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anti-Mouse (Murine) ATP2A1 Anticorps:
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The different forms of phospholamban in zebrafish may provide a novel SERCA regulatory mechanism.
study showed that accordian acc(dta5) mutants harbor a novel mutation in atp2a1; indicate the acc(dta5) mutation diminishes SERCA1 function to a greater degree than other acc alleles through haploinsufficient or dominant-negative molecular mechanisms
encodes the sarco(endo)plasmic reticulum Ca2+-ATPase 1 (SERCA1), a Ca2+ pump found in the muscle sarcoplasmic reticulum (SR) that is responsible for pumping Ca2+ from the cytosol back to the SR
concluded that the motility dysfunction in embryonic and larval accordion zebrafish stems directly from defective calcium transport in skeletal muscle due to mutation in SERCA rather than defective CNS drive.
Atp2a1/serca1 is expressed as soon as the end of gastrulation in a subset of the myod-positive cells, and later labels prospective slow muscle cells in the superficial part of the somite.
Cell functions regulated by protein-protein interactions of the SERCA1a-sarcolipin complex is accomplished via s-palmitoylation and s-oleoylation of sarcolipin.
The changes in expression of SERCA1 potentially disturb the normal Ca2+ channel as well as the balance of Ca2+ homeostasis.
These findings provide a quantitative basis for SERCA1a function that leverages molecular-scale thermodynamic data and rationalizes enzyme activity across broad ranges of K(+), Ca(2+), and Mg(2+) concentrations.
Phospholamban (PLB) oligomerization, quaternary structure, and sarco(endo)plasmic reticulum calcium ATPase (SERCA) binding were quantified by fluorescence resonance energy transfer (FRET) in an intact cellular environment.
interactions between the cytoplasmic domain of phospholamban and negatively charged phospholipids might play a role in moderating the regulation of SERCA, with implications for cardiac muscle contractility.
functional studies and three new crystal structures of the rabbit skeletal muscle Ca2+-ATPase.
Protonation of the Ca(2+) ligands of the SR Ca(2+)-ATPase (SERCA1a) was studied by a combination of rapid scan FTIR spectroscopy and electrostatic calculations.
the major SR membrane lipid PC is optimal for all steps and, unlike the other headgroups, contributes favorable electrostatics and non-electrostatic elements during the Ca-ATPase transition
ATP-dependent Ca(2+) transport by SERCA in single giant unilamellar vesicles was detected directly using confocal fluorescence microscopy.
Glycine 105 as Pivot for a Critical Knee-like Joint between Cytoplasmic and Transmembrane Segments of the Second Transmembrane Helix in Ca2+-ATPase.(
Here we describe the methods to analyze these processes in the transport cycle with a representative member of P-type ATPase family, SERCA1a, sarco(endo)plasmic reticulum Ca(2+)-ATPase
oligonucleotide-based drugs could be used to fine-tune SERCA function to counterbalance the extent of the pathological insults.
Inhibition of the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA1) by rutin derivatives.
Infrared spectroscopy was used to characterise recombinant sarcoplasmic reticulum Ca2+-ATPase (SERCA1a).
Data show that biselyngbyasides (BLSs) bind to the pump SERCA1a calcium ATPase near the cytoplasmic surface of the transmembrane region.
Rescue of mutated SERCA1 to sarcoplasmic reticulum membrane can re-establish resting cytosolic Ca(2+) concentration and prevent the appearance of pathological signs of cattle pseudomyotonia
Conformation of the SERCA1A calcium ATPase in the presence of different lipids.
Ca(2+) and PLB phosphorylation relieve SERCA-PLB inhibition by distinct mechanisms, but both are achieved primarily by structural changes within the SERCA-PLB complex, not by dissociation of that complex.
Phosphorylated phospholamban stabilizes a unique conformation of SERCA that is characterized by a compact architecture.
Data suggest some phytoestrogenic flavonoids cooperate to inhibit SERCA, alter ATP binding properties of SERCA, and alter phosphorylation/dephosphorylation of SERCA by binding to several sites that are close to ATP binding site.
Data suggest that phospholamban PLN's conformational equilibrium is central to maintain sarcoplasmic reticulum Ca(2+)-ATPase SERCA's apparent Ca(2+) affinity within a physiological window.
Our results indicate that the phospholipid headgroup PC:PE negatively correlated and could potentially contribute to reductions in SERCA activity seen in functionally overloaded plantaris.
CAPN3 deficiency leads to degradation of SERCA proteins and Ca2+ dysregulation in the skeletal muscle.
Ebf3 binds directly to the promoter of Atp2a1 and synergises with MyoD in the induction of Atp2a1
Formalin evokes calcium transients from the endoplasmatic reticulum via SERCA1-dependent, TRPA1-independent mechanism that may underlie formaldehyde-induced pan-neuronal excitation and subsequent inflammation.
SERCA1b is considered to play an essential role in the regulation of [Ca2+]i and its ab ovo gene silencing results in decreased skeletal muscle differentiation.
Data show that in healthy transgenic mice, cardiac-specific sarcoplasmic reticulum calcium ATPase SERCA1a expression increased active cell-surface glucose transporter GLUT4 and glucose uptake in the myocardium.
Data suggest that the cardiac depressant properties of neuronostatin possibly associated with loss of sarcoplasmic reticulum Ca2+-ATPase SERCA phosphorylation.
Results indicated that sine oculis homeobox 1 (Six1) overexpression could significantly promote the expression of fast-type muscle genes Atp2a1, Srl, and Mylpf.
Protein levels of CSQ1, SERCA1, and SERCA2 are re-adjusted in skeletal muscles depending on the demands of diverse exercise training programs.
dystrophic phenotype observed in delta-sarcoglycan-null (Sgcd(-/-)) mice and dystrophin mutant mdx mice is dramatically improved by skeletal muscle-specific overexpression of sarcoplasmic reticulum Ca(2+) ATPase 1 (SERCA1)
Targeted disruption of the gene encoding this protein in the sarco(endo)plasmic reticulum impairs diaphragm function and is lethal in neonatal mice.
Sarcolipin is a novel regulator of SERCA pump activity, and its inhibitory effect can be reversed by beta-adrenergic agonists.
The results indicate that SERCA overexpression can reduce the *OH-induced contractile dysfunction in murine myocardium, whereas a reduced SR Ca(2+)-ATPase activity aggravates this injury.
Our studies point to an important regulation of SERCA1b expression at the protein level and hints to a role in the growth of the developing muscle.
Increased TR expression in the hypertrophied heart is associated with an improvement in contractile function and increased SERCA expression.
In dystrophin-deficient mdx mice the serca1 is overpression in laryngeal muscles.
Study demonstrated that (a) the distribution and the expression levels of total SERCA1 and SERCA2, the activity of SR Ca2+ ATPase, and the oligomerization of SERCA1 are similar in patients with myotonic dystrophy 1, myotonic dystrophy 2, hypothyroid myopathy and control subjects; and (b) SERCA1b is expressed in patients with myotonic dystrophy, mainly in myotonic dystrophy 2 muscles.
These results suggest that sAnk1 interacts with SLN both directly and in complex with SERCA1 and reduces SLN's inhibitory effect on SERCA1 activity.
The sphingolipid sphingosine increases the [Ca(2+)]i by inhibiting the sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA), in a similar manner to thapsigargin (Tg), a specific inhibitor of this Ca(2+) pump.
Thus the human SERCA1b has a different expression pattern from that of rodents and it is associated with DM2.
We conclude that PLB C-terminal residues are critical for localization, oligomerization, and regulatory function. In particular, the PLB C terminus is an important determinant of the quaternary structure of the SERCA regulatory complex.
Aberrant splicing of SERCA1 may alter intracellular Ca(2+) signalling in myotonic dystrophy 1 and 2 myotubes. The differing dysregulation of intracellular Ca(2+) handling in DM1 and DM2 may explain their distinct sarcolemmal hyperexcitabilities.
We performed a detailed study of SERCA1 protein expression in muscle of patients with BD and BS, and evaluated the alternative splicing of SERCA1 in primary cultures of normal human muscle
These results indicate that PKC signaling is involved in the splicing of SERCA1 and provide new evidence for a link between alternative splicing and PKC signaling.
both topology and function of PLN are shaped by the interactions with lipids, which fine-tune the regulation of SERCA
Modeling of the inhibitory interaction of phospholamban with the Ca2+ ATPase.
regulation by sarcolipin's involvement in binding to transmembrane helices alone or in association with phospholamban
kinetic analysis of SERCA1 and SERCA2 isoforms and the effects of mutation
The coexistence of SERCA1 and -2, together with complex mixtures of MyHCs in most of the fibers provide the human EOMs with a unique molecular portfolio that allows a highly specific fine-tuning regimen of contraction and relaxation.
The combination of these histological and immunoblot results is consistent with the hypothesis that diaphragm remodeling elicited by severe COPD is characterized by a fast-to-slow SERCA isoform transformation.
SERCA1 gene transfer increased fractional myocardial cell shortening (compared to LacZ) and accelerated relengthening kinetics.
We suggest that aberrant splicing of SERCA1 mRNAs might contribute to impaired Ca2+ homeostasis in DM1 muscle
The maximal turnover rates of the ATPase activity for SPCA1 isoforms were 4.7-6.4-fold lower than that of SERCA1a (lowest for the shortest SPCA1a isoform).
SERCA1, 2, and 3 sensitivity to thapsigargin is dependent on a phenylalanine 256 to valine mutation
Results demonstrate that a cattle congenital pseudomyotonia is caused by a SERCA1 deficiency, resulting from a defect in the ATP2A1 gene
crystal structure of SERCA, crystallized in the E1 conformation and determined at 2.9A resolution
Mutation in ATP2A1 is associated with congenital muscular dystony type 1
study reports the identification of a missense mutation in ATP2A1 in congential pseudomytonia of Chianina cattle; mutation analysis of ATP2A1 exons revealed a perfectly associated missense mutation in exon 6 (c.491G>A) leading to p.Arg164His substitution
In this study, we provide biochemical evidence for a selective deficiency in SERCA1 protein levels in sarcoplasmic reticulum membranes from Chianina cattle with congenital pseudomyotonia
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 to the sarcoplasmic reticulum lumen, and is involved in muscular excitation and contraction. Mutations in this gene cause some autosomal recessive forms of Brody disease, characterized by increasing impairment of muscular relaxation during exercise. Alternative splicing results in two transcript variants encoding different isoforms.
ATPase, Ca++ transporting, fast twitch 1
, sarcoendoplasmic reticulum calcium ATPase
, ATPase, Ca++ transporting, cardiac muscle, fast twitch 1
, ATPase, Ca++ transporting, cardiac muscle, slow twitch 2
, sarcoplasmic/endoplasmic reticulum calcium ATPase 1-like
, ATPase, Ca++ transporting, slow twitch 2
, sarcoplasmic/endoplasmic reticulum calcium ATPase 1
, ATPase, Ca++ transporting, ubiquitous
, SR Ca(2+)-ATPase 1
, calcium pump 1
, calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform
, endoplasmic reticulum class 1/2 Ca(2+) ATPase