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Case Report: rigid spine muscular dystrophy 1 in a compound heterozygote with two novel mutations in SEPN1 gene; a novel missense mutation (c.1384T>C; p.Sec462Arg) and a novel nonsense mutation (c.1525C>T; p.Gln509Ter), inherited from his father and mother respectively.
We report two previously undescribed mutations in SEPN1. Our study adds two novel homozygous mutations to the number of reported pathogenic SEPN1 variants.
The physiological function of SelN in muscle tissue and the pathogenesis leading to SEPN1-related myopathies. [Review]
Data show that the spectrum of severity of SEPN1-related myopathiesis wider than previously reported.
Data show that Argonaute 2 (Montrer EIF2C2 Anticorps) expression is critical for stem cells to escape senescence by downregulating miR10b and miR23b, and that selenoprotein N1 is also involved in ATSC survival and self-renewal through ROS (Montrer ROS1 Anticorps)-mediated p38 MAPK (Montrer MAPK14 Anticorps) inactivation.
this series of patients illustrates the clinical, histopathological and MRI (Montrer C7ORF49 Anticorps) findings of SEPN1-related myopathy. It also adds new mutations to the limited number of fully described pathogenic SEPN1 variants.
Mutations of the selenoprotein N gene, which is implicated in rigid spine muscular dystrophy, cause the classical phenotype of multiminicore disease
A new SEPN1 point mutation, 943g->A causing G315S was found in a rigid spine muscular dystrophy patient with cor pulmonale.
SEPN1 mutation analysis revealed that the patient was a compound heterozygote: a previously described insertion (713-714 insA (Montrer INS Anticorps)), and a novel nonsense mutation (R439stop).
Two patients with 'Dropped head syndrome' due to mutations in SEPN1 genes.
SEPN1 enhances SERCA2 activity by reducing luminal cysteines that are hyperoxidized by ERO1-generated peroxides.
SepN deficiency leads to abnormal lung development characterized by enlarged alveoli, which is associated with decreased tissue elastance and increased quasi-static compliance of Sepn1(-/-) lungs.
Data show that Sepn1(-/-) mice developed an obvious phenotype, characterized by limited motility and body rigidity during the swimming session.
we describe for the first time a major physiological function of SelN in skeletal muscles, as a key regulator of SC function, which likely plays a central role in the pathophysiological mechanism leading to SEPN1-RM.
In whole embryos, Sepn1 transcripts were detected as early as E5.5, with expression levels peaking at E12.5, and then strongly decreasing until birth.
alteration of myofibril architecture and tendon-like structure in embryos deficient for SelN function provide new insights into the pathological mechanism of SelN-related myopathy
sepn1 and ryr1 (Montrer RYR1 Anticorps) are required for the same cellular differentiation events and are needed for normal calcium fluxes
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. Mutations in this gene cause the classical phenotype of multiminicore disease and congenital muscular dystrophy with spinal rigidity and restrictive respiratory syndrome. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.