Mitochondrial preparations isolated from rat ventral prostate were capable of oxidizing isocitrate by way of NADP isocitrate dehydrogenase (NADP-IDH) and NAD-IDH. NAD-IDH activity required ADP for activation. The pH responses for NAD-IDH and NADP-IDH were quite different. The results indicated that two different enzymes were involved in the NAD- and NADP-IDH activities. Indirect evidence indicated that NADPH-NAD transhydrogenase activity might also be involved in the mitochondrial pathway for isocitrate oxidation. NADP-IDH activity was significantly greater than NAD-IDH activity. The oxidation of isocitrate through IDH activity was coupled to the cytochrome system by NADPH- and NADH-cytochrome c reductase activities. Citrate, via isocitrate, oxidation proceeded at a much slower rate suggesting that aconitase activity could be limiting in the oxidation of citrate. In comparison to other tissues, the prostate oxidative enzyme activities are considerably lower. The results suggest that the accumulation of high prostate citrate levels is not due to a limitation imposed by a lack of IDH activity in prostate mitochondria.
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Front Plant Sci
January 2025
National Center for Traditional Chinese Medicine (TCM) Inheritance and Innovation, Guangxi Botanical Garden of Medicinal Plants, Nanning, China.
Dihydroporphyrin iron (DH-Fe) is a novel plant growth regulator that plays significant roles in plant stress resistance. We found that is extremely sensitive to low temperature (LT) with a threshold of 25°C. To evaluate whether and how DH-Fe alleviates LT stress in , different DH-Fe concentrations (0, 10, 20, and 40 μg·L) were applied to estimate its effects on C and N metabolism and antioxidative capacity in grown under 20°C.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
Key Laboratory of Animal Biochemistry and Nutrition, Ministry of Agriculture, College of Veterinary Medicine, Henan Agricultural University, Zhengzhou 450046, Henan, China; Key Laboratory of Veterinary Biotechnology of Henan Province, College of Veterinary Medicine, Henan Agricultural University, Zhengzhou 450046, Henan, China. Electronic address:
Ammonia can cause cells to produce a large amount of reactive oxygen species (ROS), leading to the oxidative stress of cells. As the main intracellular reductant, nicotinamide adenine dinucleotide phosphate (NADPH) plays a crucial role in maintaining reduced glutathione (GSH), helping to remove ROS and protect cells from oxidative damage. Our study demonstrated that SIRT5 desuccinylated isocitrate dehydrogenase 2 (IDH2) to enhance its activity, resulting in increased NADPH production.
View Article and Find Full Text PDFMol Carcinog
January 2025
Department of Neurosurgery, The Third Affiliated Hospital of Zhengzhou University, Zhengzhou, Henan, The People's Republic of China.
RNF7 (Ring Finger Protein 7) is a key component of CRLs (Cullin-RING-type E3 ubiquitin ligases) and has been found to possess intrinsic anti-ROS capabilities. Aberrant expression of RNF7 has been observed in various tumor types and is known to significantly influence tumor initiation and progression. However, the specific role of RNF7 in glioblastoma remains unclear.
View Article and Find Full Text PDFHum Reprod
January 2025
The International Peace Maternity and Child Health Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai, China.
Study Question: Is elevated plasma molybdenum level associated with increased risk for idiopathic premature ovarian insufficiency (POI)?
Summary Answer: Elevated plasma molybdenum level is associated with an increased risk of idiopathic POI through vascular endothelial injury and inhibition of granulosa cell proliferation.
What Is Known Already: Excessive molybdenum exposure has been associated with ovarian oxidative stress in animals but its role in the development of POI remains unknown.
Study Design, Size, Duration: Case-control study of 30 women with idiopathic POI and 31 controls enrolled from August 2018 to May 2019.
J Am Chem Soc
January 2025
Department of Chemistry, University of California, Berkeley, California 94720, United States.
Dioxygen (O) is a potent oxidant used by aerobic organisms for energy transduction and critical biosynthetic processes. Numerous metalloenzymes harness O to mediate C-H bond hydroxylation reactions, but most commonly feature iron or copper ions in their active site cofactors. In contrast, many manganese-activated enzymes─such as glutamine synthetase and isocitrate lyase─perform redox neutral chemical transformations and very few are known to activate O or C-H bonds.
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