Plasma membrane calcium ATPase expression in the rat spinal cord

Tachibana, Tetsuya; Ogura, Hiroyuki; Tokunaga, Atsushi; Dai, Yi; Yamanaka, Hiroki; Seino, Daisuke; Noguchi, Koichi

doi:10.1016/j.molbrainres.2004.08.001

Cited by 13 publications

(8 citation statements)

References 16 publications

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“…Studies on the cellular localization of PMCA mRNA and protein by use of in situ hybridization and immunocytochemistry, respectively, confirmed the presence of all isoforms in the spinal cord [12] . PMCA1, -2 and -3 mRNAs were expressed in neuronal cell bodies throughout the layers of the spinal cord whereas PMCA4 mRNA was localized to a small number of neurons in laminae Ⅰ-Ⅴ.…”

Section: Distribution Of Pmca Isoforms In the Spinal Cordmentioning

confidence: 76%

“…Immunocytochemistry with antibodies specific to each isoform localized staining mostly to the neuropil, although PMCA4 immunoreactivity was also found in the cell bodies of neurons in laminae Ⅱ-Ⅳ [12] . The distribution of the staining was distinct for each isoform.…”

Section: Distribution Of Pmca Isoforms In the Spinal Cordmentioning

confidence: 99%

“…PMCA1 and PMCA4 are ubiquitously expressed throughout most tissues, including the brain and the spinal cord, whereas PMCA2 and -3 are especially abundant in the spinal cord and the brain [8][9][10][11][12] . The alternative splicing of the primary PMCA transcripts generates approximately 30 variants, each with a unique distribution, cellular localization, signaling cascade and functional characteristics [9,13] .…”

Section: Distribution Of Pmca Isoforms In the Spinal Cordmentioning

confidence: 99%

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Role of plasma membrane calcium ATPase 2 in spinal cord pathology

Fakira

Elkabes²

2010

WJBC

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A number of studies have indicated that plasma membrane calcium ATPases (PMCAs) are expressed in the brain and spinal cord and could play important roles not only in the maintenance of cellular calcium homeostasis but also in the survival and function of central nervous system cells under pathological conditions. The different regional and cellular distributions of the various PMCA isoforms and splice variants in the nervous system and the diverse phenotypes of PMCA knockout mice support the notion that each isoform might play a distinct role. Especially in the spinal cord, the survival of neurons and, in particular, motor neurons could be dependent on PMCA2. This is indicated by the knockdown of PMCA2 in pure spinal cord neuronal cultures that leads to cell death via a decrease in collapsing response mediator protein 1 levels. Moreover, the progressive decline in the number of motor neurons in PMCA2-null mice and heterozygous mice further supports this notion. Therefore, the reported reduction in PMCA2 mRNA and protein levels in the inflamed spinal cord of mice affected by experimental autoimmune encephalomyelitis (EAE), an animal model of multiple sclerosis, and after spinal cord contusion injury, suggests that changes in PMCA2 expression could be a cause of neuronal pathology and death during inflammation and injury. Glutamate excitotoxicity mediated via kainate receptors has been implicated in the neuropathology of both EAE and spinal cord injury, and has been identified as a trigger that reduces PMCA2 levels in pure spinal cord neuronal cultures through degradation of the pump by calpain without affecting PMCA2 transcript levels. It remains to be determined which other stimuli modulate PMCA2 mRNA expression in the aforementioned pathological conditions of the spinal cord.

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Section: Distribution Of Pmca Isoforms In the Spinal Cordmentioning

confidence: 76%

Section: Distribution Of Pmca Isoforms In the Spinal Cordmentioning

confidence: 99%

Section: Distribution Of Pmca Isoforms In the Spinal Cordmentioning

confidence: 99%

See 1 more Smart Citation

Role of plasma membrane calcium ATPase 2 in spinal cord pathology

Fakira

Elkabes²

2010

WJBC

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“…Four major PMCA isoforms (1–4) have been identified (Carafoli, 1991; Strehler & Zacharias, 2001), and we previously showed that PMCA2 and PMCA4 are the major isoforms expressed in DRG neurons (Usachev et al 2002). In addition, strong PMCA4 immunoreactivity was detected in the superficial layers of the dorsal horn (Tachibana et al 2004), the area where the majority of TRPV1‐positive central processes terminate (Guo et al 1999; Cavanaugh et al 2011). Here we examined the functional significance of PMCAs in presynaptic boutons of DRG neurons.…”

Section: Resultsmentioning

confidence: 99%

Mitochondria and plasma membrane Ca²⁺‐ATPase control presynaptic Ca²⁺ clearance in capsaicin‐sensitive rat sensory neurons

Shutov

Kim

Houlihan

et al. 2013

The Journal of Physiology

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Key points• The first sensory synapse formed between the central processes of primary afferents and dorsal horn neurons plays an important role in controlling the flow of nociceptive information from the periphery to the CNS, and plasticity at this synapse contributes to centrally mediated pain hypersensitivity.• Although exocytosis and synaptic plasticity are regulated by presynaptic Ca 2+ , the mechanisms underlying presynaptic Ca 2+ signalling at the first sensory synapse are not well understood.• In this study we show that the plasma membrane Ca 2+ -ATPase and mitochondria are the major regulators of presynaptic Ca 2+ signalling in capsaicin-sensitive dorsal root ganglion neurons accounting for ∼47 and ∼40% of presynaptic Ca 2+ clearance, respectively.• Quantitative analysis of changes in cytosolic and mitochondrial Ca 2+ concentrations demonstrates that the mitochondrial Ca 2+ uniporter is highly sensitive to cytosolic Ca 2+ at this synapse.• These results help us understand presynaptic mechanisms at the first sensory synapse. AbstractThe central processes of primary nociceptors form synaptic connections with the second-order nociceptive neurons located in the dorsal horn of the spinal cord. These synapses gate the flow of nociceptive information from the periphery to the CNS, and plasticity at these synapses contributes to centrally mediated hyperalgesia and allodynia. Although exocytosis and synaptic plasticity are controlled by Ca 2+ at the release sites, the mechanisms underlying presynaptic Ca 2+ signalling at the nociceptive synapses are not well characterized. We examined the presynaptic mechanisms regulating Ca 2+ clearance following electrical stimulation in capsaicin-sensitive nociceptors using a dorsal root ganglion (DRG)/spinal cord neuron co-culture system.

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“…Ca 2+ -ATPase also displays ATP-dependent activity, and its role is to regulate intracellular Ca 2+ (iCa 2+ ) concentrations. This enzyme contributes to the signaling pathways triggered by this second messenger and protects cells from excitotoxic damage mediated by elevated iCa 2+ levels [13,14]. Evidence from the literature supports a decrease in both the activity and the expression of these enzymes in the development of axonal loss and MS [15][16][17].…”

Section: Introductionmentioning

confidence: 99%

Anthocyanins suppress the secretion of proinflammatory mediators and oxidative stress, and restore ion pump activities in demyelination

Carvalho

Gutierres

Bohnert

et al. 2015

The Journal of Nutritional Biochemistry

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Plasma membrane calcium ATPase expression in the rat spinal cord

Cited by 13 publications

References 16 publications

Role of plasma membrane calcium ATPase 2 in spinal cord pathology

Role of plasma membrane calcium ATPase 2 in spinal cord pathology

Mitochondria and plasma membrane Ca²⁺‐ATPase control presynaptic Ca²⁺ clearance in capsaicin‐sensitive rat sensory neurons

Anthocyanins suppress the secretion of proinflammatory mediators and oxidative stress, and restore ion pump activities in demyelination

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Plasma membrane calcium ATPase expression in the rat spinal cord

Cited by 13 publications

References 16 publications

Role of plasma membrane calcium ATPase 2 in spinal cord pathology

Role of plasma membrane calcium ATPase 2 in spinal cord pathology

Mitochondria and plasma membrane Ca2+‐ATPase control presynaptic Ca2+ clearance in capsaicin‐sensitive rat sensory neurons

Anthocyanins suppress the secretion of proinflammatory mediators and oxidative stress, and restore ion pump activities in demyelination

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Mitochondria and plasma membrane Ca²⁺‐ATPase control presynaptic Ca²⁺ clearance in capsaicin‐sensitive rat sensory neurons