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Moderate to strong cytoplasmic immunoreactivity was observed in liver cancers and several malignant melanomas, thyroid, endometrial, colorectal, cervical, lung and prostate cancers along with a few lung, renal and pancreatic cancers. Remaining cancer tissues were in general weakly stained or negative.
The pyruvate dehydrogenase (PDH) complex is a nuclear-encoded mitochondrial multienzyme complex that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It provides the primary link between glycolysis and the tricarboxylic acid (TCA) cycle, and thus is one of the major enzymes responsible for the regulation of glucose metabolism. The enzymatic activity of PDH is regulated by a phosphorylation/dephosphorylation cycle, and phosphorylation results in inactivation of PDH. The protein encoded by this gene is one of the three pyruvate dehydrogenase kinases that inhibits the PDH complex by phosphorylation of the E1 alpha subunit. This gene is predominantly expressed in the heart and skeletal muscles. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Mar 2010]
Enzymes ENZYME proteins Transferases Kinases Atypical kinases Predicted intracellular proteins Disease related genes Potential drug targets Protein evidence (Kim et al 2014) Protein evidence (Ezkurdia et al 2014)
Enzymes ENZYME proteins Transferases Kinases Atypical kinases Predicted intracellular proteins Disease related genes Potential drug targets Protein evidence (Kim et al 2014) Protein evidence (Ezkurdia et al 2014)
