Glyoxylate reductase/hydroxypyruvate reductase regulates the free d ‐aspartate level in mammalian cells

2021 ◽  
Author(s):  
Masumi Katane ◽  
Satsuki Matsuda ◽  
Yasuaki Saitoh ◽  
Tetsuya Miyamoto ◽  
Masae Sekine ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Hydroxypyruvate Reductase ◽  
Glyoxylate Reductase

scholarly journals Purification and characterization of a novel NADPH(NADH)-dependent glyoxylate reductase from spinach leaves. Comparison of immunological properties of leaf glyoxylate reductase and hydroxypyruvate reductase

1986 ◽  
Vol 239 (3) ◽  
pp. 653-659 ◽  
Author(s):  
L A Kleczkowski ◽  
D D Randall ◽  
D G Blevins
Keyword(s):  
High Specificity ◽  
Maximal Activity ◽  
Purification And Characterization ◽  
Leaf Extracts ◽  
Hydroxypyruvate Reductase ◽  
Ph Range ◽  
Glyoxylate Reductase ◽  
Spinach Leaves

A novel reductase displaying high specificity for glyoxylate and NADPH was purified 3343-fold from spinach leaves. The enzyme was found to be an oligomer of about 125 kDa, composed of four equal subunits of 33 kDa each. A Km for glyoxylate was about 14-fold lower with NADPH than with NADH (0.085 and 1.10 mM respectively), but the maximal activity, 210 mumol/min per mg of protein, was similar with either cofactor. Km values for NADPH and NADH were 3 and 150 microM respectively. Optimal rates with either NADPH or NADH were found in the pH range 6.5-7.4. The enzyme also showed some reactivity towards hydroxypyruvate with rates less than 2% of those observed for glyoxylate. Results of immunological studies, using antibodies prepared against either glyoxylate reductase or spinach peroxisomal hydroxypyruvate reductase, suggested substantial differences in molecular structure of the two proteins. The high rates of NADPH(NADH)-glyoxylate reductase in crude leaf extracts of spinach, wheat and soya bean (30-45 mumol/h per mg of chlorophyll) and its strong affinity for glyoxylate suggest that the enzyme may be an important side component of photorespiration in vivo. In leaves of nitrogen-fixing legumes, this reductase may also be involved in ureide breakdown, utilizing the glyoxylate produced during allantoate metabolism.

Effect of Paraquat on Dark-Grown Phaseolus vulgaris Cells

Weed Science ◽  
1993 ◽  
Vol 41 (4) ◽  
pp. 528-533 ◽  
Author(s):  
Hagit Zer ◽  
Mordechai Chevion ◽  
Israel Goldberg
Keyword(s):  
Tissue Culture ◽  
Mammalian Cells ◽  
Oxidant Stress ◽  
Plant Cells ◽  
Iron Ions ◽  
Active Process ◽  
Hydroxypyruvate Reductase ◽  
Cellular Defense ◽  
Paraquat Toxicity ◽  
Eukaryotic Organisms

Paraquat is known to affect all green plants and other eukaryotic organisms including mammalian cells. The aim of this study was to improve the understanding of paraquat toxicity in nonphotosynthetic plant cells using dark-grown kidney bean cells in tissue culture. It is shown that uptake of paraquat is an active process, and that paraquat inhibits cell growth, reduces DNA synthesis, and inhibits the activity of hydroxypyruvate reductase while enhancing the activity of glutathione reductase which is involved in cellular defense against oxidant stress. Additionally, it is demonstrated that iron ions are involved in paraquat toxicity. We conclude that uptake of paraquat into cells is via polyamine channels and that the deleterious effects of paraquat on these nonphotosynthetic cells are mediated by iron.

scholarly journals Glyoxylate Reductase/Hydroxypyruvate Reductase: A Novel Prognostic Marker for Hepatocellular Carcinoma Patients after Curative Resection

Pathobiology ◽  
2013 ◽  
Vol 80 (3) ◽  
pp. 155-162 ◽  
Author(s):  
Yinglian Pan ◽  
Runzhou Ni ◽  
Qingchun Deng ◽  
Xiaodong Huang ◽  
Yixin Zhang ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Prognostic Marker ◽  
Curative Resection ◽  
Hydroxypyruvate Reductase ◽  
Glyoxylate Reductase

Structural Basis of Substrate Specificity in Human Glyoxylate Reductase/Hydroxypyruvate Reductase

2006 ◽  
Vol 360 (1) ◽  
pp. 178-189 ◽  
Author(s):  
Michael P.S. Booth ◽  
R. Conners ◽  
Gill Rumsby ◽  
R. Leo Brady
Keyword(s):  
Substrate Specificity ◽  
Structural Basis ◽  
Hydroxypyruvate Reductase ◽  
Glyoxylate Reductase

scholarly journals Integrative analysis of the hydroxypyruvate reductases revealing their distinct roles in photorespiration of Chlamydomonas

2021 ◽  
Author(s):  
Menglin Shi ◽  
Lei Zhao ◽  
Yong Wang
Keyword(s):  
Sequence Comparison ◽  
Higher Plants ◽  
Crop Improvement ◽  
Activity Measurement ◽  
Quinone Oxidoreductase ◽  
Hydroxypyruvate Reductase ◽  
Eukaryotic Organism ◽  
Physiological Metabolism ◽  
Genes Encoding ◽  
Glyoxylate Reductase

Photorespiration plays an important role in maintaining normal physiological metabolism in higher plants and other oxygenic organisms such as algae. The unicellular eukaryotic organism Chlamydomonas is reported to have a different photorespiration system from that in higher plants, and only two out of nine genes encoding photorespiratory enzymes have been experimentally characterized. Hydroxypyruvate reductase (HPR), which is responsible for the conversion of hydroxypyruvate into glycerate, is poorly understood and not yet explored in Chlamydomonas. To identify the candidate genes encoding hydroxypyruvate reductase in Chlamydomonas (CrHPR) and uncover their elusive functions, we performed sequence comparison, enzyme activity measurement, subcellular localization, and analysis of knockout/knockdown strains. Together we identify five proteins to be good candidates as CrHPRs, all of which are detected with the activity of hydroxypyruvate reductase. CrHPR1, a NADH-dependent enzyme in mitochondria, may function as the major component of photorespiration, and deletion of CrHPR1 causes severe photorespiratory defects. CrHPR2 takes parts in the cytosolic bypass of photorespiration as the compensatory pathway of CrHPR1 for the reduction of hydroxypyruvate. CrHPR4, with NADH as the cofactor, may participate in photorespiration by acting as the chloroplastidial glyoxylate reductase in glycolate-quinone oxidoreductase system. Therefore, our results reveal that the CrHPRs are far more complex than previously recognized, and provide a greatly expanded knowledge base for studies to understand how CrHPRs perform their functions in photorespiration. These will facilitate the genetic engineering for crop improvement by synthetic biology.

scholarly journals Identification and Characterization of Genes Encoding the Hydroxypyruvate Reductases in Chlamydomonas Reveal Their Distinct Roles in Photorespiration

2021 ◽  
Vol 12 ◽  
Author(s):  
Menglin Shi ◽  
Lei Zhao ◽  
Yong Wang
Keyword(s):  
Higher Plants ◽  
Crop Improvement ◽  
Activity Measurement ◽  
Quinone Oxidoreductase ◽  
Hydroxypyruvate Reductase ◽  
Eukaryotic Organism ◽  
Genes Encoding ◽  
Identification And Characterization ◽  
Glyoxylate Reductase

Photorespiration plays an important role in maintaining normal physiological metabolism in higher plants and other oxygenic organisms, such as algae. The unicellular eukaryotic organism Chlamydomonas is reported to have a photorespiration system different from that in higher plants, and only two out of nine genes encoding photorespiratory enzymes have been experimentally characterized. Hydroxypyruvate reductase (HPR), which is responsible for the conversion of hydroxypyruvate into glycerate, is poorly understood and not yet explored in Chlamydomonas. To identify the candidate genes encoding hydroxypyruvate reductases in Chlamydomonas (CrHPR) and uncover their elusive functions, we performed sequence comparison, enzyme activity measurement, subcellular localization, and analysis of knockout/knockdown strains. Together, we identify five proteins to be good candidates for CrHPRs, all of which are detected with the activity of hydroxypyruvate reductase. CrHPR1, a nicotinamide adenine dinucleotide (NADH)-dependent enzyme in mitochondria, may function as the major component of photorespiration. Its deletion causes severe photorespiratory defects. CrHPR2 takes part in the cytosolic bypass of photorespiration as the compensatory pathway of CrHPR1 for the reduction of hydroxypyruvate. CrHPR4, with NADH as the cofactor, may participate in photorespiration by acting as the chloroplastidial glyoxylate reductase in glycolate-quinone oxidoreductase system. Therefore, the results reveal that CrHPRs are far more complex than previously recognized and provide a greatly expanded knowledge base for studies to understand how CrHPRs perform their functions in photorespiration. These will facilitate both modification of photorespiration and genetic engineering for crop improvement by synthetic biology.

Ultrastructural Alterations in Hela Cells Induced by Spider Venom

1967 ◽  
Vol 25 ◽  
pp. 20-21
Author(s):  
Dale E. McClendon ◽  
Paul N. Morgan ◽  
Bernard L. Soloff
Keyword(s):  
Growth Medium ◽  
Mammalian Cells ◽  
Carcinoma Cells ◽  
Venom Protein ◽  
Sterile Saline ◽  
Carbon Coated ◽  
Available Information ◽  
Loxosceles Reclusa ◽  
Essential Growth ◽  
Solution Cultures

It has been observed that minute amounts of venom from the brown recluse spider, Loxosceles reclusa, are capable of producing cytotoxic changes in cultures of certain mammalian cells (Morgan and Felton, 1965). Since there is little available information concerning the effect of venoms on susceptible cells, we have attempted to characterize, at the electron microscope level, the cytotoxic changes produced by the venom of this spider.Cultures of human epithelial carcinoma cells, strain HeLa, were initiated on sterile, carbon coated coverslips contained in Leighton tubes. Each culture was seeded with approximately 1x105 cells contained in 1.5 ml of a modified Eagle's minimum essential growth medium prepared in Hank's balanced salt solution. Cultures were incubated at 36° C. for three days prior to the addition of venom. The venom was collected from female brown recluse spiders and diluted in sterile saline. Protein determinations on the venom-were made according to the spectrophotometric method of Waddell (1956). Approximately 10 μg venom protein per ml of fresh medium was added to each culture after discarding the old growth medium. Control cultures were treated similarly, except that no venom was added. All cultures were reincubated at 36° C.

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