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Human ATP2A2 Protein expressed in Wheat germ - ABIN1775707
Ahmad, Shen, Vandeput, Szabo-Fresnais, Krall, Degerman, Goetz, Klussmann, Movsesian, Manganiello: Regulation of Sarcoplasmic Reticulum Ca2+ ATPase 2 (SERCA2) Activity by Phosphodiesterase 3A (PDE3A) in Human Myocardium: PHOSPHORYLATION-DEPENDENT INTERACTION OF PDE3A1 WITH SERCA2. dans The Journal of biological chemistry 2015
Atp2a2/serca2 is found in a larger subset of cells, but is not ubiquitous as reported in adults.
the genomic organization and the equine ATP2A2 coding sequence and an association analysis for chronic pastern dermatitis using a sample of South German draft horses
SGK3 (Montrer SGK3 Protéines) a kinase transcriptionally regulated by estrogen receptor alpha (ERalpha (Montrer ESR1 Protéines)) in breast cancer, sustains ERalpha (Montrer ESR1 Protéines) signaling and drives the acquired aromatase (Montrer CYP19A1 Protéines) inhibitors resistance by protecting against endoplasmic reticulum (EnR (Montrer LARGE Protéines)) stress-induced ERalpha (Montrer ESR1 Protéines) downregulation and cell death through preserving SERCA2b function.
Darier disease (DD) is a rare autosomal dominant skin disorder due to mutations in the ATP2A2 gene.
SERCA2a gene transfer significantly improves left ventricle function and dimensions in doxorubicin-induced cardiomyopathy, suggesting LV-SERCA2a gene transfer an attractive treatment modality for doxorubicin-induced heart failure.
Studies indicate that Darier disease (DD) is caused by mutations in the ATP2A2 gene, whereas the ATP2C1 (Montrer ATP2C1 Protéines) gene is associated with Hailey-Hailey disease (HHD (Montrer ATP2C1 Protéines)).
Taken together, these results suggest that SERCA2 contributes to the migration of CCL21 (Montrer CCL21 Protéines)-activated Dendritic Cells as an important feature of the adaptive immune response and provide novel insights regarding the role of SERCA2 in Dendritic Cells functions.
VMP1 (Montrer VMP1 Protéines) modulates SERCA2 activity to control endoplasmic reticulum contacts for autophagosome formation.
The left atrium / right atrium expression ratio was significantly increased in Atrial fibrillation for SERCA2 - gene related to calcium uptake and release, and located on the sarcoplasmic reticulum membrane.
Loss of SERCA2 impairs ER-to-Golgi transport of nascent DC.
We propose that the increased SERCA1a (Montrer ATP2A1 Protéines) expression indicates the existence and location of compensating mechanisms in ischemic muscle.
Results show that ATP2A2 is variably expressed in astrocytoma tissues and its expression correlates with tumor grade. Its overexpression suppresses growth of astrocytoma cells.
Data suggest that the beneficial effects of SERCA2a gene transfer may involve the attenuation of ER stress-associated myocardial apoptosis.
Oxidative/nitrosative stress associated with lung resection influences SERCA2a activity independent of any influence on protein expression or phospholamban (Montrer PLN Protéines) phosphorylation.
overexpression of SERCA2a by in vivo rAAV1-mediated intracoronary gene transfer preserved systolic function, potentially prevented diastolic dysfunction, and improved ventricular remodeling.
Data show that rabbit cold tolerance is probably related to increased muscle oxidative metabolism and heat production by SERCA1 (Montrer ATP2A1 Protéines) and that these changes are not completely dependent on normal thyroid function.
These results indicate a mechanism relating SERCA1 (Montrer ATP2A1 Protéines) vicinal-cysteines oxidation to muscle fatigue.
Pin1 (Montrer PIN1 Protéines) serves as a modulator of SERCA2a and Na(2+)/Ca(2 (Montrer CA2 Protéines)+) exchanger 1 Ca(2 (Montrer CA2 Protéines)+) handling proteins, with loss of function resulting in impaired cardiomyocyte relaxation.
Pep2.5 prevented the down-regulation of SERCA2 expression in a) murine heart samples obtained from mice with sepsis and b) in cardiomyocytes exposed to serum from septic shock patients. Thus, we speculate that Pep2.5 may be able to prevent down-regulation of cardiac SERCA2 expression in patients with sepsis.
The findings support a salutary role of TLR9 (Montrer TLR9 Protéines) in some subsets of HF conditions and underline the importance for future studies on the mechanisms of TLR9 (Montrer TLR9 Protéines) in diastolic HF.
Our results indicate that changes in cell shape changed nuclear morphology and then the gene expression of IP3R1 (Montrer ITPR1 Protéines) and SERCA2, which produced different intracellular calcium transient patterns.
Nevertheless, the functional role of protein serotonylation in controlling SAN automaticity is largely unexplored. In this study, we screened the cardiomyocytes proteins and found that sarco(endo)plasmic reticulum Ca ATPase type 2a (SERCA2a) can be serotonylated. Simulation studies using mathematical SAN cell model showed that variation of Ca(2 (Montrer CA2 Protéines)+) affinity of SERCA2a pump cause either tachycardia or bradycardia.
Muscle RANK deletion had no significant effects on the sham or denervated slow-twitch soleus muscles. These data identify a novel role for RANK as a key regulator of Ca(2 (Montrer CA2 Protéines)+)storage and SERCA (Montrer ATP2A3 Protéines) activity, ultimately affecting denervated skeletal muscle function.
Generated were mice harboring N-ethyl-N-nitrosourea (ENU)-induced allelic mutations in Serca2: three missense mutations and one nonsense mutation. Mice harboring these Serca2 mutations developed tumors that were categorized as either early onset squamous cell tumors (SCT), with development similar to null-type knockout mice [2,4] (aggressive form; M682, M814), or late onset tumors (mild form; M1049, M1162).
Identify Atrap as a novel regulatory protein of the cardiac Ca(2+)-ATPase SERCA2a. Suggest that Atrap enhances the activity of SERCA2a and, consequently, facilitates ventricular relaxation.
CAPN3 (Montrer CAPN3 Protéines) deficiency leads to degradation of SERCA (Montrer ATP2A3 Protéines) proteins and Ca2 (Montrer CA2 Protéines)+ dysregulation in the skeletal muscle.
SERCA2a gene transfer in the failing heart not only improves contractile function but also directly restores electric stability through amelioration of key arrhythmogenic substrate.
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.
Calcium ATPase at 60A
, ATPase, Ca++ transporting, cardiac muscle, slow twitch 2
, sarcoplasmic/endoplasmic reticulum calcium ATPase 2
, sarcoplasmic/endoplasmic reticulum calcium ATPase 2-like
, ATPase, Ca++ dependent, slow-twitch, cardiac muscle-2
, SR Ca(2+)-ATPase 2
, calcium pump 2
, calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform
, cardiac Ca2+ ATPase
, endoplasmic reticulum class 1/2 Ca(2+) ATPase
, calcium ATPase
, sarcoplasmic reticulum Ca2+-transport ATPase isoform
, Ca(2+)-transport ATPase class 3
, sarcoplasmic/endoplasmic-reticulum Ca(2+) pump gene 2
, ATPase, Ca++ transporting, slow twitch 2
, sarco(endo)plasmic reticulum Ca(2+)-dependent ATPase 2
, sarco/endoplasmic reticulum Ca2+-ATPase 2
, sarcoplasmic reticulum slow-twitch Ca2 ATPase