A sarco/endoplasmic reticulum Ca(2+)-ATPase 3-type Ca2+ pump is expressed in platelets, in lymphoid cells, and in mast cells.

Wuytack, Frank; Papp, Béla; Verboomen, Hilde; Raeymaekers, Luc; Dode, Leonard; Bobe, Régis; Enouf, Jocelyne; Bokkala, S; Authi, Kalwant S.; Casteels, Rik

doi:10.1016/s0021-9258(17)42273-3

Cited by 195 publications

(32 citation statements)

References 23 publications

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“…With anti-ratSerca 3 Abs, some label was found in the cytoplasm (Figure 6). This is compatible with their crossreactivity with a potential SERCA isoform in the ER, in agreement with the distribution of the original antigen in some other cell types (Wuytack et al 1994). Anti-PtSerca(peptide) Abs clearly labeled alveolar sacs on their lateral side (upper part of Figure 7) and IM-AS regions where they emerge at the section surface (lower part of Figure 7), whereas they hardly recognize any internal structures beyond alveolar sacs.…”

Section: Resultssupporting

confidence: 87%

“…The following Abs were used. Established rabbit Abs (diluted 1:15 in PBS) against the C-terminal region (amino acid residues 987-999) of rat SERCA Type 3 (Wuytack et al 1994) obtained from F. Wuytack (Louvain, Belgium) were used, because these Abs specifically recognize a ∼106 kD SERCA in AS fractions (Figure 2). For further specification we used chicken Abs against the PtSERCA sequence described for alveolar sacs in Paramecium (Hauser et al 1998).…”

Section: Methodsmentioning

confidence: 99%

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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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Section: Resultssupporting

confidence: 87%

Section: Methodsmentioning

confidence: 99%

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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“…Given the importance of autonomous pacemaking activity and cytosolic Ca 2+ oscillations to mDA neuronal physiology (Zampese and Surmeier, 2020), the SNr enrichment of Atp2a3 mRNA, which encodes the sarco/endoplasmic reticulum Ca 2+ -ATPase isoform 3 (SERCA3), is of particular interest. SERCA3 is predominantly expressed in hematopoietic and endothelial cells (Bobe et al, 1994; Burk et al, 1989; Wuytack et al, 1994), with cerebellar Purkinje neurons being the only neuronal population previously demonstrated to express SERCA3 (Baba-Aïssa et al, 1996). Our RiboTag data indicate translation of Atp2a3/SERCA3 in the SNr, SNc, and VTA, although relative abundance was highest in the SNr ( Figure 5E ).…”

Section: Resultsmentioning

confidence: 99%

Subcellular and regional localization of mRNA translation in midbrain dopamine neurons

Hobson

Kong

Angelo

et al. 2021

Preprint

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Local translation within excitatory and inhibitory neurons is involved in neuronal development and synaptic plasticity. Despite the extensive dendritic and axonal arborizations of central monoaminergic neurons, the subcellular localization of protein synthesis is not well-characterized in these populations. Here, we investigated mRNA localization and translation in midbrain dopaminergic (mDA) neurons, cells with enormous axonal and dendritic projections, both of which exhibit stimulation-evoked dopamine (DA) release. Using highly-sensitive ribosome-bound RNA-sequencing and imaging approaches in mDA axons, we found no evidence for axonal mRNA localization or translation. In contrast, mDA neuronal dendritic projections into the substantia nigra reticulata (SNr) contain ribosomes and mRNAs encoding the major components of DA synthesis, release, and reuptake machinery. Surprisingly, we also observed dendritic localization of mRNAs encoding synaptic vesicle-related proteins, including those involved in vesicular exocytic fusion. Our results are consistent with a role for local translation in the regulation of DA release from dendrites, but not from axons. Our translatome data further defined a molecular signature of the sparse mDA neurons resident in the SNr, including enrichment of Atp2a3/SERCA3, an ER calcium pump previously undescribed in mDA neurons.

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“…A new rationale for these distinct roles of multiple Ca# + pools has come from evidence for a plurality of sarco\ endoplasmic reticulum Ca# + ATPases (SERCAs), which take up Ca# + into Ca# + pools. First, human platelets co-express the 100 kDa ubiquitous SERCA 2b [9], the polyclonal antibody N 89-recognizable 97 kDa SERCA 3a [10,11] and the monoclonal antibody PL\IM 430-recognizable 97 kDa SERCA 3b isoform [12][13][14][15]. Secondly, this latter isoform was found to be associated precisely with the IP $ -sensitive Ca# + pool.…”

Section: Introductionmentioning

confidence: 98%

Platelet sarco/endoplasmic reticulum Ca2+ATPase isoform 3b and Rap 1b: interrelation and regulation in physiopathology

Lacabaratz

Corvazier

Kovàcs³

et al. 1998

Biochemical Journal

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Platelet Ca2+ signalling involves intracellular Ca2+ pools, whose content is controlled by sarco/endoplasmic reticulum Ca2+ATPases (SERCAs). Among these, a key role is played by the inositol trisphosphate-sensitive Ca2+ pool, associated with the SERCA 3b isoform. We have investigated the control of this Ca2+ pool through the cAMP-dependent phosphorylation of the GTP-binding protein, Rap (Ras-proximate) 1b. We first looked for this Ca2+ pool target of regulation by studying the expression of the different SERCA and Rap 1 proteins in human platelets and various cell lines, by Western blotting and reverse transcription-PCR. Since co-expression of Rap 1b and SERCA 3b was obtained, we looked for their protein-protein interaction as a function of the cAMP-dependent phosphorylation of Rap 1b. Co-immunoprecipitations of SERCA 3b and Rap 1b proteins were found in the absence of phosphorylation, induced by the catalytic subunit of the cAMP-dependent protein kinase (csPKA). In contrast, upon pre-treatment of platelet membranes with csPKA, the SERCA 3b dissociated from the Rap 1b protein, in agreement with a role of its phosphorylated state in their interaction. Finally, we looked for adaptation of this complex in a platelet pathological model of hypertension. We investigated the expression of both proteins, as well as the cAMP-dependent phosphorylation of Rap 1b and SERCA 3b activity in platelets from control normotensive Wistar-Kyoto rats and from spontaneously hypertensive rats (SHRs). A decrease in SERCA 3b activity was associated with a decrease in Rap 1b endogenous phosphorylation in SHR platelets, consistent with a functional role in the regulation of the SERCA 3b-associated Ca2+ pool.

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A sarco/endoplasmic reticulum Ca(2+)-ATPase 3-type Ca2+ pump is expressed in platelets, in lymphoid cells, and in mast cells.

Cited by 195 publications

References 23 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

Subcellular and regional localization of mRNA translation in midbrain dopamine neurons

Platelet sarco/endoplasmic reticulum Ca2+ATPase isoform 3b and Rap 1b: interrelation and regulation in physiopathology

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A sarco/endoplasmic reticulum Ca(2+)-ATPase 3-type Ca2+ pump is expressed in platelets, in lymphoid cells, and in mast cells.

Cited by 195 publications

References 23 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

Subcellular and regional localization of mRNA translation in midbrain dopamine neurons

Platelet sarco/endoplasmic reticulum Ca2+ATPase isoform 3b and Rap 1b: interrelation and regulation in physiopathology

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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