Argininosuccinate lyase interacts with cyclin A2 in cytoplasm and modulates growth of liver tumor cells
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Argininosuccinate lyase interacts with cyclin A2 in cytoplasm and modulates growth of liver tumor cells
Arginine is a critical amino acid in specific cancer types including hepatocellular carcinoma (HCC) and melanoma. Novel molecular mechanisms and therapeutic targets in arginine metabolism-mediated cancer formation await further identification. Our laboratory has previously demonstrated that arginine metabolic enzyme argininosuccinate lyase (ASL) promoted HCC formation in part via maintenance of...
متن کاملAttenuation of argininosuccinate lyase inhibits cancer growth via cyclin A2 and nitric oxide.
Arginine biosynthesis and nitric oxide (NO) production are important for cancer homeostasis. Degradation of arginine may be used to inhibit liver tumors with low argininosuccinate synthetase (ASS) expression. In this report, we investigated an alternative therapeutic approach by targeting argininosuccinate lyase (ASL). ASL is transcriptionally induced by endoplasmic reticulum stress and is over...
متن کاملKinetic mechanism of bovine liver argininosuccinate lyase.
The kinetic mechanism of bovine liver argininosuccinate lyase has been determined at pH 7.5, 25 degrees C. Fumarate and arginine are both noncompetitive inhibitors versus argininosuccinate. The dead-end inhibitor, succinate, is competitive versus fumarate and argininosuccinate, but noncompetitive versus arginine. Citrulline is competitive versus arginine and noncompetitive versus argininosuccin...
متن کاملNitro analogs of substrates for argininosuccinate synthetase and argininosuccinate lyase.
The nitro analogs of aspartate and argininosuccinate were synthesized and tested as substrates and inhibitors of argininosuccinate synthetase and argininosuccinate lyase, respectively. The Vmax for 3-nitro-2-aminopropionic acid was found to be 60% of the maximal rate of aspartate utilization in the reaction catalyzed by argininosuccinate synthetase. Only the nitronate form of this substrate, in...
متن کاملReversed argininosuccinate lyase activity in fumarate hydratase-deficient cancer cells
BACKGROUND Loss of function of fumarate hydratase (FH), the mitochondrial tumor suppressor and tricarboxylic acid (TCA) cycle enzyme, is associated with a highly malignant form of papillary and collecting duct renal cell cancer. The accumulation of fumarate in these cells has been linked to the tumorigenic process. However, little is known about the overall effects of the loss of FH on cellular...
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ژورنال
عنوان ژورنال: Oncology Reports
سال: 2016
ISSN: 1021-335X,1791-2431
DOI: 10.3892/or.2016.5334