Results 201 to 210 of about 30,591 (234)
Hydrogen cyanide acts as a regulator of reactive oxygen species metabolism. [PDF]
Piekarniak M +3 more
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Proline dehydrogenase (oxidase) in cancer
AbstractProline dehydrogenase (oxidase, PRODH/POX), the first enzyme in the proline degradative pathway, plays a special role in tumorigenesis and tumor development. Proline metabolism catalyzed by PRODH/POX is closely linked with the tricarboxylic acid (TCA) cycle and urea cycle.
James M Phang
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Regulation and function of proline oxidase under nutrient stress [PDF]
AbstractUnder conditions of nutrient stress, cells switch to a survival mode catabolizing cellular and tissue constituents for energy. Proline metabolism is especially important in nutrient stress because proline is readily available from the breakdown of extracellular matrix (ECM), and the degradation of proline through the proline cycle initiated by ...
Jui Pandhare +2 more
exaly +3 more sources
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Overexpression of proline oxidase induces proline-dependent and mitochondria-mediated apoptosis
Molecular and Cellular Biochemistry, 2006Proline oxidase (POX), a mitochondrial inner-membrane protein, catalyzes the rate-limiting oxidation of proline to pyrroline- 5-carboxylate (P5C). Previously we showed that overexpression of POX is associated with generation of reactive oxygen species (ROS) and apoptosis in POX-inducible colorectal cancer cells, DLD-1.POX.
Chien-An A Hu, Steven P Donald, Jian Yu
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PROLINE OXIDASES IN HANSENULA SUBPELLICULOSA
Journal of Bacteriology, 1964Ling, Chung-Mei (Illinois Institute of Technology, Chicago), and L. R. Hedrick . Proline oxidases in Hansenula subpelliculosa . J. Bacteriol. 87: 1462–1470.
C M, LING, L R, HEDRICK
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BioFactors, 2016
AbstractProlidase is a cytosolic imidodipeptidase that specifically splits imidodipeptides with C‐terminal proline or hydroxyproline. The enzyme plays an important role in the recycling of proline from imidodipeptides for resynthesis of collagen and other proline‐containing proteins.
Ilona Zaręba, Jerzy Palka
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AbstractProlidase is a cytosolic imidodipeptidase that specifically splits imidodipeptides with C‐terminal proline or hydroxyproline. The enzyme plays an important role in the recycling of proline from imidodipeptides for resynthesis of collagen and other proline‐containing proteins.
Ilona Zaręba, Jerzy Palka
exaly +3 more sources
Glucocorticoid control of hepatic proline oxidase
Metabolism, 1977Since adrenal corticosteroids are known to affect amino acid metabolism and gluconeogenesis, we examined the relationship of these hormones to hepatic proline oxidase, the mitochondrial enzyme degrading L-proline. In adrenalectomized rats hepatic proline oxidase activity decreased to about 50% of control levels within 5-6 days.
E M, Kowaloff, A S, Granger, J M, Phang
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Proline oxidase in cultured mammalian cells
Journal of Cellular Physiology, 1977AbstractWe sought a cultured cell line with Proline Oxidase activity to study the regulation and physiologic role of the enzyme in mammalian tissues. Among the cell lines tested, only LLC‐RK1 cells, derived from rabbit kidney, had significant Proline Oxidase activity; the Km for proline of the enzyme from these cells was similar to that for the liver ...
S J, Downing +4 more
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Proline Oxidase (POX) as A Target for Cancer Therapy
Current Drug Targets, 2015Proline dehydrogenase/proline oxidase (PRODH/POX) is an enzyme catalyzing the first step of proline degradation, during which ROS and/or ATP is generated. POX is widely distributed in living organisms and is responsible for a number of regulatory processes such as redox homeostasis, osmotic adaptation, cell signaling and oxidative stress.
Joanna, Kononczuk +5 more
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Characteristics of proline oxidase in rat tissues.
Journal of biochemistry, 1980In adult rats the activity of proline oxidase is high in the liver and kidney and moderate in the brain and heart, but it is not detectable in the lung, skeletal muscle, spleen, or small intestine. The activity in the liver is 1.5 times higher in females than males.
Y, Kawabata, N, Katunuma, Y, Sanada
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