Search results for "Plasma Membrane Calcium-Transporting ATPases"

showing 4 items of 4 documents

The role of Plasma Membrane Calcium ATPases (PMCAs) in neurodegenerative disorders

2017

Selective degeneration of differentiated neurons in the brain is the unifying feature of neurodegenerative disorders such as Parkinson's disease (PD) or Alzheimer's disease (AD). A broad spectrum of evidence indicates that initially subtle, but temporally early calcium dysregulation may be central to the selective neuronal vulnerability observed in these slowly progressing, chronic disorders. Moreover, it has long been evident that excitotoxicity and its major toxic effector mechanism, neuronal calcium overload, play a decisive role in the propagation of secondary neuronal death after acute brain injury from trauma or ischemia. Under physiological conditions, neuronal calcium homeostasis is…

0301 basic medicineCalcium pumpExcitotoxicitychemistry.chemical_elementCalciumProtein oxidationmedicine.disease_causeProtein Structure SecondaryPlasma Membrane Calcium-Transporting ATPases03 medical and health sciences0302 clinical medicinemedicineAnimalsHumansPhylogenyCalcium metabolismMembrane potentialChemistryGeneral NeuroscienceNeurodegenerationNeurodegenerative Diseasesmedicine.diseaseCytosol030104 developmental biologyNeuroscience030217 neurology & neurosurgeryNeuroscience Letters
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Separation of presynaptic Cav2 and Cav1 channel function in synaptic vesicle exo- and endocytosis by the membrane anchored Ca2+ pump PMCA

2021

Significance Synaptic vesicle (SV) release from presynaptic terminals requires nanometer precise control of action potential (AP)–triggered calcium influx through voltage-gated calcium channels (VGCCs). SV recycling also depends on calcium signals, though in different spatiotemporal domains. Mechanisms for separate control of SV release and recycling by AP-triggered calcium influx remain elusive. Here, we demonstrate largely independent regulation of release and recycling by two different populations of VGCCs (Cav2, Cav1), identify Cav1 as one of potentially multiple calcium entry routes for endocytosis regulation, and show functional separation of simultaneous calcium signals in the nanome…

Drosophila ; Dmca1D ; cacophony ; PMCA ; synapse0301 basic medicine570ATPasecacophonyPresynaptic TerminalsAction PotentialsEndocytosisDmca1DSynaptic vesicleExocytosis03 medical and health scienceschemistry.chemical_compoundGlutamatergicPlasma Membrane Calcium-Transporting ATPases0302 clinical medicinePMCAsynapsemedicineAnimalsDrosophila ProteinsAxonNeurotransmitterProbabilityMotor NeuronsMultidisciplinaryVoltage-dependent calcium channelbiologyCell Membrane424500 Naturwissenschaften und Mathematik::570 Biowissenschaften; Biologie::570 Biowissenschaften; BiologieBiological SciencesEndocytosisCell biologyElectrophysiology030104 developmental biologymedicine.anatomical_structureDrosophila melanogasterchemistryReceptors Glutamatebiology.proteinDrosophilaCalciumCalcium ChannelsSynaptic Vesicles030217 neurology & neurosurgeryNeuroscienceProceedings of the National Academy of Sciences of the United States of America
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Downregulation of PMCA2 increases the vulnerability of midbrain neurons to mitochondrial complex I inhibition

2013

Parkinson's disease is an age-associated disorder characterized by selective degeneration of dopaminergic neurons. The molecular mechanisms underlying the selective vulnerability of this subset of neurons are, however, not fully understood. Employing SH-SY5Y neuroblastoma cells and primary mesencephalic neurons, we here demonstrate a significant increase in cytosolic calcium after inhibition of mitochondrial complex I by means of MPP(+), which is a well-established environmental toxin-based in vitro model of Parkinson's disease. This increase in calcium is correlated with a downregulation of the neuron-specific plasma membrane Ca(2+)-ATPase isoform 2 (PMCA2). Interestingly, two other import…

Male1-Methyl-4-phenylpyridiniummedicine.medical_specialtySERCADown-Regulationchemistry.chemical_elementCalciumToxicologyCREBRats Sprague-DawleyPlasma Membrane Calcium-Transporting ATPaseschemistry.chemical_compoundDownregulation and upregulationMesencephalonCell Line TumorInternal medicinemedicineAnimalsHumansCyclic AMP Response Element-Binding ProteinNeuronsCalcium metabolismElectron Transport Complex IbiologyGeneral NeuroscienceMPTPNeurodegenerationmedicine.diseaseRatsEndocrinologychemistrybiology.proteinCalciumsense organsIntracellularNeuroToxicology
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Plasma membrane Ca2+ ATPase 4 is required for sperm motility and male fertility.

2004

Calcium and Ca(2+)-dependent signals play a crucial role in sperm motility and mammalian fertilization, but the molecules and mechanisms underlying these Ca(2+)-dependent pathways are incompletely understood. Here we show that homozygous male mice with a targeted gene deletion of isoform 4 of the plasma membrane calcium/calmodulin-dependent calcium ATPase (PMCA), which is highly enriched in the sperm tail, are infertile due to severely impaired sperm motility. Furthermore, the PMCA inhibitor 5-(and-6)-carboxyeosin diacetate succinimidyl ester reduced sperm motility in wild-type animals, thus mimicking the effects of PMCA4 deficiency on sperm motility and supporting the hypothesis of a pivot…

MaleTime FactorsBiochemistryMiceTestisProtein IsoformsCloning MolecularCation Transport Proteinsreproductive and urinary physiologySperm motilityMice KnockoutRecombination GeneticReverse Transcriptase Polymerase Chain ReactionPlasma Membrane Calcium-Transporting ATPasesFluoresceinsTransport proteinCell biologyBlotting SouthernBiochemistrySperm Motilityendocrine systemDNA ComplementaryGenotypeBlotting WesternMolecular Sequence Datachemistry.chemical_elementSuccinimidesCalcium-Transporting ATPasesFertilization in VitroCalciumBiologyPlasma Membrane Calcium-Transporting ATPasesAnimalsHumansMolecular BiologyFluorescent DyesCalcium metabolismModels Geneticurogenital systemCell BiologyBlotting NorthernSpermProtein Structure TertiaryRatsCalcium ATPaseAlternative SplicingFertilitychemistryMicroscopy FluorescencePlasma membrane Ca2+ ATPaseCalciumThe Journal of biological chemistry
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