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SERCA2Sarcoplasmic Endoplasmic Reticular Calcium ATPase 2
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Since intracellular [Ca.sup.2+] in cardiac cells is maintained by [Ca.sup.2+] influx (through L-type [Ca.sup.2+] channels; the primary trigger for SR [Ca.sup.2+] release) and efflux (through NCX; the major pathway for [Ca.sup.2+] efflux from the cell) [64], as well as [Ca.sup.2+] release (via the ryanodine receptors) and uptake by both SR (through SERCA2) and mitochondria, it is possible that the observed differences in these results may be attributed to differential changes in [Ca.sup.2+] transport activities in these organelles.
Inhibition of SERCA activity is coupled to a small decrease in SERCA2 protein expression levels in HG culture conditions (Figures 7(c) and 7(d)).
Protein aggregation of SERCA2 mutants associated with Darier disease elicits ER stress and apoptosis in keratinocytes.
In hyperthyroidism, at rest, myocardial contractility has been already increased due to molecular changes as altered synthesis of MHC, increase of SERCA2 expression.
In that trial, a gene known as SERCA2 is delivered via an inert virus - a modified virus without infectious particles.
More compellingly, the ATP2A2 gene that is mutated in Darier's disease encodes SERCA2.
Three different SERCA genes were identified-SERCA1, SERCA2, and SERCA3.
Such changes may be modulated by calcium release channels (RYR2) and calcium transporting ATPases (SERCA2) on the sarcoplasmic reticulum (SR) and by sarcolemmal proteins that traffic between caveolae and the rest of the membrane.
(1) It is inherited in an autosomal dominant fashion, resulting from a mutation in chromosome 12q23-q24.1, which encodes the gene ATP 2A2, which in turn encodes a SERCA2 (sarco/endoplasmic reticulum calcium)-ATPase pump.
Tmem64 also interacts with SERCA2 through tyrosine-based activation motif (ITAM) that has a common Fc receptor gamma subunit (FCR[gamma]) and DNAX-activating protein 12 (DAP12).
Ca(2+)-Clock-dependent pacemaking in the sinus node is impaired in mice with a cardiac specific reduction in SERCA2 abundance.
The activity of sarcoplasmic reticulum calcium adenosine triphosphatase, that is, SERCA2, and calsequestrin is drastically decreased during aging [47, 48], due to the lower level of expression of these proteins.