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In these studies found that SelS increases in negative correlation with tau phosphorylation in brain.
The results suggest that SelS is required for C99 degradation through endoplasmic reticulum-associated degradation, resulting in inhibition of amyloid beta production.
regulating liver and serum Selenoprotein S levels might become a new strategy for the prevention and treatment of DM and its macrovascular complications
SEPS1 may be a potential gene marker for disease diagnosis and prognosis.
interaction between SelK and p97(VCP (show vcp Proteins)) is SelS-dependent, and the resulting ERAD complex (SelS-p97(VCP (show vcp Proteins))-SelK) plays an important role in ERAD and ER stress
Potential roles of the SEPS1 gene in the pathogenesis and etiology of Hashimoto's thyroiditis.
SNP rs4965814 of SELS may affect the susceptibility to ischemic stroke.
The SEPS1 -105G>A is associated with an increased risk of Kashin-Beck disease and influences the expression of PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins) signaling pathway in Kashin-Beck disease patients
Although VIMP can interact with CLIMP-63 (show CKAP4 Proteins) and Syn5L, it does not interact with MT-binding ER proteins (such as Reep1 (show REEP1 Proteins)) that shape the tubular smooth ER
Selenoprotein S is a marker but not a regulator of endoplasmic reticulum stress in intestinal epithelial cells in inflammatory bowel diseases.
the genetic reduction of Seps1 appears to specifically exacerbate the inflammatory profile of fast-twitch muscle fibres, which are typically more vulnerable to degeneration in dystrophy.
Pro(178) and Pro(183) of SelS play important roles in the translocation of p97(VCP (show vcp Proteins)) to the ER membrane and protect cells from ER stress
SelS expression is prominent in neurons and hardly detectable in astrocytes from control mice
The SEPS1 protein expression in liver of septic mouse is markedly elevated.
These findings suggest that SEPS1 could be a new ER stress-dependent survival factor that protects macrophage against ER stress-induced cellular dysfunction.
We found that suppression of SEPS1 by small interfering RNA severely increases astrocyte injure caused by OGD (show FGFR1 Proteins), suggesting that selenoprotein S protects astrocytes against ischemia.
This gene encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Studies suggest that this protein may regulate cytokine production, and thus play a key role in the control of the inflammatory response. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.
, histocompatibility 47
, minor histocompatibility antigen H47