Tricarboxylic acid cycle dysfunction as a cause of human diseases and tumor formation

2006 ◽  
Vol 291 (6) ◽  
pp. C1114-C1120 ◽  
Author(s):  
Jean-Jacques Brière ◽  
Judith Favier ◽  
Anne-Paule Gimenez-Roqueplo ◽  
Pierre Rustin
Keyword(s):  
Succinate Dehydrogenase ◽  
Clinical Features ◽  
Tricarboxylic Acid Cycle ◽  
Tricarboxylic Acid ◽  
Tumor Formation ◽  
Human Diseases ◽  
Acid Cycle ◽  
Cycle Enzyme

A renewed interest in tricarboxylic acid cycle enzymopathies has resulted from the report that, in addition to devastating encephalopathies, these can result in various types of tumors in human. We first review the major features of the cycle that may underlie this surprising variety of clinical features. After discussing the rare cases of encephalopathies associated with specific deficiencies of some of the tricarboxylic acid cycle enzyme, we finally examine the mechanism possibly causing tumor/cancer formation in the cases of mutations affecting fumarase or succinate dehydrogenase genes.

scholarly journals Tricarboxylic acid cycle enzyme activities in a mouse model of methylmalonic aciduria

2019 ◽  
Vol 128 (4) ◽  
pp. 444-451 ◽  
Author(s):  
Parith Wongkittichote ◽  
Gary Cunningham ◽  
Marshall L. Summar ◽  
Elena Pumbo ◽  
Patrick Forny ◽  
...  
Keyword(s):  
Mouse Model ◽  
Enzyme Activities ◽  
Tricarboxylic Acid Cycle ◽  
Methylmalonic Aciduria ◽  
Tricarboxylic Acid ◽  
Acid Cycle ◽  
Cycle Enzyme

scholarly journals Succinate Dehydrogenase Loss in Familial Paraganglioma: Biochemistry, Genetics, and Epigenetics

2015 ◽  
Vol 2015 ◽  
pp. 1-14 ◽  
Author(s):  
Yeng F. Her ◽  
L. James Maher
Keyword(s):  
Succinate Dehydrogenase ◽  
Tricarboxylic Acid Cycle ◽  
Tricarboxylic Acid ◽  
Acid Cycle ◽  
Atp Production ◽  
Metabolic Defects ◽  
Biochemical Genetic

It is counterintuitive that metabolic defects reducing ATP production can cause, rather than protect from, cancer. Yet this is precisely the case for familial paraganglioma, a form of neuroendocrine malignancy caused by loss of succinate dehydrogenase in the tricarboxylic acid cycle. Here we review biochemical, genetic, and epigenetic considerations in succinate dehydrogenase loss and present leading models and mysteries associated with this fascinating and important tumor.

scholarly journals Chloroacridine derivatives as potential anticancer agents which may act as tricarboxylic acid cycle enzyme inhibitors

2020 ◽  
Vol 130 ◽  
pp. 110515
Author(s):  
Miroslawa Cichorek ◽  
Anna Ronowska ◽  
Krystyna Dzierzbicka ◽  
Monika Gensicka-Kowalewska ◽  
Milena Deptula ◽  
...  
Keyword(s):  
Anticancer Agents ◽  
Enzyme Inhibitors ◽  
Tricarboxylic Acid Cycle ◽  
Tricarboxylic Acid ◽  
Acid Cycle ◽  
Cycle Enzyme

Measurement of Tricarboxylic Acid Cycle Enzyme Activities in Plants

2017 ◽  
pp. 167-182 ◽  
Author(s):  
Rebeca Patricia Omena-Garcia ◽  
Wagner L. Araújo ◽  
Yves Gibon ◽  
Alisdair R. Fernie ◽  
Adriano Nunes-Nesi
Keyword(s):  
Enzyme Activities ◽  
Tricarboxylic Acid Cycle ◽  
Tricarboxylic Acid ◽  
Acid Cycle ◽  
Cycle Enzyme

scholarly journals The localization of enzymes of intermediary metabolism in Astasia and Euglena

1973 ◽  
Vol 134 (2) ◽  
pp. 607-616 ◽  
Author(s):  
Nicole Bégin-Heick
Keyword(s):  
Succinate Dehydrogenase ◽  
Isocitrate Lyase ◽  
Tricarboxylic Acid Cycle ◽  
Glyoxylate Cycle ◽  
Intracellular Localization ◽  
Tricarboxylic Acid ◽  
Malate Synthase ◽  
Particulate Fraction ◽  
Acid Cycle ◽  
The Glyoxylate Cycle

Results are presented on the intracellular localization of some of the enzymes of gluconeogenesis, of the tricarboxylic acid cycle and of related enzymes in Astasia and Euglena grown with various substrates. The results indicate the particulate nature of at least part of the malate synthase of Astasia and of part of the malate synthase and isocitrate lyase in Euglena. However, the presence of glyoxysomes (microbodies) in Astasia and Euglena is still open to question, since it has not, so far, been possible to separate the enzymes of the glyoxylate cycle from succinate dehydrogenase in the particulate fraction.

scholarly journals Rapid determination of tricarboxylic acid cycle enzyme activities in biological samples

2010 ◽  
Vol 11 (1) ◽  
pp. 5 ◽  
Author(s):  
Sergio Goncalves ◽  
Vincent Paupe ◽  
Emmanuel P Dassa ◽  
Jean-Jacques Brière ◽  
Judith Favier ◽  
...  
Keyword(s):  
Biological Samples ◽  
Enzyme Activities ◽  
Rapid Determination ◽  
Tricarboxylic Acid Cycle ◽  
Tricarboxylic Acid ◽  
Acid Cycle ◽  
Cycle Enzyme

scholarly journals Tricarboxylic acid-cycle and related enzymes in restricted facultative methylotrophs

1975 ◽  
Vol 148 (3) ◽  
pp. 505-511 ◽  
Author(s):  
J Colby ◽  
L J Zatman
Keyword(s):  
Succinate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Isocitrate Dehydrogenase ◽  
Tricarboxylic Acid Cycle ◽  
Tricarboxylic Acid ◽  
Methylotrophic Bacteria ◽  
Acid Cycle ◽  
Oxoglutarate Dehydrogenase ◽  
Specific Activities ◽  
Succinyl Coa Synthetase

The isolation is described of pure cultures of three non-methane-utilizing methylotrophic bacteria which, together with the previously described Bacillus PM6, have a very limited range of growth substrates; these organisms are designated “restricted facultative’ methylotrophs. Two of these isolates, W6A and W3A1, grow only on glucose out of 50 non-C1 compounds tested, whereas the third isolate S2A1 and Bacillus PM6 grow on betaine, glucose, gluconate, alanine, glutamate, citrate and nutrient agar, but not on any of a further 56 non-C1 compounds. Crude sonic extracts of trimethylamine-grown and glucose-grown W6A and W3A1 isolates, and of trimethylamine-grown C2A1 (an obligate methylotroph) contain (i) no detectable 2-oxogltarate dehydrogenase activity, (ii) very low or zero specific activities of succinate dehydrogenase and succinyl-CoA synthetase and (iii) NAD+-dependent isocitrate dehydrogenase activity. Extracts of trimethylamine-grown PM6 and S2A1 methylotrophs have (i) very low 2-oxoglutarate dehydrogenase specific activities, (ii) comparatively high specific activities of succinate dehydrogenase, malate dehydrogenase and succinyl-CoA synthetase and (iii) NADP+-dependent isocitrate dehydrogenase activity but no NAD+-dependent isocitrate dehydrogenase activity. The activities of most of these enzymes are increased during growth on glucose, alanine, glutamate or citrate, but only very low 2-oxoglutarate dehydrogenase activities are present under all growth conditions. The restricted facultative methylotrophs grow on certain non-C1 compounds in the absence of 2-oxoglutarate dehydrogenase and, in some cases, of other enzymes of the tricarboxylic acid cycle; these lesions cannot therefore be the sole cause of obligate methylotrophy.

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