Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.2.1.13 (glyceraldehyde-3-phosphate dehydrogenase)
 6,511 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Roosters homozygous for the rose comb allele (R/R) are subfertile. In previous research, these subfertile roosters were characterized by an in vitro sperm penetration assay as having limited sperm motility. The objectives in the present study were to characterize sperm motility by computer-assisted sperm motion analysis and to account for a mechanism underlying poor sperm motility. Percentages of motile sperm differed between subfertile males and fertile controls (r/r) by 29% (p < 0.001). The concentration of intracellular ATP in sperm form subfertile roosters was less than in that from fertile controls (p < 0.001). The genotypic difference is sperm motility, as measured with the sperm penetration assay, was maintained when ATP production was dependent on anaerobic glycolysis (p < 0.001). In this case, sperm were incubated with exogenous glucose and cyanide. Consequently, we could not attribute the genotypic difference in sperm mobility to mitochondrial respiration. In contrast, glucose transport, as measured by the uptake of [1,2-3H]-2-deoxy-D-glucose, was reduced in sperm from subfertile roosters (p < 0.001). Neither hexokinase nor glyceraldehyde-3-phosphate dehydrogenase activity differed between genotypes (p > 0.05). Likewise, lactate dehydrogenase activity did not differ between genotypes (p > 0.05). As evidenced by creatine kinase activity and dynein ATPase activity, neither the potential for energy transfer nor utilization within the axoneme differed between genotypes (p > 0.05). Therefore, we attribute the subfertility of roosters homozygous for the rose comb allele to decreased spermatozoal glucose transport.
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PMID:Reduced glucose transport in sperm from roosters (Gallus domesticus) with heritable subfertility. 931 82

Creatine kinase (CK) plays a crucial role in cardiac energy transduction. During chronic cardiac stress conditions leading to hypertrophy and/or heart failure, the profile of CK isoenzyme activities changes towards a fetal pattern with increases of BB- and MB-CK and decreases of MM-CK and mito-CK. Changes of myocardial CK gene expression are only indirectly reflected by measurements of CK activities. The purpose of this work was, therefore, to determine myocardial expression of B-, M- and sarcomeric mito-CK genes in an animal model of heart failure where hemodynamic alterations and CK system changes are well defined, that is, in the rat heart post-myocardial infarction. Intact residual left ventricular myocardium was harvested 2 months following infarction (MI; n = 7) or sham operation (sham; n = 6) after in vivo left-ventricular end-diastolic pressure (LVEDP) was recorded. Total CK activity was measured spectrophotometrically, CK isoenzyme distribution with agarose gel electrophoresis. Steady state mRNA levels coding for B-, M- and mito-CK genes were measured with quantitative PCR and were normalized for GAPDH expression. Total CK activity tended to be reduced in MI (5.51 +/- 0.62 IU/mg protein) compared to sham (6.77 +/- 0.24; P = 0.55). CK isoenzyme distribution showed an increase of fetal BB- + MB-CK (MI 22.0 +/- 3.1%, sham 15.1 +/- 1.0%; P < 0.05), no change of MM-CK and a decrease of mito-CK (27.0 +/- 1.5% sham, 20.8 +/- 2.0% MI: P < 0.05). Relative B-CK mRNA levels increased (sham 0.46 +/- 0.06, MI 1.03 +/- 0.09; P < 0.05) and M-CK mRNA levels decreased (sham 1.06 +/- 0.08. MI 0.66 +/- 0.09; P < 0.05) significantly post-MI. The increase of B-CK mRNA (r = 0.72; P = 0.009) and the decrease of M-CK mRNA (r = 0.76; P = 0.003) correlated significantly with in vivo LVEDP. Mito-CK mRNA levels remained unchanged after MI (sham 0.94 +/- 0.16, MI 0.98 +/- 0.09). Intact residual left-ventricular myocardium post-MI is characterized by increased B-CK-mRNA and reduced M-CK-mRNA expression.
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PMID:Changes of creatine kinase gene expression in rat heart post-myocardial infarction. 960 29

We have recently discovered an alternative function of the putative metastasis suppressor protein Nm23, which is identical to nucleoside diphosphate kinase, as a protein phosphotransferase in vitro. While purified native Nm23 protein did not phosphorylate other proteins, we could purify a Nm23-associated protein that activates the protein phosphotransferase function; it was identified as a glyceraldehyde-3-phosphate dehydrogenase (GAPDH) isoenzyme. Co-expression and purification of (His)6-tagged GAPDH in combination with either Nm23-H1 or Nm23-H2 in baculovirus-infected Sf9 cells showed that only Nm23-H1, but not Nm23-H2, forms a stable complex with GAPDH. Protein phosphotransferase activity was confirmed for the recombinant GAPDH.Nm23-H1 complex but not for either of the enzymes alone, nor was this activity observed after simple mixing of the purified proteins in vitro. The molecular mass of the highly purified recombinant GAPDH.Nm23-H1 complex suggests that a dimer of GAPDH interacts with a dimer of Nm23-H1. In contrast to the complex with GAPDH, co-expression of Nm23-H1 with antioxidant protein (MER-5) or creatine kinase did not activate the protein phosphotransferase function, indicating that this activation may specifically require GAPDH as a binding partner.
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PMID:Glyceraldehyde-3-phosphate dehydrogenase and Nm23-H1/nucleoside diphosphate kinase A. Two old enzymes combine for the novel Nm23 protein phosphotransferase function. 968 45

The USDA Food Safety and Inspection Service has proposed to amend cooking regulations to require that any thermal process used for poultry products be sufficient to cause a 7 D reduction in salmonellae. Several enzymes have been suggested as potential indicators of heat processing in poultry, yet no relationship between the inactivation rates of these enzymes and salmonellae had been determine. The thermal inactivation kinetics of endogenous muscle proteins. Escherichia coli O157:H7 and Salmonella senftenberg were compared in ground turkey thigh meat in thermal death time studies. Bacteria counts were determined and muscle extracts were assayed for residual enzyme activity or protein concentration D and zeta values were calculated using regression analysis. S. senftenberg had higher D values at all temperatures and was more heat resistant than E. coli. The zeta values of E. coli on Petrifilm Coliform Count plates and phenol red sorbitol agar plates were 6.0 and 5.7 degrees C, respectively. The zeta values of S. senftenberg were 5.6 and 5.4 degrees C on Petrifilm and agar, respectively. Lactate dehydrogenase (LDH) was the most heat stable protein at 64 degrees C. LDH, glyceraldehyde-3-phosphate dehydrogenase, creatine kinase, triose phosphate isomerase (TPI), acid phosphatase, serum albumin, and immunoglobulin G had zeta values of 3.8,4.3,4.8,5.8,6.3,6.7, and 8.6 degrees C, respectively , in turkey containing 4.3% fat. The zeta values for TPI decreased to 5.4 degrees C in thigh meat containing 9.8% fat. Temperature function of TPI was most similar to that of S. senftenberg, suggesting it might function as an endogenous time-temperature integrator to monitor adequacy of processing when a performance standard based on this pathogen is implemented.
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PMID:Thermal inactivation of Escherichia coli O157:H7, Salmonella senftenberg, and enzymes with potential as time-temperature indicators in ground turkey thigh meat. 970 76

Muscle disuse induces substantial alterations in the highly plastic skeletal muscle tissues, which occur especially in antigravity slow muscles. We differentially screened a muscle cDNA array to identify modifications in gene profile expression induced in slow rat soleus muscle mechanically unloaded by hindlimb suspension as a model for muscle disuse. This study focused on muscle creatine kinase mRNA and protein and glyceraldehyde-3-phosphate dehydrogenase mRNA, which were found to be upregulated in unweighted muscles. These upregulations were analyzed over a 4-wk time course of hindlimb suspension and compared with variations in myosin heavy chain (MHC) isoforms while specifically focusing on type IIx MHC mRNA and protein. The two metabolic marker upregulations clearly preceded IIx MHC contractile protein upregulation. Muscle creatine kinase upregulation was shown to be an excellent, and the earliest, marker of muscle disuse at mRNA and protein levels.
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PMID:Upregulation of M-creatine kinase and glyceraldehyde3-phosphate dehydrogenase: two markers of muscle disuse. 995 Sep 6

We investigated the effect of sublethal concentrations of hypochlorous acid (HOCl) on intracellular thiol groups. Exposure of human umbilical vein endothelial cells to HOCl caused a decrease in cell viability, with concentrations of </=25 microM HOCl being sublethal. At these concentrations, we saw a loss of glutathione and total protein thiol groups. Of the thiol enzymes we investigated, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was particularly susceptible to inactivation, creatine kinase was moderately susceptible, and lactate dehydrogenase was unaffected by HOCl at the concentrations used. Similar results were obtained with HOCl generated over 30 min by myeloperoxidase. GAPDH activity could be regenerated on reincubation of cells in Hanks' balanced salt solution or reduction with dithiothreitol. In contrast, glutathione loss was not reversible, and further decreased with time. Cellular ATP levels decreased with sublethal HOCl concentrations and this appeared to be unrelated to the inactivation of GAPDH. Our results demonstrate that intracellular thiol groups differ in their reactivity with HOCl and suggest that HOCl may be able to regulate specific cellular functions.
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PMID:Loss of GSH and thiol enzymes in endothelial cells exposed to sublethal concentrations of hypochlorous acid. 1051 89

A new analytical approach has been applied to the determination and characterization of mercury-accessible -SH groups in pure native protein samples (ovalbumin, hemoglobin, glyceraldehyde-3-phosphate dehydrogenase, aldolase, pyruvate kinase, hexokinase, lactate dehydrogenase, alcohol dehydrogenase, creatine phosphokinase, lysozyme, and cytochrome c). The method is based on the selective reduction of Hg(II) in the presence of Hg(II)-thiol complexes with alkaline sodium tetrahydroborate, to give Hg(0) in a continuous flow reaction system coupled with atomic fluorescence spectrometric (AFS) detection. The method is fast and specific and allows one to work with nanomole amounts of a single protein without any preliminary incubation and without any separation of Hg(II) from thiol-complexed mercury. The meaning of the results obtained in the determination of the accessible -SH groups in native proteins by using chemical probes is discussed.
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PMID:Application of mercury cold vapor atomic fluorescence spectrometry to the characterization of mercury-accessible -SH groups in native proteins. 1052 12

We investigated the effect of dopa and dopamine on creatine kinase (CK) activity in the presence of ferrylmyoglobin (ferrylMb). CK was sharply inhibited by dopa and dopamine in the presence of ferrylMb. Dopa and dopamine markedly promoted the reduction of ferrylMb to metmyoglobin (metMb). The semiquinone from dopa and dopamine may be involved in CK inactivation. During inactivation of the enzyme, both kinetic parameters Vmax and Km changed. In addition, reduced glutathione restored the activity of CK at an early stage. These results suggest that inactivation of CK is dominantly due to oxidation of sulfhydryl (SH) groups of the enzyme. Other catechols, such as adrenaline and noradrenaline, little inactivated CK activity, whereas they promoted the reduction of ferrylMb to metMb. Other SH enzymes, including alcohol dehydrogenase (ADH) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH), were inactivated to a lesser extent by dopa and dopamine in the presence of ferrylMb. Adrenaline and noradrenaline did not significantly prevent the inactivation of ADH and very slightly inhibited GAPDH. These results suggest that dopa and dopamine act as prooxidants to inactivate SH enzymes in the presence of ferrylMb.
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PMID:Inactivation of creatine kinase induced by dopa and dopamine in the presence of ferrylmyoglobin. 1059 1

Coupling of ATP-generating with ATP-consuming processes is an essential component in the cardiac bioenergetics responsible for optimal myocardial function. Although a number of enzymatic systems have been implicated in securing proper intracellular energy communication, their integrative response in a failing myocardium has not been determined so far. Therefore, we measured catalytic activities of enzymes responsible for the communication between ATP-generating and ATP-consuming processes in ventricular samples obtained from normal dogs and dogs with tachycardia-induced heart failure. In the failing myocardium, phosphotransfer activities of creatine kinase, adenylate kinase, 3-phosphoglycerate kinase and pyruvate kinase, which collectively deliver ATP and remove ADP from myofibrillar ATPases, were depressed by 30, 21, 44 and 20%, respectively, when compared to normal controls. The activity of hexokinase, an enzyme which directs phosphoryls into the glycolytic phosphotransfer pathway, was unchanged. Also, the activity of glyceraldehyde-3-phosphate dehydrogenase, which may shuttle inorganic phosphate between ATPases and ATP-synthases, was not affected by heart failure. However, the CO2-hydration activity of carbonic anhydrase, which together with creatine kinase, is presumed responsible for removal of protons from ATPases, was diminished by 21%. As these enzymatic systems are collectively required for adequate delivery of high-energy phosphoryl to, and removal of end-products from, cellular ATPases, the cumulative deficit in their flux capacities may provide a bioenergetic basis for impaired contraction-relaxation in the failing heart.
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PMID:Reduced activity of enzymes coupling ATP-generating with ATP-consuming processes in the failing myocardium. 1063 Jun 20

Site-specific S-glutathionylation is emerging as a novel mechanism by which S-nitrosoglutathione (GSNO) may modify functionally important protein thiols. Here, we show that GSNO-Sepharose mimicks site-specific S-glutathionylation of the transcription factors c-Jun and p50 by free GSNO in vitro. Both c-Jun and p50 were found to bind to immobilized GSNO through the formation of a mixed disulphide, involving a conserved cysteine residue located in the DNA-binding domains of these transcription factors. Furthermore, we show that c-Jun, p50, glycogen phosphorylase b, glyceraldehyde-3-phosphate dehydrogenase, creatine kinase, glutaredoxin and caspase-3 can be precipitated from a mixture of purified thiol-containing proteins by the formation of a mixed-disulphide bond with GSNO-Sepharose. With few exceptions, protein binding to this matrix correlated well with the susceptibility of the investigated proteins to undergo GSNO- but not diamide-induced mixed-disulphide formation in vitro. Finally, it is shown that covalent GSNO-Sepharose chromatography of HeLa cell nuclear extracts results in the enrichment of proteins which incorporate glutathione in response to GSNO treatment. As suggested by DNA-binding assays, this group of nuclear proteins include the transcription factors activator protein-1, nuclear factor-kappaB and cAMP-response-element-binding protein. In conclusion, we introduce GSNO-Sepharose as a probe for site-specific S-glutathionylation and as a novel and potentially useful tool to isolate and identify proteins which are candidate targets for GSNO-induced mixed-disulphide formation.
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PMID:Novel application of S-nitrosoglutathione-Sepharose to identify proteins that are potential targets for S-nitrosoglutathione-induced mixed-disulphide formation. 1088 Mar 56


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