Results 151 to 160 of about 5,002 (185)

Therapeutic Targeting of Argininosuccinate Synthase 1 (ASS1)-Deficient Pulmonary Fibrosis [PDF]

open access: yesMolecular Therapy, 2021
Argininosuccinate synthase 1 (ASS1) serves as a critical enzyme in arginine biosynthesis; however, its role in interstitial lung diseases, particularly idiopathic pulmonary fibrosis (IPF), remains largely unknown. This study aims at characterization and targeting of ASS1 deficiency in pulmonary fibrosis.
Nicholas J Kenyon, Ching-Hsuan
exaly   +6 more sources

Downregulation of Argininosuccinate Synthase 1 (ASS1) Is Associated With Hypoxia in Placental Development

open access: yesHuman Cell, 2023
Argininosuccinate synthase (ASS1) is involved in nitric oxide production, which has a key role in placental development improving pregnancy outcomes. Syncytiotrophoblast and extravillous trophoblast differentiations are milestones of placental development and their impairment can cause pathologies, such as preeclampsia (PE) and fetal growth restriction
Giovanni Tossetta   +2 more
exaly   +8 more sources

Argininosuccinate Synthetase 1 (ASS1) Is a Common Metabolic Marker of Chemosensitivity for Targeted Arginine- and Glutamine-Starvation Therapy

open access: yesCancer Letters, 2017
Argininosuccinate synthetase 1 (ASS1) is the rate-limiting enzyme that catalyzes the biosynthesis of arginine (Arg). Many malignant human tumors are auxotrophic for Arg because ASS1 is silenced.
David H Hawke   +2 more
exaly   +2 more sources

Citrulline Depletion by ASS1 Is Required for Proinflammatory Macrophage Activation and Immune Responses

Molecular Cell, 2022
Citrulline can be converted into argininosuccinate by argininosuccinate synthetase (ASS1) in the urea cycle and the citrulline-nitric oxide cycle. However, the regulation and biological function of citrulline metabolism remain obscure in the immune system. Unexpectedly, we found that macrophage citrulline declines rapidly after interferon gamma (IFN-γ)
Peng Jiang, Youxiang Mao
exaly   +3 more sources

ASS1 Regulates Immune Microenvironment via CXCL8 Signaling in Ovarian Cancer

open access: yesBiochemical and Biophysical Research Communications, 2022
Ovarian cancer is one of the most serious and deadly cancers for female and currently no effective screening approaches have been achieved. Therefore it is usually diagnosed at an advanced stage and most patients have a poor prognosis. The development of ovarian cancer is a comprehensive process depending on the cross-talk between the various cells in ...
Xu Feng, Gong Yang, Zhaodong Ji
exaly   +3 more sources

Endothelial Cell Ass1 Inhibits Arteriosclerotic Calcification in Diabetes Mellitus

open access: yesBiomedicine and Pharmacotherapy
Endothelial cell (EC) dysfunction is an important pathological feature of early calcification in diabetic plaques. Argininosuccinic synthase 1 (Ass1) is important in protecting EC activity. Therefore, this study aimed to explore the effect of endothelial Ass1 on calcification in diabetic plaques and its potential regulatory mechanism.
Zhongqun Wang, Lihua Li
exaly   +3 more sources

PRMT7 Interacts with ASS1 and Citrullinemia Mutations Disrupt the Interaction

Journal of Molecular Biology, 2017
Protein arginine methyltransferase 7 (PRMT7) catalyzes the introduction of monomethylation marks at the arginine residues of substrate proteins. PRMT7 plays important roles in the regulation of gene expression, splicing, DNA damage, paternal imprinting, cancer and metastasis. However, little is known about the interaction partners of PRMT7.
Mamta, Verma   +7 more
openaire   +2 more sources

Diversion of Aspartate in ASS1-Deficient Tumours Fosters De Novo Pyrimidine Synthesis [PDF]

open access: yesNature, 2015
Cancer cells hijack and remodel existing metabolic pathways for their benefit. Argininosuccinate synthase (ASS1) is a urea cycle enzyme that is essential in the conversion of nitrogen from ammonia and aspartate to urea. A decrease in nitrogen flux through ASS1 in the liver causes the urea cycle disorder citrullinaemia.
David Dimmock   +2 more
exaly   +3 more sources

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