Plasma membrane Ca2+-ATPase isoforms: distribution of mRNAs in rat brain by in situ hybridization

Stahl, William L.; Eakin, Thomas J.; Owens, James W. M.; Breininger, John F.; Filuk, Peter E.; Anderson, William R.

doi:10.1016/0169-328x(92)90229-5

Cited by 108 publications

(67 citation statements)

References 35 publications

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“…Scale bar ϭ 12 m. expression, the increase observed from E10 to P0 in chick cerebellum was similar to the up-regulation reported from P2 to P30 in developing rat cerebellum (Brandt and Neve, 1992), which has a postnatal development (Armengol and Sotelo, 1991). The high amount of PMCA2 variants observed in the last stages of development is similar to that reported in adult rat cerebellum (Stahl et al, 1992;Filoteo et al, 1997;Stauffer et al, 1997). By contrast, the content of variants PMCA3a and 3b was quite different at each stage, although their expression levels did not change during development.…”

Section: (P0) Acegsupporting

confidence: 73%

“…1). The low abundance of PMCA1 with respect to PMCA2 and 3 in chick cerebellum has also been reported in adult rat cerebellum (Stahl et al, 1992;Filoteo et al, 1997;Burette et al, 2003). In addition, variants 1a and 1b showed a different pattern of expression during neural development that can be compared with that reported in developing rat brain (Brandt and Neve, 1992;Strehler and Zacharias, 2001;Kip et al, 2006).…”

Section: Discussionmentioning

confidence: 88%

“…These interneurons establish inhibitory synapses with different regions of Purkinje cells (Palay and Chan-Palay, 1974). On the contrary, PMCA2 was the only isoform identified in mature granule cells of chick cerebellum, although the presence of PMCA1 and 3, and even PMCA4, have been reported in granule cell of adult rat cerebellum (Stahl et al, 1992;Stauffer et al, 1997;Burette et al, 2003).…”

Section: (P0) Acegmentioning

confidence: 97%

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Developmental distribution of plasma membrane Ca²⁺‐ATPase isoforms in chick cerebellum

Sepúlveda¹,

Hidalgo‐Sánchez²,

Marcos³

et al. 2007

Developmental Dynamics

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The plasma membrane Ca 2؉ -ATPase (PMCA) is highly expressed in the nervous system, but little information is available about its implication in neuronal development. We have analyzed the expression and localization of different isoforms of PMCA in membrane vesicles and sections of chick cerebellum from embryonic day 10 to hatching. We found that the relative amount of each PMCA isoform and their spatiotemporal distribution in the cerebellum are directly linked to precise cellular types during the cerebellar maturation, even in a non-neural tissue as choroid plexus. Purkinje cells contain the highest diversity of PMCA isoforms of the cerebellar cortex since the moment of its morphogenesis. From embryonic day 15, the PMCA2 was highly expressed in the whole Purkinje cell, while PMCAs 1 and 3 had a more restricted distribution in the soma and dendritic branches, and these distributions were evolving according with cell maturation. Other cellular types seem to contain a specific combination of isoforms, but with a well-defined distribution pattern at late moments of development. Thus, PMCAs 1 and 3 were located in the soma of molecular layer interneurons, and only the PMCA2 was observed in granule cells at hatching. Furthermore, PMCA isoforms are also expressed in cellular compartments characterized by a high amount of synapses, suggesting a key role of these proteins in synaptogenesis and in the maturation of neuronal electrophysiological properties.

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Section: (P0) Acegsupporting

confidence: 73%

Section: Discussionmentioning

confidence: 88%

Section: (P0) Acegmentioning

confidence: 97%

See 1 more Smart Citation

Developmental distribution of plasma membrane Ca²⁺‐ATPase isoforms in chick cerebellum

Sepúlveda¹,

Hidalgo‐Sánchez²,

Marcos³

et al. 2007

Developmental Dynamics

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“…Tissue distribution of the PMCA isoforms in human and rat has been examined by S1 nuclease protection, polymerase chain reaction, in situ hybridization, and at the protein level by Western blot analysis (8,10,21). These studies have shown that PMCA1 and 4 are broadly distributed, leading to the suggestion that they represent the "housekeeping" isoforms.…”

Section: Discussionmentioning

confidence: 99%

Plasma Membrane Ca2+ Pump Isoforms 2a and 2b Are Unusually Responsive to Calmodulin and Ca2+

Elwess¹,

Filoteo²,

Enyedi³

et al. 1997

Journal of Biological Chemistry

118

103

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The full-length a and b variants of the rat plasma membrane calcium pump, isoform 2 (rPMCA2a and rPMCA2b), were constructed and expressed in COS-7 cells. To characterize these isoforms, calcium transport was determined in a microsomal fraction. Both rPMCA2a and rPMCA2b had a much higher affinity for calmodulin than the corresponding forms of hPMCA4, and rPMCA2b had the highest affinity among the isoforms that have been tested so far. When analyzed at a relatively high calmodulin concentration, rPMCA2b and, to a lesser extent, rPMCA2a showed higher apparent calcium affinity; i.e. they were more active at lower Ca 2؉ concentrations than hPMCA4b. This indicates that these two variants of rat isoform 2 will tend to maintain a lower free cytosolic Ca 2؉ level in cells where they are expressed. Both variants also showed a higher level of basal activity (in the complete absence of calmodulin) than hPMCA4b, a property which would reinforce their ability to maintain a low free cytosolic Ca 2؉ concentration. Experiments designed to determine the source of the higher apparent Ca 2؉ affinity of rPMCA2b showed that it came from the properties of the carboxyl terminus, rather than from any difference in the catalytic core.The plasma membrane Ca 2ϩ pump plays a key role in controlling the intracellular Ca 2ϩ concentration. This P-type ATPase is regulated by calmodulin and is responsible for the ATP powered removal of Ca 2ϩ from eukaryotic cells (1). The plasma membrane Ca 2ϩ pump (PMCA) 1 has a low level of activity in the absence of calmodulin. Calmodulin binds to an autoinhibitory domain (the C domain), and increases both the maximum velocity of the pump and the apparent Ca 2ϩ affinity.To date, at least four different genes have been found which encode for PMCA (2). Additional variability is obtained by alternate splices occurring at two sites in the pump (3-7). In each of the four genes, the alternative splice sites (8) are located in the middle of the cytosolic loop between transmembrane domains 2 and 3 (splice site A) (9) and downstream of the last transmembrane domain, in the middle of the calmodulinbinding domain (splice site C) (9 -11). The first 18 amino acids of the calmodulin-binding domain are conserved for all PMCA isoforms, but the presence of the alternative RNA splice site in the middle of this region (at splice site C) changes the remainder of the calmodulin-binding domain as well as the carboxyl terminus (10). The isoforms whose mRNA contains a spliced-in exon are called "a," while those isoforms lacking the additional exon are called "b." 2 The a variants of the isoforms have a less basic calmodulin-binding domain as well as a different carboxyl terminus than the b variants. When synthetic peptides corresponding to representative a and b forms of the calmodulinbinding domain were compared, the b form of the peptide showed a 10-fold higher affinity for calmodulin than the a form of the peptide (12). Additionally, full-length isoforms hPMCA4a and hPMCA4b were overexpressed in COS-1 cells and the calmodulin-res...

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“…PMCA1 and PMCA4 are ubiquitous; PMCA1 is essential for the survival of the embryos, while the lack of PMCA4, the main calcium efflux protein in sperms, results in male infertility [2,3]. The rapidly activated PMCA2 and PMCA3 transporters are predominantly present in the nervous system and muscle [4].…”

Section: Introductionmentioning

confidence: 99%

Decreased calcium pump expression in human erythrocytes is connected to a minor haplotype in the ATP2B4 gene

et al. 2017

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a b s t r a c tPlasma membrane Ca 2+ -ATPases are key calcium exporter proteins in most tissues, and PMCA4b is the main calcium transporter in the human red blood cells (RBCs). In order to assess the expression level of PMCA4b, we have developed a flow cytometry and specific antibody binding method to quantitatively detect this protein in the erythrocyte membrane. Interestingly, we found several healthy volunteers showing significantly reduced expression of RBC-PMCA4b. Western blot analysis of isolated RBC membranes confirmed this observation, and indicated that there are no compensatory alterations in other PMCA isoforms. In addition, reduced PMCA4b levels correlated with a lower calcium extrusion capacity in these erythrocytes. When exploring the potential genetic background of the reduced PMCA4b levels, we found no missense mutations in the ATP2B4 coding regions, while a formerly unrecognized minor haplotype in the predicted second promoter region closely correlated with lower erythrocyte PMCA4b protein levels. In recent GWA studies, SNPs in this ATP2B4 haplotype have been linked to reduced mean corpuscular hemoglobin concentrations (MCHC), and to protection against malaria infection. Our data suggest that an altered regulation of gene expression is responsible for the reduced RBC-PMCA4b levels that is probably linked to the development of human disease-related phenotypes.

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Plasma membrane Ca2+-ATPase isoforms: distribution of mRNAs in rat brain by in situ hybridization

Cited by 108 publications

References 35 publications

Developmental distribution of plasma membrane Ca²⁺‐ATPase isoforms in chick cerebellum

Developmental distribution of plasma membrane Ca²⁺‐ATPase isoforms in chick cerebellum

Plasma Membrane Ca2+ Pump Isoforms 2a and 2b Are Unusually Responsive to Calmodulin and Ca2+

Decreased calcium pump expression in human erythrocytes is connected to a minor haplotype in the ATP2B4 gene

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Plasma membrane Ca2+-ATPase isoforms: distribution of mRNAs in rat brain by in situ hybridization

Cited by 108 publications

References 35 publications

Developmental distribution of plasma membrane Ca2+‐ATPase isoforms in chick cerebellum

Developmental distribution of plasma membrane Ca2+‐ATPase isoforms in chick cerebellum

Plasma Membrane Ca2+ Pump Isoforms 2a and 2b Are Unusually Responsive to Calmodulin and Ca2+

Decreased calcium pump expression in human erythrocytes is connected to a minor haplotype in the ATP2B4 gene

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Developmental distribution of plasma membrane Ca²⁺‐ATPase isoforms in chick cerebellum

Developmental distribution of plasma membrane Ca²⁺‐ATPase isoforms in chick cerebellum