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SLN overexpression is associated with severe muscle atrophy and weakness.
SLN plays an important role in adaptive muscle remodeling potentially through calcineurin stimulation, which could have important implications for other muscle diseases and conditions
Cardiac function of Sln(Cre/+) mice was not significantly different from WT mice in all aspects that were examined.
the N termini of SLN and PLB (show PLN ELISA Kits) influence their respective unique functions
UCP1 (show UCP1 ELISA Kits) and SLN are required to maintain optimal thermogenesis and loss of both systems compromises survival of mice under cold stress
both SLN knockout (Sln(-/-)) and skeletal muscle-specific (show EIF3K ELISA Kits) SLN overexpression (Sln(OE)) mice to explore energy metabolism by pair feeding (fixed calories) and high-fat diet feeding (ad libitum)
overexpression of neither wild type nor FLAG-tagged variants of sarcolipin in transgenic mice had any major significant effects on body mass, energy expenditure, even when mice were fed on a high fat diet
SLN and PLN (show PLN ELISA Kits) are co-expressed in most fibers, which suggests that super-inhibition of SERCAs may be physiologically important in the regulation of intracellular Ca2 (show CA2 ELISA Kits)+ in human skeletal muscle.
results suggest that beta-AR signaling partially compensates for a lack of SLN to activate muscle-based DIT, but SLN is the primary and more effective mediator.
Sarcolipin deficiency increases the transport stoichiometry of SERCA (show ATP2A3 ELISA Kits) pumps and decreases the relative contribution of SERCA (show ATP2A3 ELISA Kits) pumps to resting oxygen consumption.
Self-assembling study of sarcolipin and its mutants in multiple molecular dynamic simulations has been reported.
These results suggest that sAnk1 interacts with SLN both directly and in complex with SERCA1 (show ATP2A1 ELISA Kits) and reduces SLN's inhibitory effect on SERCA1 (show ATP2A1 ELISA Kits) activity.
analysis of transmembrane dynamics of the Thr (show TRH ELISA Kits)-5 phosphorylated sarcolipin pentameric channel
Phospholamban (show PLN ELISA Kits) and sarcolipin are membrane proteins that differentially regulate SERCA (show ATP2A3 ELISA Kits) function. (Review)
Molecular dynamics simulations help to clarify and to understand better the SLN pentamer channel that had a hydrophobic gate and could switch Na(+) and Cl(-) ion permeability by hydrated and vacuum states.
Although SLN and PLB (show PLN ELISA Kits) binding to SERCA (show ATP2A3 ELISA Kits) have different functional outcomes on the coupling efficiency of SERCA (show ATP2A3 ELISA Kits), both proteins decrease the apparent Ca(2 (show CA2 ELISA Kits)+) affinity of the pump, suggesting that SLN and PLB (show PLN ELISA Kits) inhibit SERCA (show ATP2A3 ELISA Kits) by using a similar mechanism.
The C-terminal tail of SLN is a distinct, essential domain in the regulation of SERCA (show ATP2A3 ELISA Kits).
The selective downregulation of SLN and enhanced sarcoplasmic reticulum Ca(2 (show CA2 ELISA Kits)+) uptake in human AF suggest that SLN downregulation could play an important role in abnormal intracellular Ca(2 (show CA2 ELISA Kits)+) cycling in atrial pathology.
sarcolipin binds to phospholamban (show PLN ELISA Kits) and inhibits polymerization
Cell functions regulated by protein-protein interactions of the SERCA1a (show ATP2A1 ELISA Kits)-sarcolipin complex is accomplished via s-palmitoylation and s-oleoylation of sarcolipin.
The expression of SLN and PLB (show PLN ELISA Kits) mRNA and protein relative to SERCA1 (show ATP2A1 ELISA Kits) or SERCA2 (show ATP2A2 ELISA Kits) was assessed in ventricle, atrium, and skeltal msucle of mouse, rat, rabbit and pig.
Sarcoplasmic reticulum Ca(2+)-ATPases are transmembrane proteins that catalyze the ATP-dependent transport of Ca(2+) from the cytosol into the lumen of the sarcoplasmic reticulum in muscle cells. This gene encodes a small proteolipid that regulates several sarcoplasmic reticulum Ca(2+)-ATPases. The transmembrane protein interacts with Ca(2+)-ATPases and reduces the accumulation of Ca(2+) in the sarcoplasmic reticulum without affecting the rate of ATP hydrolysis.