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8/3/2019 Plasma Membrane Ca2
1/5
Plasma membrane Ca2+ATPaseFrom Wikipedia, the free encyclopedia
This article is about the ion transporter . For the protein assay, see Protein Misfolding Cyclic
Amplification.
Rendered image of the Ca2+ pump
The plasma membrane Ca2+ ATPase (PMCA) is a transport proteinin the plasma
membraneofcells that serves to removecalcium(Ca2+) from the cell. It is vital for regulating the
amount of Ca2+ within cells.[1] In fact, the PMCA is involved in removing Ca2+ from alleukaryotic cells.
[2] There is a very large transmembraneelectrochemical gradientof Ca2+driving the entry of theioninto
cells, yet it is very important for cells to maintain lowconcentrations of Ca2+ for propercell signalling;
thus it is necessary for the cell to employion pumps to remove the Ca2+.[3]The PMCA and thesodium
calcium exchanger(NCX) are together the main regulators ofintracellularCa2+ concentrations.[2]Since
it transports Ca2+into the extracellular space, the PMCA is also an important regulator of the calcium
concentration in theextracellular space.[4]
The PMCA belongs to a family ofP-type primary ion transport ATPases that form an aspartyl
phosphateintermediate.[2]
The PMCA is expressed in a variety oftissues, including the brain.[5]
Contents
[hide]
1 Actions
2 Structure
3 Isoforms
4 Pathology
5 History
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a.org/wiki/Brainhttp://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#cite_note-Jensen06-4http://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPasehttp://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#Actionshttp://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#Structurehttp://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#Isoformshttp://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#Pathologyhttp://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#History8/3/2019 Plasma Membrane Ca2
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6 References
7 External links
[edit]Actions
The pump is powered by thehydrolysis ofadenosine triphosphate (ATP), with a stoichiometry of one
Ca2+ion removed for each molecule of ATP hydrolysed. It binds tightly to Ca2+ ions (has a high affinity,
with aKmof 100 to 200 nM) but does not remove Ca2+ at a very fast rate.[6]This is in contrast to
the NCX, which has a low affinity and a high capacity. Thus, the PMCA is effective at binding
Ca2+ even when itsconcentrations within the cell are very low, so it is suited for maintaining Ca2+ at its
normally very low levels.[3]Calcium is an importantsecond messenger, so its levels must be kept low in
cells to prevent noise and keep signalling accurate.[7] The NCX is better suited for removing large
amounts of Ca2+ quickly, as is needed inneurons after anaction potential. Thus the activities of the
two types of pump complement each other.
The PMCA functions in a similar manner to other p-type ion pumps.[3]ATP transfers a phosphate to the
PMCA, which forms a phosphorylated intermediate.[3]
Ca2+/calmodulinbinds and further activates the PMCA, increasing the affinity of the protein's Ca2+-
binding site 20 to 30 times.[6]Calmodulin also increases the rate at which the pump extrudes Ca2+ from
the cell, possibly up to tenfold.[3]
In brain tissue, it has been postulated that certain types of PMCA are important for
regulatingsynapticactivity, since the PMCA is involved in regulating the amount of calcium within the
cell at the synapse,[5]and Ca2+ is involved in release ofsynaptic vesicles.
[edit]Structure
The structure of the PMCA is similar to that of theSERCA calcium pumps, which are responsible for
removing calcium from the cytoplasm into the lumen of thesarcoplasmic reticulum.[2] It is thought that
the PMCA pump has 10 segments that cross the plasma membrane, with both Cand N termini on the
inside of the cell.[2] At the C terminus, there is a long "tail" of between 70 and 200amino acids in
length.[2] This tail is thought to be responsible for regulation of the pump.[2]
[edit]Isoforms
There are fourisoforms of PMCA, called PMCA 1 through 4. [5]
ATP2B1- PMCA1
ATP2B2- PMCA2
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rg/wiki/Plasma_membrane_Ca2%2B_ATPase#cite_note-6http://en.wikipedia.org/wiki/Neuronhttp://en.wikipedia.org/wiki/Action_potentialhttp://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#cite_note-Carafoli-2http://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#cite_note-Carafoli-2http://en.wikipedia.org/wiki/Calmodulinhttp://en.wikipedia.org/wiki/Binding_sitehttp://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#cite_note-Siegel-5http://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#cite_note-Carafoli-2http://en.wikipedia.org/wiki/Synapsehttp://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#cite_note-Jensen06-4http://en.wikipedia.org/wiki/Synaptic_vesiclehttp://en.wikipedia.org/w/index.php?title=Plasma_membrane_Ca2%2B_ATPase&action=edit§ion=2http://en.wikipedia.org/wiki/SERCAhttp://en.wikipedia.org/wiki/Sarcoplasmic_reticulumhttp://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#cite_note-Strehler-1http://en.wikipedia.org/wiki/C-terminushttp://en.wikipedia.org/wiki/N_terminushttp://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#cite_note-Strehler-1http://en.wikipedia.org/wiki/Amino_acidhttp://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#cite_note-Strehler-1http://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#cite_note-Strehler-1http://en.wikipedia.org/w/index.php?title=Plasma_membrane_Ca2%2B_ATPase&action=edit§ion=3http://en.wikipedia.org/wiki/Isoformhttp://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#cite_note-Jensen06-4http://en.wikipedia.org/wiki/ATP2B1http://en.wikipedia.org/wiki/ATP2B28/3/2019 Plasma Membrane Ca2
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ATP2B3- PMCA3
ATP2B4- PMCA4
Each isoform is coded by a different gene and is expressed in different areas of the body.[5]Alternate
splicing of the mRNA transcripts of these genes results in different subtypes of these isoforms.[2]Over
20 splice variants have been identified so far.[2]
Three PMCA isoforms, PMCA1, PMCA2, and PMCA3, occur in the brain in varying distributions.
[6] PMCA1 is ubiquitous throughout alltissues in humans, and without it embryos do not survive.[4] Lack
of PMCA4, which is also very common in many tissues, is survivable, but leads to infertility in males.
[4] PMCA types 2 and 3 are activated more quickly and are, therefore, better suited to excitable cell
types such as those in nervous and muscle tissue, which experiences large influxes of Ca2+ when
excited.[5] PMCA types 1, 2, and 4 have been found inglial cells called astrocytesin mammals, though
it was previously thought that only the NCX was present in glia.[8]
Astrocytes help to maintain ionic
balance in the extracellular space in the brain.
Knock-out of PMCA2 causes inner earproblems, including hearing loss and problems withbalance.[9]
PMCA4 exists incaveolae.[9]Isoform PMCA4b interacts with nitric oxide synthase and reduces
synthesis ofnitric oxideby that enzyme.[9]
PMCA isoform 4 has a molecular weight of 134,683, calculated from its sequence.[10] This is in good
agreement with the results of SDS gel electrophoresis.[11]
[edit]
PathologyWhen the PMCA fails to function properly, disease can result. Improperly functioning PMCA proteins
have been found associated with conditions such as sensorineural deafness,diabetes,
andhypertension.[4]
Inexcitotoxicity, a process in which excessive amounts of
the neurotransmitterglutamateoveractivate neurons, resulting in excessive influx of Ca2+ into cells, the
activity of the PMCA may be insufficient to remove the excess Ca2+.
A May 2010 online press release from the Yale University School of Medicine noted that persistent
PMCA2 expression in breast cancers lowers calcium levels inside malignant cells, allowing them to
avoid controlled cell death (apoptosis), which would be the norm otherwise. According to Dr. John
Wysolmerski, M.D., professor of endocrinology and lead author of the study (which will appear in the
online early edition of the Proceedings of the National Academy of Sciences), such tumors are also
usually positive for the HER2 protein and have a tendency to involve the lymph nodes, making the
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rg/wiki/Enzymehttp://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#cite_note-Schuh-8http://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#cite_note-9http://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#cite_note-10http://en.wikipedia.org/w/index.php?title=Plasma_membrane_Ca2%2B_ATPase&action=edit§ion=4http://en.wikipedia.org/wiki/Sensorineural_deafnesshttp://en.wikipedia.org/wiki/Diabeteshttp://en.wikipedia.org/wiki/Hypertensionhttp://en.wikipedia.org/wiki/Plasma_membrane_Ca2%2B_ATPase#cite_note-Talarico-3http://en.wikipedia.org/wiki/Excitotoxicityhttp://en.wikipedia.org/wiki/Neurotransmitterhttp://en.wikipedia.org/wiki/Glutamatehttp://en.wikipedia.org/wiki/Neuron8/3/2019 Plasma Membrane Ca2
4/5
prognosis markedly worse. These breast cancers are more common among young women, which
could explain why they often have worse prognoses than other postmenopausal women.[12]
[edit]History
PMCAs were first discovered in the 1960s in the membranes ofred blood cells.[2]The presence of an
ATPase was discovered in the membranes in 1961, and then in 1966 it was discovered that these
ATPases pump Ca2+ out of the cytosol.[3]
PMCA was first purified from red blood cell membranes in 1979 [13][14]
[edit]References
1. ^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.PMID15351500.
2. ^ abcdefghijStrehler, EE; Zacharias DA (2001)."Role of alternative splicing in
generating isoform diversity among plasma membrane calcium pumps".Physiological
Reviews (American Physiological Society) 81 (1): 2150. PMID11152753. Retrieved 2007-01-30.
3. ^ abcdef Carafoli, E (1991)."Calcium pump of the plasma membrane".Physiological
Reviews71 (1): 129153.PMID1986387. Retrieved 2007-01-30.
4. ^ abcdTalarico 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 Vision11: 169178. PMID15765049.
5. ^ abcde 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: Published online ahead of print. 17170045. Retrieved 2007-01-13.[dead
link]
6. ^ abc Siegel, GJ; Agranoff BW, Albers RW, Fisher SK, Uhler MD, editors (1999). Basic
Neurochemistry: Molecular, Cellular, and Medical Aspects. 6th ed. Philadelphia:
Lippincott,Williams & Wilkins. Retrieved on January 13, 2007.
7. ^Burette, A; Weinberg RJ (2007). "Perisynaptic organization of plasma membrane
calcium pumps in cerebellar cortex". Journal of Comparative Neurology500 (6): 1127
1135.doi:10.1002/cne.21237.PMID17183553.
8. ^Fresu, L; Dehpour A, Genazzani AA, Carafoli E, Guerini D (1999). "Plasma membrane
calcium ATPase isoforms in astrocytes". Glia28 (2): 150155. doi:10.1002/(SICI)1098-
1136(199911)28:23.0.CO;2-7.PMID10533058.
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Plasma membrane Ca2+ATPase
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