Pyruvate Dehydrogenase E1-alpha subunit: Understanding the Catalysts in Glycolysis

Thu, 12/29/2016 - 14:01

Pyruvate Dehydrogenase E1-alpha subunit (PDHA1) is one of multiple enzymes in a mitochondrial complex, called the Pyruvate Dehydrogenase (PDH) complex, involved in the transition between glycolysis and the tricarboxylic acid (TCA) cycle during cellular respiration. The PDHA1 enzyme catalyzes the reaction that produces acetyl-CoA and CO2 from pyruvate (1). PDHA1 also regulates the PDH complex through reversible phosphorylation.

PDHA1 antibody

Pyruvate Dehydrogenase E1-alpha subunit [p Ser293] Antibody [NB110-93479] - Pyruvate Dehydrogenase E1-alpha subunit [p Ser293] antibody (1:250) was tested in HeLa cells with Dylight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and Dylight 550 (red).

PDHA1 deficiencies cause major deficits in metabolism of carbohydrates and consequently energy production, which negatively impacts development of the brain in utero. Mild deficiencies can cause developmental delays or seizures, while severe deficiencies can cause epilepsy or death. PDHA1 deficiency is X-linked, so the disorder affects males more than females (1). A deficiency of Pyruvate Dehydrogenase E1-alpha subunit is also the leading cause of lactic acidosis in children (2). Lactic acidosis is a metabolic condition in which lactic acid collects in the bloodstream at a faster rate than it can be removed.

The inactive form of the pyruvate dehydrogenase complex contributes to malignant phenotypes in multiple cancers (3). In tumor cells, researchers found that despite the presence of oxygen, pyruvate was reacting to form lactate instead of acetyl-CoA. This is known as the Warburg effect, and a high concentration of the inactive form of the pyruvate dehydrogenase complex in cancer cells is a known cause. The inactive form of PDH complex, when produced at high levels, discourages conversion of pyruvate into acetyl-CoA. p53 expression decreases the activity of the inactive form of the Pyruvate dehydrogenase complex, which in turn promotes normal pyruvate metabolism (4). In order to fully understand the benefits of PDHA1 and the damages that mutations can cause, more research must be conducted.


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  1. Prasad C, Rupar T, Prasad AN. Pyruvate dehydrogenase deficiency and epilepsy [PMID 21908116]
  2. Lib MY, Brown RM, Brown GK, Marusich MF, Capaldi RA. Detection of pyruvate dehydrogenase E1 alpha-subunit deficiencies in females by immunohistochemical demonstration of mosaicism in cultured fibroblasts [PMID: 12070266]
  3. McFate T, Mohyeldin A, Lu H, Thakar J, Henriques J, Halim ND, Wu H, Schell MJ, Tsang TM, Teahan O, Zhou S, Califano JA, Jeoung NH, Harris RA, Verma A. Pyruvate dehydrogenase complex activity controls metabolic and malignant phenotype in cancer cells. [PMID: 18541534]
  4. Contractor T, Harris CR. p53 negatively regulates transcription of the pyruvate dehydrogenase kinase Pdk2. [PMID: 22123926]

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