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Cow (Bovine) Polyclonal ASS1 Primary Antibody für IHC (p), IHC - ABIN314255
Hao, Xie, Gross: Argininosuccinate synthetase is reversibly inactivated by S-nitrosylation in vitro and in vivo. in The Journal of biological chemistry 2004
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Human Monoclonal ASS1 Primary Antibody für IHC, ELISA - ABIN969503
Laróvere, Angaroni, Antonozzi, Bezard, Shimohama, de Kremer: Citrullinemia type I, classical variant. Identification of ASS-p~G390R (c.1168G>A) mutation in families of a limited geographic area of Argentina: a possible population cluster. in Clinical biochemistry 2009
Human Polyclonal ASS1 Primary Antibody für IP, ELISA - ABIN190834
Corbin, Pendleton, Solomonson, Eichler: Phosphorylation of argininosuccinate synthase by protein kinase A. in Biochemical and biophysical research communications 2008
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Human Polyclonal ASS1 Primary Antibody für ICC, IF - ABIN4281472
Slebos, Jehmlich, Brown, Yin, Chung, Yarbrough, Liebler: Proteomic analysis of oropharyngeal carcinomas reveals novel HPV-associated biological pathways. in International journal of cancer 2012
The remaining five patients were diagnosed with neonatal intrahepatic cholestasis due to citrin (zeige slc25a13 Antikörper) deficiency, and have respectively carried mutations of the SLC25A13 (zeige slc25a13 Antikörper) gene including [c.851-854delGTAT+c.851-854delGTAT], [c.851-854delGTAT+IVS6+5G>A], [c.851-854delGTAT+IVS16ins3kb], [c.851-854delGTAT+IVS6-11A>G] and [c.851-854delGTAT+c.1638-1660dup23]
Results indicate that the reduced ASS1 expression in Dox-resistant sarcomas may contribute to drug resistance in association with the expression of P-glycoprotein.
Cisplatin-induced synthetic lethality to arginine-starvation therapy by transcriptional suppression of ASS1 is regulated by DEC1 (zeige BHLHE40 Antikörper), HIF-1alpha (zeige HIF1A Antikörper), and c-Myc (zeige MYC Antikörper) transcription network and is independent of ASS1 promoter DNA methylation (zeige HELLS Antikörper).
Low expression of ASS1 is associated with glioblastoma.
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 Antikörper) 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 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 Antikörper) 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 Antikörper)-328 is mediated by PKCalpha (zeige PKCa Antikörper)
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 Antikörper) coordinately downregulates nitric oxide synthase (zeige NOS Antikörper) (eNOS (zeige NOS3 Antikörper)) 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