Mitochondrial Lactate Dehydrogenase Is Involved in Oxidative-Energy Metabolism in Human Astrocytoma Cells (CCF-STTG1)

Lemire, Joseph; Mailloux, Ryan J.; Appanna, Vasu D.

doi:10.1371/journal.pone.0001550

Cited by 79 publications

(93 citation statements)

References 54 publications

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“…The existence of MCT and LDH proteins in mitochondria in different healthy tissues was reported previously by us (10,25) and others (2,5,34) and supported by the MitoCarta list (45). However, for first time we report on the presence of MCT and LDH isoforms in the mitochondrial reticula of breast cell lines.…”

Section: Discussionsupporting

confidence: 80%

Mitochondrial and plasma membrane lactate transporter and lactate dehydrogenase isoform expression in breast cancer cell lines

Hussien

Brooks

2011

Physiological Genomics

144

133

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Hussien R, Brooks GA. Mitochondrial and plasma membrane lactate transporter and lactate dehydrogenase isoform expression in breast cancer cell lines. Physiol Genomics 43: 255-264, 2011. First published December 21, 2010 doi:10.1152/physiolgenomics.00177.2010We hypothesized that dysregulation of lactate/pyruvate (monocarboxylate) transporters (MCT) and lactate dehydrogenase (LDH) isoforms contribute to the Warburg effect in cancer. Therefore, we assayed for the expression levels and the localizations of MCT (1, 2, and 4), and LDH (A and B) isoforms in breast cancer cell lines MCF-7 and MDA-MB-231 and compared results with those from a control, untransformed primary breast cell line, HMEC 184. Remarkably, MCT1 is not expressed in MDA-MB-231, but MCT1 is expressed in MCF-7 cells, where its abundance is less than in control HMEC 184 cells. When present in HMEC 184 and MCF-7 cells, MCT1 is localized to the plasma membrane. MCT2 and MCT4 were expressed in all the cell lines studied. MCT4 expression was higher in MDA-MB-231 compared with MCF-7 and HMEC 184 cells, whereas MCT2 abundance was higher in MCF-7 compared with MDA-MB-231 and HMEC 184 cells. Unlike MCT1, MCT2 and MCT4 were localized in mitochondria in addition to the plasma membrane. LDHA and LDHB were expressed in all the cell-lines, but abundances were higher in the two cancer cell lines than in the control cells. MCF-7 cells expressed mainly LDHB, while MDA-MB-231 and control cells expressed mainly LDHA. LDH isoforms were localized in mitochondria in addition to the cytosol. These localization patterns were the same in cancerous and control cell lines. In conclusion, MCT and LDH isoforms have distinct expression patterns in two breast cancer cell lines. These differences may contribute to divergent lactate dynamics and oxidative capacities in these cells, and offer possibilities for targeting cancer cells. glycolysis; Warburg effect; monocarboxylate transporters; lactate dehydrogenase

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Section: Discussionsupporting

confidence: 80%

Mitochondrial and plasma membrane lactate transporter and lactate dehydrogenase isoform expression in breast cancer cell lines

Hussien

Brooks

2011

Physiological Genomics

144

133

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“…The levels of fumarate, citrate, ATP, and ADP were ascertained by high-performance liquid chromatography (HPLC) as described previously (15,16). Two-milligram protein equivalents from the soluble fractions from cells grown in control, Al-stressed (15 mM Al), and Ga-stressed (1 mM) conditions for 24 h, 28 h, and 70 h were treated with 0.5% (vol/vol) perchloric acid to remove the protein.…”

mentioning

confidence: 99%

Involvement of Fumarase C and NADH Oxidase in Metabolic Adaptation ofPseudomonas fluorescensCells Evoked by Aluminum and Gallium Toxicity

Chénier

Bériault

Mailloux

et al. 2008

Appl Environ Microbiol

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Iron (Fe) is a critical element in all aerobic organisms as it participates in a variety of metabolic networks. In this study, aluminum (Al) and gallium (Ga), two Fe mimetics, severely impeded the ability of the soil microbe Pseudomonas fluorescens to perform oxidative phosphorylation. This was achieved by disrupting the activity and expression of complexes I, II, and IV. These toxic metals also inactivated aconitase (ACN) and fumarase A (FUM A), two tricarboxylic acid cycle enzymes dependent on Fe for their catalytic activity, while FUM C, an Fe-independent enzyme, displayed an increase in activity and expression under these stressed situations. Furthermore, in the Al-and Ga-exposed cells, the activity and expression of an H 2 O-forming NADH oxidase were markedly increased. The incubation of the Al-and Ga-challenged cells in an Fe-containing medium led to the recovery of the affected enzymatic activities. Taken together, these data provide novel insights into how environmental pollutants such as Al and Ga interfere with cellular Fe metabolism and also illustrate the ability of Pseudomonas fluorescens to modulate metabolic networks to combat this situation.

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“…The efficacy of this cell line stems from its maintenance of normal astrocytic properties (Mentz et al, 1999). The astrocytic cell line was cultured as described by Lemire et al (2008). The media [a-minimal essential medium (MEM)] either included fetal bovine serum (FBS) or was devoid of FBS (5 mM D-glucose is present in a-MEM).…”

Section: Materials and Methods Culturing And Isolation Of Ccf-sttg1 Cmentioning

confidence: 99%

Aluminum‐induced defective mitochondrial metabolism perturbs cytoskeletal dynamics in human astrocytoma cells

Lemire

Mailloux

Puiseux‐Dao

et al. 2008

J of Neuroscience Research

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Although aluminum (Al), a known environmental toxin, has been implicated in a variety of neurological disorders, the molecular mechanism responsible for these conditions is not fully understood. In this report, we demonstrate the ability of Al to trigger mitochondrial dysfunction and ineffective adenosine triphosphate (ATP) production. This situation severely affected cytoskeletal dynamics. Whereas the control cells had well-defined structures, the Al-exposed astrocytoma cells appeared as globular structures. Creatine kinase (CK) and profilin-2, two critical modulators of cellular morphology, were markedly diminished in the astrocytoma cells treated with Al. Antioxidants such as alpha-ketoglutarate and N-acetylcysteine mitigated the occurrence of the globular-shaped cells promoted by Al toxicity. Taken together, these data reveal an intricate link between ATP metabolism and astrocytic dysfunction and provide molecular insights into the pathogenesis of Al-induced neurological diseases.

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Mitochondrial Lactate Dehydrogenase Is Involved in Oxidative-Energy Metabolism in Human Astrocytoma Cells (CCF-STTG1)

Cited by 79 publications

References 54 publications

Mitochondrial and plasma membrane lactate transporter and lactate dehydrogenase isoform expression in breast cancer cell lines

Mitochondrial and plasma membrane lactate transporter and lactate dehydrogenase isoform expression in breast cancer cell lines

Involvement of Fumarase C and NADH Oxidase in Metabolic Adaptation ofPseudomonas fluorescensCells Evoked by Aluminum and Gallium Toxicity

Aluminum‐induced defective mitochondrial metabolism perturbs cytoskeletal dynamics in human astrocytoma cells

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