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ASS1 acetylation by CLOCK exhibits circadian oscillation in human cells and mouse liver, possibly caused by rhythmic interaction between CLOCK and ASS1, leading to the circadian regulation of ASS1 and ureagenesis.
update reports 137 mutations in the ASS1 gene (64 of which are novel), consisting of 89 missense mutations, 19 nonsense mutations, 17 mutations that affect splicing, and 12 deletions; the change p.Gly390Arg is by far the most common mutation and is widely spread throughout the world
Of 21 ASS potential kinetic mutations, 13 were totally inactive while 8 exhibited decreased affinity for aspartate and citrulline.
Low ASS1 expression was associated with higher recurrence , shorter disease-free survival and shorter overall survival in patients with pancreatic ductal adenocarcinoma.
The authors showed that ASS1 mutations linked to type I citrullinemia disrupt the ASS1-PRMT7 (zeige PRMT7 ELISA Kits) interaction, which might explain the molecular pathogenesis of the disease.
Identification of three novel CTLN1 mutations in fourteen patients with citrullinemia type 1 has been reported.
In this trial, arginine deprivation with ADI-PEG20 improved PFS in patients with ASS1-deficient mesothelioma. Targeting arginine is safe and warrants further clinical investigation in arginine-dependent cancers.
combining hypoxia and ADI-PEG20 synergistically inhibited ASS1.
ASS1 genomic variants (rs10901080 and rs10793902) can serve as pharmacogenomic biomarkers to predict hydroxyurea treatment efficacy in sickle cell disease/beta-thalassemia compound heterozygous patients.
results show that ASS1 is elevated at the mRNA and protein levels in mesothelioma 3D spheroids and in human pleural mesotheliomas. We also have uncovered a survival role for ASS1
In diabetic mice, ablation of Ass resulted in diminished endothelium-derived nitric oxide-mediated vascular relaxation responses.
cAMP-induced Ass1 expression is important in controlling the magnitude of decidualization through regulating L-Arg level.
We demonstrate that the transgenic mouse system reported here has the merit of sensitivity and direct visualization advantage, and is ideal for annotating temporal and spatial expression profiles and the regulation mode of the ASS gene.
Thus, extracellular arginine fuels rapid NO production in activated macrophages, and citrulline recycling via Ass1 and Asl (zeige ADSL ELISA Kits) is a fail-safe system that sustains optimum NO production.
Partial argininosuccinate synthase ablation protects only in acute ethanol-induced liver injury by decreasing nitrosative stress but not in a more chronic scenario where oxidative stress and impaired fatty acid beta-oxidation are key events.
Loss of Ass1 is associated with citrullinemia type I and other hyperammonemic syndromes.
calcium-dependent phosphorylation of argininosuccinate synthase Ser (zeige SIGLEC1 ELISA Kits)-328 is mediated by PKCalpha (zeige PKCa ELISA Kits)
dose-dependent reduction of ASS as a result of siRNA treatment corresponded to diminished capacity to produce NO, despite saturating levels of arginine in the medium; reduced expression of ASS resulted in loss of viability due to apoptosis
In endothelial cells TNF-alpha (zeige TNF ELISA Kits) coordinately downregulates nitric oxide synthase (zeige NOS ELISA Kits) (eNOS (zeige NOS3 ELISA Kits)) and argininosuccinate synthase expression, resulting in a severely impaired citrulline-NO cycle.
These results represent the first demonstration that vascular endothelial nitric oxide production can be regulated by dynamic argininosuccinate synthase phosphorylation.
The protein encoded by this gene catalyzes the penultimate step of the arginine biosynthetic pathway. There are approximately 10 to 14 copies of this gene including the pseudogenes scattered across the human genome, among which the one located on chromosome 9 appears to be the only functional gene for argininosuccinate synthetase. Mutations in the chromosome 9 copy of this gene cause citrullinemia. Two transcript variants encoding the same protein have been found for this gene.
, argininosuccinate synthetase 1
, citrulline--aspartate ligase
, citrulline-aspartate ligase
, arginosuccinate synthetase 1
, arginosuccinate synthetase
, argininosuccinate synthase 1
, argininosuccinate synthase-like