in the pellicles of Paramecium tetraurelia

Wright, Mark V.; Houten, Judith L. Van

doi:10.1016/0005-2736(90)90160-p

Cited by 40 publications

(60 citation statements)

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“…On exocytosis stimulation, in Paramecium internal Ca 2+ concentration ([Ca 2+ ] i ) increases in the cell cortex, first by alveolar sac store mobilization and then by storeoperated influx of external Ca 2+ (Erxleben and Plattner 1994;Erxleben et al 1997;Klauke and Plattner 1997). As would be expected, the plasmalemmal Ca 2+ -ATPase of Paramecium is stimulated by Ca 2+ /calmodulin (CaM) (Wright and Van Houten 1990;Smith and Hennessey 1993), whereas the SERCA pump of alveolar sacs is CaM-insensitive (Stelly et al 1991;Kissmehl et al 1998). This is in agreement with recent cloning of these two types of Ca 2+ pumps from Paramecium (Elwess and Van Houten 1997;Hauser et al 1998) and reflects the situation in higher eukaryotic systems (Raeymaekers and Wuytack 1996).…”

supporting

confidence: 85%

Microdomain Arrangement of the SERCA-type Ca²⁺ Pump (Ca²⁺-ATPase) in Subplasmalemmal Calcium Stores of Paramecium Cells

Plattner

Flötenmeyer

Kissmehl

et al. 1999

J Histochem Cytochem.

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SUMMARYWe localized SERCA pumps to the inner region of alveolar sac membranes, facing the cell interior, by combining ultrastructural and biochemical methods. Immunogold labeling largely predominated in the inner alveolar sac region which displayed aggregates of intramembrane particles (IMPs). On image analysis, these represented o ligomeric arrangements of ‫ف‬ 8-nm large IMP subunits, suggesting formation of SERCA aggregates (as known from sarcoplasmic reticulum). We found not only monomers of typical molecular size ( ‫ف‬ 106 kD) but also oligomeric forms on Western blots (using anti-SERCA antibodies, also against endogenous SERCA from alveolar sacs) and on electrophoresis gelautoradiographs of 32 P-labeled phosphoenzyme intermediates. Selective enrichment of SERCA-pump molecules in the inner alveolar sac membrane region may eliminate Ca 2+ after centripetal spread observed during exocytosis activation, while the plasmalemmal Ca 2+ pump may maintain or reestablish [Ca 2+ ] in the narrow subplasmalemmal space between the outer alveolar sac membrane region and the cell membrane. We show for the first time the microzonal arrangement of SERCA molecules in a Ca 2+ store of a secretory system, an intensely discussed issue in stimulus-secretion coupling research.

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confidence: 85%

Microdomain Arrangement of the SERCA-type Ca²⁺ Pump (Ca²⁺-ATPase) in Subplasmalemmal Calcium Stores of Paramecium Cells

Plattner

Flötenmeyer

Kissmehl

et al. 1999

J Histochem Cytochem.

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“…Hyperpolarization in response to at least some organic attractants cannot be accounted for by simple K ϩ or Na ϩ efflux or Cl -influx , and indirect evidence exists to support the role of a plasma membrane Ca 2ϩ pump as the hyperpolarizing entity in chemoresponse to these attractants [Wright and Van Houten, 1990;Wright et al, 1992Wright et al, , 1993Yano et al, 1996].…”

Section: Introductionmentioning

confidence: 96%

Intracellular pH and chemoresponse to NH4+ inParamecium

Davis

Fiekers

Houten

1998

Cell Motil. Cytoskeleton

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Paramecium are attracted to ammonium chloride solutions relative to sodium chloride control solutions, but little is known about the mechanisms by which attraction is evoked. A known effect of ammonium solutions in other cell types is an alteration of intracellular pH. We show here that intracellular pH is elevated upon initial exposure to 5 mM NH 4 Cl, but appears to decline within 10 minutes, both in wild type cells and in two mutants which do not show sustained attraction to NH 4 Cl using the standard behavioral assay, the T-maze. We also present quantitative values of swimming parameters that underlie the response to NH 4 Cl.

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“…This includes a plasmamembrane Ca 2+ -ATPase [56] and a SERCA-type (sarcoplasmic/endoplasmic reticulum Ca 2+ -ATPase) Ca 2+ pump [57] whose biogenesis starts in the endoplasmic reticulum and finally is enriched in the cortical Ca 2+ stores, the "alveoli" [58][59][60]. However, experimental analysis of the SERCA [61] and calculations from the kinetics of these pumps suggest that they are less powerful regulators in maintaining a low cytoplasmic Ca 2+ concentration than extrusion of Ca 2+ ions via the contractile vacuole complex [62].…”

Section: Functional Overlap Between the V-atpase And Other Pumpsmentioning

confidence: 99%

The V-ATPase in Paramecium: functional specialization by multiple gene isoforms

Wassmer

Sehring

Kissmehl

et al. 2008

Pflugers Arch - Eur J Physiol

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The vacuolar H(+)-ATPase (V-ATPase), a multisubunit, adenosine triphosphate (ATP)-driven proton pump, is essential for numerous cellular processes in all eukaryotes investigated so far. While structure and catalytic mechanism are similar to the evolutionarily related F-type ATPases, the V-ATPase's main function is to establish an electrochemical proton potential across membranes using ATP hydrolysis. The holoenzyme is formed by two subcomplexes, the transmembraneous V(0) and the cytoplasmic V(1) complexes. Sequencing of the whole genome of the ciliate Paramecium tetraurelia enabled the identification of virtually all the genes encoding V-ATPase subunits in this organism and the studying of the localization of the enzyme and roles in membrane trafficking and osmoregulation. Surprisingly, the number of V-ATPase genes in this free-living protozoan is strikingly higher than in any other species previously studied. Especially abundant are V(0)-a-subunits with as many as 17 encoding genes. This abundance creates the possibility of forming a large number of different V-ATPase holoenzymes by combination and has functional consequences by differential targeting to various organelles.

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Characterization of a putative Ca2+-transporting Ca2+-ATPase in the pellicles of Paramecium tetraurelia

Cited by 40 publications

References 50 publications

Microdomain Arrangement of the SERCA-type Ca²⁺ Pump (Ca²⁺-ATPase) in Subplasmalemmal Calcium Stores of Paramecium Cells

Microdomain Arrangement of the SERCA-type Ca²⁺ Pump (Ca²⁺-ATPase) in Subplasmalemmal Calcium Stores of Paramecium Cells

Intracellular pH and chemoresponse to NH4+ inParamecium

The V-ATPase in Paramecium: functional specialization by multiple gene isoforms

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Characterization of a putative Ca2+-transporting Ca2+-ATPase in the pellicles of Paramecium tetraurelia

Cited by 40 publications

References 50 publications

Microdomain Arrangement of the SERCA-type Ca2+ Pump (Ca2+-ATPase) in Subplasmalemmal Calcium Stores of Paramecium Cells

Microdomain Arrangement of the SERCA-type Ca2+ Pump (Ca2+-ATPase) in Subplasmalemmal Calcium Stores of Paramecium Cells

Intracellular pH and chemoresponse to NH4+ inParamecium

The V-ATPase in Paramecium: functional specialization by multiple gene isoforms

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Product

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Microdomain Arrangement of the SERCA-type Ca²⁺ Pump (Ca²⁺-ATPase) in Subplasmalemmal Calcium Stores of Paramecium Cells

Microdomain Arrangement of the SERCA-type Ca²⁺ Pump (Ca²⁺-ATPase) in Subplasmalemmal Calcium Stores of Paramecium Cells