Crowding-Induced Uncompetitive Inhibition of Lactate Dehydrogenase: Role of Entropic Pushing

2020 ◽  
Vol 124 (5) ◽  
pp. 727-734 ◽  
Author(s):  
Marin Matić ◽  
Suman Saurabh ◽  
Josef Hamacek ◽  
Francesco Piazza
Keyword(s):  
Lactate Dehydrogenase ◽  
Uncompetitive Inhibition

scholarly journals Role of glycerol 3-phosphate dehydrogenase in glyceride metabolism. Effect of diet on enzyme activities in chicken liver

1975 ◽  
Vol 146 (1) ◽  
pp. 223-229 ◽  
Author(s):  
J W Harding ◽  
E A Pyeritz ◽  
E S Copeland ◽  
H B White
Keyword(s):  
Lactate Dehydrogenase ◽  
High Fat Diet ◽  
Acyl Carrier Protein ◽  
Fatty Acid Synthetase ◽  
Carrier Protein ◽  
High Fat ◽  
Carbohydrate Diet ◽  
Metabolic Role ◽  
Glycerol 3 Phosphate Dehydrogenase

1. The metabolic role of hepatic NAD-linked glycerol 3-phosphate dehydrogenase (EC 1.1.1.8) was investigated vis-a-vis glyceride synthesis, glyceride degradation and the maintainence of the NAD redox state. 2. Five-week-old chickens were placed on five dietary regimes: a control group, a group on an increased-carbohydrate-lowered-fat diet, a group on a high-fat-lowered-carbohydrate diet, a starved group and a starved-refed group. In each group the specific activity (mumol/min per g wet wt. of tissue) of hepatic glycerol 3-phosphate dehydrogenase was compared with the activities of the β-oxoacyl-(acyl-carrier protein) reductase component of fatty acid synthetase, glycerol kinase (EC 2.7.1.30) and lactate dehydrogenase (EC 1.1.1.27). 3. During starvation, the activities of glycerol 3-phosphate dehydrogenase, glycerol kinase and lactate dehydrogenase rose significantly. After re-feeding these activities returned to near normal. All three activities rose slightly on the high-fat diet. Lactate dehydrogenase activity rose slightly, whereas those of the other two enzymes fell slightly on the increased-carbohydrate-lowered-fat diet. 4. The activity of the β-oxoacyl-(acyl-carrier protein) reductase component of fatty acid synthetase, a lipid-synthesizing enzyme, contrasted strikingly with the other three enzyme activities. Its activity was slightly elevated on the increased-carbohydrate diet and significantly diminished on the high-fat diet and during starvation. 5. The changes in activity of the chicken liver isoenzyme of glycerol 3-phosphate dehydrogenase in response to dietary stresses suggest that the enzyme has an important metabolic role other than or in addition to glyceride biosynthesis.

scholarly journals The Role of Plasma Lactate Dehydrogenase Testing in the Prediction of Severe Conditions in Newborn Infants: A Prospective Study

2020 ◽  
Vol Volume 10 ◽  
pp. 31-35
Author(s):  
Ton Nu Van Anh ◽  
Tran Kiem Hao ◽  
Huynh Huu Hoang
Keyword(s):  
Lactate Dehydrogenase ◽  
Prospective Study ◽  
Newborn Infants ◽  
Plasma Lactate ◽  
A Prospective Study

scholarly journals Role of lactate dehydrogenase (LDH) in identifying relapse for patients with stage I testis cancer on active surveillance

2020 ◽  
Vol 19 ◽  
pp. e400
Author(s):  
A. Bobrowski ◽  
L. Landoni ◽  
L. Anson-Cartwright ◽  
A. Hansen ◽  
P. Chung ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Active Surveillance ◽  
Stage I ◽  
Testis Cancer

pHe, [Ca2+]e, and cell death during metabolic inhibition: role of phospholipase A2 and sarcolemmal phospholipids

1998 ◽  
Vol 274 (1) ◽  
pp. H18-H26 ◽  
Author(s):  
Jan A. Post ◽  
Sheng-Yong Wang ◽  
Glenn A. Langer
Keyword(s):  
Cell Death ◽  
Arachidonic Acid ◽  
Lactate Dehydrogenase ◽  
Present Model ◽  
Cell Lysis ◽  
Metabolic Inhibition ◽  
Ldh Release ◽  
External Ph ◽  
Sarcolemmal Integrity

This study measures cellular lactate dehydrogenase (LDH) release during metabolic inhibition as a monitor of sarcolemmal integrity as affected by variation of external pH (pHe) and Ca2+ concentration ([Ca2+]e). The sigmoidal relationship between pHe and LDH release and pHe and net Ca2+ uptake was essentially identical with the 50% maximal value occurring at pH 7.0 for both. This suggests that a process(es) sensitive to both pHe and [Ca2+]eplays a role in cell lysis during the course of metabolic inhibition. Variation of pHe during metabolic inhibition did not alter the decline in cellular ATP, nor did it affect changes in sarcolemmal phospholipid topology. Intracellular pH followed changes of pHe with a few minutes lag. Cell lysis increased in a graded manner as pHe and [Ca2+]ewere increased, but pHe was the sole determinant of lysis, i.e., [Ca2+]elevel had no effect, at the lowest (6.2) and the highest (8.0) pHe levels. pHe variation did not affect the release of radiolabeled arachidonic acid, nor did inhibitors of phospholipase A2(PLA2) affect cell lysis at varying pHe. Therefore, cellular PLA2 activation could not be implicated for a role in cell lysis in the present model of metabolic inhibition. Alternatively, we propose that Ca2+ binding to the cytoplasmic leaflet, in combination with membrane alterations secondary to the metabolic insult, combine to destabilize the sarcolemma (20). This Ca2+ binding to the negatively charged phosphatidylserine results in the expression of the bilayer destabilizing effect of phosphatidylethanolamine. This Ca2+ binding is greatly diminished by lowered pH, resulting in an attenuation of cell lysis.

scholarly journals The prognostic role of lactate dehydrogenase serum levels in patients with hepatocellular carcinoma who are treated with sorafenib: the influence of liver fibrosis

2016 ◽  
Vol 7 (4) ◽  
pp. 615-623 ◽  
Author(s):  
Masayoshi Yada ◽  
Masayuki Miyazaki ◽  
Kenta Motomura ◽  
Akihide Masumoto ◽  
Makoto Nakamuta ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Lactate Dehydrogenase ◽  
Liver Fibrosis ◽  
Serum Levels ◽  
Prognostic Role

Major role of lactate dehydrogenase D-LDH1 for the synthesis of lactic acid in Fructobacillus tropaeoli CRL 2034

2020 ◽  
Vol 104 (17) ◽  
pp. 7409-7426
Author(s):  
Juliana Bleckwedel ◽  
Florencia Mohamed ◽  
Fernanda Mozzi ◽  
Raúl Ricardo Raya
Keyword(s):  
Lactic Acid ◽  
Lactate Dehydrogenase
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