Localization of two genes encoding plasma membrane Ca&lt;sup&gt;2&lt;/sup&gt;&lt;sup&gt;+&lt;/sup&gt; ATPases isoforms 2 (ATP2B2) and 3 (ATP2B3) to human chromosomes 3p26→p25 and Xq28, respectively

Wang, M.G.; Yi, Hua; Hilfiker, Helene; Carafoli, Ernesto; Strehler, E.E.; McBride, O W

doi:10.1159/000133794

Cited by 40 publications

(20 citation statements)

References 11 publications

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“…Caa was mapped using a polymorphism in enzyme activity, and therefore probably represents a different isoform from that cloned as GTT3. This result is consistent with the mapping of the human gene for isoform 2 (ATP2B2) to chromosome 3p26-p25, a region that shows conservation of synteny with mouse chromosome 6 (Wang et al 1994). The mapping of clone GTT9 on MMU8 provides confirmation of the recent cytogenetic assignment of the mouse homolog of the yeast RAD23 gene to chromosome 8C3 (van der Spek et al 1996).…”

Section: Mappingsupporting

confidence: 85%

Isolation and mapping of novel mouse brain cDNA clones containing trinucleotide repeats, and demonstration of novel alleles in recombinant inbred strains.

Chambers¹,

Abbott²

1996

Genome Res.

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Abnormal expansion of trinucleotide repeats {TRs) has now been implicated in the pathogenesis of at least nine human genetic disorders, particularly those in which anticipation and/or fragile sites have been demonstrated. Anticipation, the phenomenon of increasing severity of phenotype in successive generations, has never been seen in species other than man. Nevertheless, animal models for the dynamic mutation of TRs would be extremely valuable. We have screened a mouse brain cDNA library in an attempt to identify clones representing each of the 10 possible classes of trinucleotide repeat. Thirty-seven clones were analyzed in detail. Of the 37 sequences, 18 displayed significant levels of homology with sequences in GenBank, 10 of them with human expressed sequence tags {ESTs}. We then analyzed 25 of the clones by PCR of the sequence containing the repeat in a number of different mouse strains and species to assess levels of variability of repeat length. Of the 25 clones analyzed in this way, 64% showed length variation between Mus musculus spp. and Iqus spretus, and 32% showed variation between Mus musculus musculus-derived standard laboratory inbred strains. Where variation was detected {17 repeat-containing clones in all), the gene was mapped by linkage analysis. None of the repeats isolated showed any signs of extreme expansion. However, two of the repeats were shown to have undergone size changes during the establishment of a number of recombinant inbred strains, suggesting that these repeats are at least moderately unstable.

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Section: Mappingsupporting

confidence: 85%

Isolation and mapping of novel mouse brain cDNA clones containing trinucleotide repeats, and demonstration of novel alleles in recombinant inbred strains.

Chambers¹,

Abbott²

1996

Genome Res.

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“…There are four mammalian genes that encode the different PMCA isoforms (PMCA1-4) [5][6][7] . 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] .…”

Section: Distribution Of Pmca Isoforms In the Spinal Cordmentioning

confidence: 99%

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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“…Primarily, PMCAs are activated by Ca 2+ -calmodulin, acidic phospholipids and serine/threonine phosphorylation (James et al, 1988;Enyedi et al, 1989;Falchetto et al, 1991Falchetto et al, , 1992. In addition to mediating regulation by Ca 2+ -calmodulin, the COOH-terminal region of the calcium pump has also been shown to be the target of phosphorylation by protein kinases A and C ( Roufogalis, 1995;Penniston and Enyedi, 1998) and to be affected by proteases such as calpain (Carafoli, 1994;Wang et al, 1994).…”

Section: F T L L F V G E G F F 980 Gacatcgacagtggaaggaatgctcccctgcamentioning

confidence: 99%

“…Mammalian PMCAs are encoded by four non-allelic genes located on different chromosomes, and additional isoform variants (as many as 30 in total) are generated via alternative RNA splicing of the primary gene transcripts at two major regulatory sites, one adjacent to the amino-terminal phospholipid responsive region and another within the carboxyl-terminal CaM binding domain (Olson et al, 1991;Brandt et al, 1992;Latif et al, 1993;Wang et al, 1994). The four PMCA genes appear to be very closely related in their exon-intron structure (Burk and Shull, 1992;Hilfiker et al, 1993;Kuzmin et al, 1994).…”

mentioning

confidence: 99%

Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfishProcambarus clarkiiantennal gland during molting

Gao

Wheatly

2004

Journal of Experimental Biology

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2991Intracellular Ca 2+ homeostasis is critical to eukaryotic cells due to the important role that cytoplasmic free Ca 2+ plays as a second messenger in initiating routine cellular events including excitation-contraction coupling, hormonal release, alterations in cell metabolism and growth. In general, cells attempt to keep intracellular (IC) Ca 2+ low to preserve its function as a signaling agent and to avoid cell toxicity. Studies suggest that this involves coordination between transmembrane proteins on apical, basolateral and internal [sarco/endoplasmic reticular (SER)] membranes that import and export Ca 2+ , such as channels, pumps, exchangers and binding proteins. Regulation of IC Ca 2+ is further challenged in polarized epithelial cells that vectorially transfer large amounts of Ca 2+ either in absorptive or secretory mode.The natural molting cycle of a freshwater crayfish, Procambarus clarkii, has emerged as an ideal non-mammalian model to study Ca 2+ homeostasis and the genes encoding the Ca 2+ handling proteins (Wheatly, 1999). As arthropods, crustaceans possess an external calcified cuticle that is periodically shed, enabling growth to occur. These episodes are preceded in premolt by reabsorption of Ca 2+ from the existing cuticle and deposition in storage sites (often regions of the digestive tract). Following ecdysis, there is intense pressure in postmolt to remineralize the new cuticle primarily with Ca 2+ absorbed from the external water. After calcification is completed, the animal returns to intermolt, a period during which net Ca 2+ flux is minimal. The beauty of this model system is that net Ca 2+ flux alternates from Ca 2+ balance (intermolt) to net loss (premolt) and then to significant net uptake (postmolt), offering an ideal model to examine the temporal and spatial regulation of genes coding for Ca 2+ handling proteins. Among crustaceans, the crayfish exhibits highly developed strategies for Ca 2+ homeostasis that have enabled it to evolve in freshwater, a highly inhospitable environment with respect to Ca 2+ availability (levels typically below 1·mmol·l -1 compared with 10·mmol·l -1 in seawater). Specifically, the antennal gland (kidney analog) produces a dilute urine, contributing significantly to the organism's

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Localization of two genes encoding plasma membrane Ca<sup>2</sup><sup>+</sup> ATPases isoforms 2 (ATP2B2) and 3 (ATP2B3) to human chromosomes 3p26→p25 and Xq28, respectively

Cited by 40 publications

References 11 publications

Isolation and mapping of novel mouse brain cDNA clones containing trinucleotide repeats, and demonstration of novel alleles in recombinant inbred strains.

Isolation and mapping of novel mouse brain cDNA clones containing trinucleotide repeats, and demonstration of novel alleles in recombinant inbred strains.

Role of plasma membrane calcium ATPase 2 in spinal cord pathology

Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfishProcambarus clarkiiantennal gland during molting

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