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ATPase, Ca++ transporting, cardiac muscle, slow twitch 2

This gene encodes one of the SERCA Ca(2+)-ATPases, which are intracellular pumps located in the sarcoplasmic or endoplasmic reticula of muscle cells. This enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol into the sarcoplasmic reticulum lumen, and is involved in regulation of the contraction/relaxation cycle. Mutations in this gene cause Darier-White disease, also known as keratosis follicularis, an autosomal dominant skin disorder characterized by loss of adhesion between epidermal cells and abnormal keratinization. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Oct 2008] (from NCBI)
Top mentioned proteins: ATPase, SERCA, CAN, Phospholamban, Endo
Papers on SERCA2
Combination of Angiotensin II and L-NG-Nitroarginine methyl ester exacerbates mitochondrial dysfunction and oxidative stress to cause heart failure.
Gupte et al., Houston, United States. In Am J Physiol Heart Circ Physiol, Feb 2016
While all treatments increased blood pressure and reduced cardiac contractile function, the L-NAME+AngII group was associated with the most severe HF as characterized by edema, hypertrophy, oxidative stress, increased expression of Nppa and Nppb, and decreased expression of Atp2a2 and Camk2b.
DNA methylation in an engineered heart tissue model of cardiac hypertrophy: common signatures and effects of DNA methylation inhibitors.
Eschenhagen et al., Hamburg, Germany. In Basic Res Cardiol, Jan 2016
RG108 reduced AE-induced Atp2a2 (SERCA2a) promoter methylation.
Small Molecular Allosteric Activator of the Sarco/Endoplasmic Reticulum Ca2+-ATPase (SERCA) Attenuates Diabetes and Metabolic Disorders.
Lebeche et al., New York City, United States. In J Biol Chem, Jan 2016
CDN1163 treatment significantly reduced the hepatic expression of genes involved in gluconeogenesis and lipogenesis, attenuated ER stress response and ER stress-induced apoptosis, and improved mitochondrial biogenesis, possibly through SERCA2-mediated activation of AMP-activated protein kinase pathway.
Dowling-Degos disease co-presenting with Darier disease.
Mousdicas et al., Indianapolis, United States. In Clin Exp Dermatol, Jan 2016
DDD results from mutations in the genes encoding keratin 5 (KRT5), protein O-glucosyltransferase 1 (POGLUT1) or protein O-fucosyltransferase 1 (POFUT1), while DD results from mutations in the ATP2A2 gene.
Cardioprotective effects of baicalein on heart failure via modulation of Ca(2+) handling proteins in vivo and in vitro.
Hou et al., Harbin, China. In Life Sci, Jan 2016
Finally we found that baicalein could modulate the expressions and activities of Ca(2+) handling proteins, including downregulation of phosphorylation of Ca(2+)/calmodulin -dependent protein kinase II (CaMKII) and expression of Na(+)/Ca(2+)-exchangers (NCX1), upregulation of sarcoplasmic reticulum Ca(2+) ATPase 2 (SERCA2) and ryanodine receptor 2 (RYR2).
Calcium-ATPases: Gene disorders and dysregulation in cancer.
Rao et al., Baltimore, United States. In Biochim Biophys Acta, Dec 2015
Mutations in human ATP2A2, ATP2C1 genes, encoding housekeeping isoforms of the endoplasmic reticulum (SERCA2) and secretory pathway (SPCA1) pumps, respectively, confer autosomal dominant disorders of the skin, whereas mutations in other isoforms underlie various muscular, neurological, or developmental disorders.
Biosynthesis and function of bacterial dialkylresorcinol compounds.
Bode et al., Frankfurt am Main, Germany. In Appl Microbiol Biotechnol, Oct 2015
We will give an overview about the DAR-related research during the last 40 years.
Darier disease: A fold (intertriginous) dermatosis.
Tüzün et al., İstanbul, Turkey. In Clin Dermatol, Jul 2015
The ATP2 A2 (SERCA2) gene mutation was detected in all patients.
New pharmacologic interventions to increase cardiac contractility: challenges and opportunities.
Movsesian, Salt Lake City, United States. In Curr Opin Cardiol, May 2015
In particular, PDE3A1 has been shown to interact directly with sarcoplasmic/endoplasmic reticulum Ca ATPase (SERCA2) in the sarcoplasmic reticulum through a phosphorylation of a site in its unique N-terminal domain, making it possible that this isoform can be selectively targeted to increase intracellular Ca cycling.
Sequential fractionation and isolation of subcellular proteins from tissue or cultured cells.
Schulz et al., Edmonton, Canada. In Methodsx, 2014
simple to replicate or adjust; this method does not require expensive reagents or use of commercial kits•The protocol can be applied to tissue samples or cultured cells without changing buffer components•Yields purified fractions of cytosolic, membrane bound and nuclear proteins, with the proper distribution of the appropriate subcellular markers: GAPDH, VDAC, SERCA2 and lamin A/C.
Regulation of SERCA pumps expression in diabetes.
Estrada-Avilés et al., Mexico. In Cell Calcium, 2014
A reduced activity and expression of SERCA2 protein have been described in heart failure and diabetic cardiomyopathy, resulting in an altered Ca(2+) handling and cardiac contractility.
Inhibition of miR-25 improves cardiac contractility in the failing heart.
Mercola et al., San Diego, United States. In Nature, 2014
Using high-throughput functional screening of the human microRNAome, here we identify miRNAs that suppress intracellular calcium handling in heart muscle by interacting with messenger RNA encoding the sarcoplasmic reticulum calcium uptake pump SERCA2a (also known as ATP2A2).
Tmem64 modulates calcium signaling during RANKL-mediated osteoclast differentiation.
Choi et al., Philadelphia, United States. In Cell Metab, 2013
Using in vitro osteoclast culture systems, we show here that Tmem64 interacts with sarcoplasmic endoplasmic reticulum Ca(2+) ATPase 2 (SERCA2) and modulates its activity.
Phospholamban ablation in hearts expressing the high affinity SERCA2b isoform normalizes global Ca²⁺ homeostasis but not Ca²⁺-dependent hypertrophic signaling.
Sipido et al., Leuven, Belgium. In Am J Physiol Heart Circ Physiol, 2012
These findings suggest that local changes in Ca(2+) homeostasis may play an important signaling role in phospholamban-SERCA double knockout mice, perhaps due to reduced microdomain Ca(2+) buffering by SERCA2b.
Modulation of cardiac contractility by the phospholamban/SERCA2a regulatome.
Hajjar et al., Cincinnati, United States. In Circ Res, 2012
Review article highlights the regulatory mechanisms of cardiac contractility by way of the multimeric SERCA/phospholamban (PLN)-ensemble.
Specific effects of endurance and sprint training on protein expression of calsequestrin and SERCA in mouse skeletal muscle.
Mänttäri et al., Oulu, Finland. In J Muscle Res Cell Motil, 2012
Protein levels of CSQ1, SERCA1, and SERCA2 are re-adjusted in skeletal muscles depending on the demands of diverse exercise training programs.
Heat-shock proteins attenuate SERCA inactivation by the anti-apoptotic protein Bcl-2: possible implications for the ER Ca2+-mediated apoptosis.
Schöneich et al., Lawrence, United States. In Biochem J, 2012
functional interactions of SERCA2b and Bcl-2 in the cell may be modulated by HSP70 and other chaperones and stress-regulated proteins.
Extreme sarcoplasmic reticulum volume loss and compensatory T-tubule remodeling after Serca2 knockout.
Louch et al., Oslo, Norway. In Proc Natl Acad Sci U S A, 2012
analysis of extreme sarcoplasmic reticulum volume loss and compensatory T-tubule remodeling after Serca2 knockout
SUMO1-dependent modulation of SERCA2a in heart failure.
Hajjar et al., New York City, United States. In Nature, 2011
data show that SUMOylation is a critical post-translational modification that regulates SERCA2a function, and provide a platform for the design of novel therapeutic strategies for heart failure
Mutations in ATP2A2, encoding a Ca2+ pump, cause Darier disease.
Hovnanian et al., Oxford, United Kingdom. In Nat Genet, 1999
After screening several genes that mapped to this region, we identified mutations in the ATP2A2 gene, which encodes the sarco/endoplasmic reticulum Ca2(+)-ATPase type 2 isoform (SERCA2) and is highly expressed in keratinocytes.
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