Disease relevance of Gapdh

• The expressions of glyseraldehyde-3-phosphate dehydrogenase (GAPDH), beta-actin, cyclophilin, and RPL13A were examined in order to validate the appropriate housekeeping genes for a long duration after inducing cerebral ischemia [1].

High impact information on Gapdh

• The procedure was based on the reduction of a tetrazolium salt as final electron acceptor and a multistep reaction using the exogenous or endogenous auxiliary enzymes aldolase, triosephosphate isomerase and glyceraldehyde-3-phosphate dehydrogenase [2].
• Using Western blotting of affinity-purified proteins we identified actin, glyceraldehyde-3-phosphate dehydrogenase, HSP27, protein-tyrosine phosphatase 1B, protein kinase Calpha, and the small G-protein ras as substrates for S-thiolation during reperfusion of the ischemic rat heart [3].
• Partial sequencing followed by a computer search of data banks has shown that the cloned cDNAs correspond to mRNAs encoding proteins with extensive homology to lactate dehydrogenase, glyceraldehyde 3-phosphate dehydrogenase, enolase, triose phosphate isomerase, and actin [4].
• In the cells treated with Abeta(1-42) alone, four proteins that were significantly oxidized were identified: glyceraldehyde-3-phosphate dehydrogenase, pyruvate kinase, malate dehydrogenase, and 14-3-3 zeta [5].
• However, the mRNA level of GAPDH relative to HPRT1 in rat hepatocytes was markedly increased by Rif [6].

Biological context of Gapdh

• Gene expression was measured as a percentage of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and subsequently confirmed using reverse transcriptase-polymerase chain reaction (RT-PCR) [7].
• Enzymes of glycolysis and tricarboxylic acid (TCA) cycle namely glyceraldehyde-3-phosphate dehydrogenase, aldolase A, pyruvate kinase and malate dehydrogenase were induced [8].

Anatomical context of Gapdh

• Two glycolytic enzymes, triose phosphate isomerase and glyceraldehyde 3-phosphate dehydrogenase, displayed reduced activity (48% and 68% of controls, respectively) in cauda epididymidal spermatozoa from ornidazole-fed rats, whereas the activities of hexokinase and lactate dehydrogenase remained unchanged [9].
• Myoblast C2C12 cells were exposed to dexamethasone, or dexamethasone and glutamine, and their myostatin messenger RNA and protein expression compared with glyceraldehyde-3-phosphate dehydrogenase [10].
• Levels of HSP 27, HSP 60, HSP 70, and HSP 90 mRNA were analyzed in hind limb skeletal muscle by reverse transcription-polymerase chain reaction with an endogenous internal standard, glyceraldehyde-3-phosphate-dehydrogenase [11].

Associations of Gapdh with chemical compounds

• Glucose oxidation appeared to be inhibited at the triose phosphate isomerase or glyceraldehyde 3-phosphate dehydrogenase reaction [12].
• Since previous studies demonstrated an increase in steady state glyceraldehyde-3-phosphate dehydrogenase RNA during low O2 exposure it is concluded that the level of this RNA is regulated post transcriptionally whereas the other four glycolytic enzyme RNAs are regulated at least partially at the level of transcription by oxygen availability [13].

Analytical, diagnostic and therapeutic context of Gapdh

• MALDI-TOF mass fingerprint analysis of tryptic peptides independently confirmed actin and glyceraldehyde-3-phosphate dehydrogenase S-thiolation during reperfusion [3].
• Total RNA specific for the BDV nucleoprotein (BDV-N) and the cellular genes glyceraldehyde-3-phosphate dehydrogenase (GAPDH), succinate-ubiquinone reductase (SDHA) and hypoxanthine phosphoribosyl-transferase-1 (HPRT) was measured by real-time RT-PCR and compared to BDV-infected control samples [14].

References