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the 3rd letter of the Roman alphabet (同)c
(music) the keynote of the scale of C major
a general-purpose programing language closely associated with the UNIX operating system

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carbonの化学記号
Calciumの化学記号

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/10/12 10:36:24」(JST)

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PDB Molecule of the Month pdb51_1

Ca²⁺ ATPase is a form of P-ATPase that transfers calcium after a muscle has contracted. The calcium ATPase are:^[1]

Plasma membrane Ca²⁺ ATPase (PMCA)
Sarcoplasmic reticulum Ca²⁺ ATPase (SERCA)

Plasma membrane Ca²⁺ ATPase (PMCA)[edit]

Main article: Plasma membrane calcium ATPase

Rendered image of the Ca²⁺ pump

The plasma membrane Ca²⁺ ATPase (PMCA) is a transport protein in the plasma membrane of cells that serves to remove calcium (Ca²⁺) from the cell. It is vital for regulating the amount of Ca²⁺ within cells.^[2] In fact, the PMCA is involved in removing Ca²⁺ from all eukaryotic cells.^[3] There is a very large transmembrane electrochemical gradient of Ca²⁺ driving the entry of the ion into cells, yet it is very important for cells to maintain low concentrations of Ca²⁺ for proper cell signalling; thus it is necessary for the cell to employ ion pumps to remove the Ca²⁺.^[4] The PMCA and the sodium calcium exchanger (NCX) are together the main regulators of intracellular Ca²⁺ concentrations.^[3] Since it transports Ca²⁺ into the extracellular space, the PMCA is also an important regulator of the calcium concentration in the extracellular space.^[5]

The PMCA belongs to a family of P-type primary ion transport ATPases that form an aspartyl phosphate intermediate.^[3]

The PMCA is expressed in a variety of tissues, including the brain.^[6]

Sarcoplasmic reticulum Ca²⁺ ATPase (SERCA)[edit]

Main article: SERCA

SERCA resides in the sarcoplasmic reticulum (SR) within muscle cells. It is a Ca²⁺ ATPase that transfers Ca²⁺ from the cytosol of the cell to the lumen of the SR at the expense of ATP hydrolysis during muscle relaxation.

References[edit]

^ nlm.nih.gov
^ Jensen, TP; Buckby LE; Empson RM (2004). "Expression of plasma membrane Ca2+ ATPase family members and associated synaptic proteins in acute and cultured organotypic hippocampal slices from rat.". Brain Research. Developmental Brain Research. 152 (2): 129–136. doi:10.1016/j.devbrainres.2004.06.004. PMID 15351500. |accessdate= requires |url= (help)
^ ^a ^b ^c Strehler, EE; Zacharias DA (2001). "Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps". Physiological Reviews (American Physiological Society) 81 (1): 21–50. PMID 11152753. Retrieved 2007-01-30.
^ Carafoli, E (1991). "Calcium pump of the plasma membrane". Physiological Reviews 71 (1): 129–153. PMID 1986387. Retrieved 2007-01-30.
^ Talarico Jr, EF; Kennedy BG; Marfurt CF; Loeffler KU; Mangini NJ (2005). "Expression and immunolocalization of plasma membrane calcium ATPase isoforms in human corneal epithelium.". Molecular Vision 11: 169–178. PMID 15765049.
^ Jensen, TP; Filoteo A; Knopfel T; Empson RM. (2006). "Pre-synaptic plasma membrane Ca2+ ATPase isoform 2a regulates excitatory synaptic transmission in rat hippocampal CA3". Journal of Physiology 579 (Pt 1): Published online ahead of print. doi:10.1113/jphysiol.2006.123901. PMC 2075377. PMID 17170045. 17170045. Retrieved 2007-01-13. ^{[dead link]}

External links[edit]

Calcium ATPase at the US National Library of Medicine Medical Subject Headings (MeSH)
EC 3.6.3.8
Overview at utoronto.ca
Cation transporting ATPase family in Pfam
UMich Orientation of Proteins in Membranes families/superfamily-22 - Calculated orientations of calcium ATPase in membrane

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English Journal

Ultrastructural and Immunohistochemical Localization of the Plasma Membrane Ca2+-ATPase 4 (PMCA4) in Ca2+-Transporting Epithelia.

Alexander RT1, Beggs MR1, Zamani R2, Marcussen N2, Frische S3, Dimke H4.
American journal of physiology. Renal physiology.Am J Physiol Renal Physiol.2015 Jul 15:ajprenal.00651.2014. doi: 10.1152/ajprenal.00651.2014. [Epub ahead of print]
Plasma Membrane Ca2+-ATPase's (PMCA) participate in epithelial Ca2+ transport and intracellular Ca2+ signaling. The Pmca4 isoform is enriched in distal nephron isolates and decreased in mice lacking the epithelial Ca2+ channel, Trpv5. We therefore hypothesized that Pmca4 plays a significant role in
PMID 26180241

Cytokines induce endoplasmic reticulum stress in human, rat and mouse beta cells via different mechanisms.

Brozzi F1, Nardelli TR, Lopes M, Millard I, Barthson J, Igoillo-Esteve M, Grieco FA, Villate O, Oliveira JM, Casimir M, Bugliani M, Engin F, Hotamisligil GS, Marchetti P, Eizirik DL.
Diabetologia.Diabetologia.2015 Jun 23. [Epub ahead of print]
AIMS/HYPOTHESIS: Proinflammatory cytokines contribute to beta cell damage in type 1 diabetes in part through activation of endoplasmic reticulum (ER) stress. In rat beta cells, cytokine-induced ER stress involves NO production and consequent inhibition of the ER Ca2+ transporting ATPase sarco/endopl
PMID 26099855

Biselyngbyasides, cytotoxic marine macrolides, are novel and potent inhibitors of the Ca(2+) pumps with a unique mode of binding.

Morita M1, Ogawa H2, Ohno O3, Yamori T4, Suenaga K3, Toyoshima C5.
FEBS letters.FEBS Lett.2015 Jun 4;589(13):1406-11. doi: 10.1016/j.febslet.2015.04.056. Epub 2015 May 6.
Biselyngbyasides (BLSs), macrolides from a marine cyanobacterium, are cytotoxic natural products whose target molecule is unknown. Here we report that BLSs are high affinity (Ki∼10 nM) inhibitors of Ca(2+)-pumps with a unique binding mode. The crystal structures of the Ca(2+)-pump in complex with
PMID 25957767