Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.11.1.7 (peroxidase)
 65,474 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The interaction of CrADP, an exchange-inert paramagnetic analogue of Mg-ADP, with yeast hexokinase has been studied by measuring the effects of CrADP on the longitudinal nuclear relaxation rate (1/T1) of the protons of water and the protons and phosphorus atom of enzyme-bound glucose-6-P. The paramagnetic effect of CrADP on 1/T1 of water protons is enhanced upon complexation with the enzyme. Titrations measuring this paramagnetic effect at several enzyme concentrations in the presence of glucose-6-P yielded a characteristic enhancement factor for 1/T1 of water protons and the dissociation constant of CrADP from the ternary enzyme . ADPCr . glucose-6-P complex. The latter value (2 mM) is similar to that obtained from kinetic inhibition studies (Danenberg and Cleland [1975]. Biochemistry. 14:28). The presence of glucose-6-P increased the enhancement of the water relaxation rate by enzyme-bound CrADP, suggesting the formation of an enzyme . CrADP . glucose-6-P complex. The existence of such a complex was confirmed by the observation of a paramagnetic effect of enzyme-bound CrADP on the l/T1 of the 31P-nucleus and protons of enzyme-bound glucose-6-P. From the paramagnetic effects of enzyme-bound CrADP on the relaxation rates of the 31P-nucleus and the carbon-bound protons of glucose-6-P in the enzyme . ADPCr . glucose-6-P complex, using the correlation time of approximately 0.7 ns, determined from the magnetic field-dependence of 1/T1 of water protons over the range 24.3-360 MHz, a Cr3+ to phosphorus distance of 6.6 +/- 0.7 A and Cr3+ to alpha- and beta-anomeric proton distances of 8.9 and 9.7 A were calculated. These results imply the absence of a direct coordination of the phosphoryl group of glucose-6-P by the nucleotide-bound metal on hexokinase but indicate van der Waals contact between a phosphoryl oxygen of glucose-6-P and the hydration sphere of the nucleotide-bound metal. The distances are consistent with a model that assumes molecular contact between the phosphorus of glucose-6-P and a beta-phosphoryl oxygen of ADP suggesting an associative phosphoryl transfer. Because after phosphorylation of ADP, the metal ion is coordinated to the transferred phosphoryl group, the overall migration of the phosphoryl group during the phosphoryl transfer is approximately 3.6 A toward the nucleotide-bound metal. Little or no catalysis of phosphoryl transfer from glucose-6-P to alpha, beta-bidentate or beta-monodentate CrADP ( less than or equal to 0.05% of the rate found with MgADP) occurred in the presence of hexokinase, as monitored by glucose formation in a coupled assay system using glucose oxidase and peroxidase. The ability of beta, gamma-bidentate CrATP to act as a substrate (Danenberg and Cleland [1975].
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PMID:Magnetic resonance studies of the spatial arrangement of glucose-6-phosphate and chromium (III)-adenosine diphosphate at the catalytic site of hexokinase. 23 78

When stimulated with different stimuli, neutrophils generate various active oxygen species. These active oxygen molecules can be analyzed by luminol chemiluminescence (LCL). Phosphatidylserine (PS)-liposomes increased the formylmethionyl-leucyl-phenylalanine-induced LCL of guinea pig peritoneal neutrophils without affecting their oxygen consumption and superoxide (O2.-) generation. Similar effects of PS-liposomes were also observed in LCL of neutrophils stimulated by phorbol myristate acetate or arachidonic acid but not by opsonized zymosan. Kinetic analysis revealed that the PS-liposome-induced increase in LCL depended on extracellulary generated O2.-. Moreover, the stimulatory effect of PS could be seen only when it formed liposomal membranes. The effect of PS-liposomes was also inhibited by superoxide dismutase, catalase, and deferoxamine, an iron chelator, but not by azide, an inhibitor of myeloperoxidase. Similar enhancement of stimulation-dependent LCL response was also observed with Fe3+ and ADP-Fe3+, but the degree of enhancement was much greater with PS-liposomes than with iron and its complex. The increase in hydroxyl radical generation by PS-liposome-treated neutrophils was confirmed by experiments with EPR spectrometry using spin-trapping agents. These results suggested that the interaction of neutrophils with PS-containing membrane surface might generate reactive oxygen species that enhance the stimulus-dependent LCL response of neutrophils.
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PMID:Stimulus-specific enhancement of luminol chemiluminescence in neutrophils by phosphatidylserine liposomes. 132 54

This study aimed to determine the kinetics of albumin resorption from and the healing of two types of albumin impregnated Vasculour II (Bard Cardiovascular) Dacron grafts (ACG-A and ACG-B) using whole blood preclotted Vasculour II Dacron grafts (without albumin) as controls (PCC). Prostheses measuring 4 mm ID x 50 mm length were implanted in the aortoiliac position in 24 dogs (ACG-A n = 12, ACG-B n = 24, PCC n = 12) and explanted after 1, 2 4, and 6 months. Platelet count, platelet aggregometry to 10(-5) M ADP, prothrombin time (PT), and partial thromboplastin time (PTT) were determined preoperatively and at explantation. Sections of the explanted grafts were assayed for human albumin by immunohistochemical techniques utilizing a rabbit polyclonal mono-specific antibody for human albumin followed by the addition of a biotinylated goat anti-rabbit IgG. Immunoperoxidase staining was then performed using Avidin D horse-radish peroxidase. Histology of the grafts (light microscopy, scanning electron microscopy, and transmission electron microscopy) as well as percent thrombus free surface area (TFSA) by computerized planimetry were also determined. Seven of 48 grafts were occluded (85.4% patency) with no difference among the three groups. Platelet aggregometry was not predictive of graft patency. No change in PT or PTT occurred nor was there any difference among the three groups. Retained albumin was detected in every one-month explant but not beyond that time, with the sensitivity for detecting human albumin in this assay being 20 mg albumin per gram of Dacron. All ACG explants at one month revealed inner capsular fibrin coagula not present in PCC specimens.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Albumin impregnated vascular grafts: albumin resorption and tissue reactions. 138 74

We studied the expression of catalase and myeloperoxidase genes in the hydrogen peroxide-resistant variants of human myeloid leukemia HL-60 cells HP50-2 and HP100-1. Southern blot hybridization with catalase and myeloperoxidase cDNA probes indicated that the copy number of the catalase gene in HP50-2 and HP100-1 cells was two and eight times, respectively, higher than that in HL-60 cells, whereas the copy number of the myeloperoxidase gene was the same. The amplified catalase and c-myc genes in HP100-1 cells were not decreased by treatment of the cells with inhibitors of poly(ADP-Ribose) polymerase, such as nicotinamide and benzamide. RNA blot hybridization with cDNA probes indicated that the content of catalase mRNA in HP50-2 and HP100-1 cells was four and 16 times higher, respectively, than that in HL-60 cells. By contrast, the content of myeloperoxidase mRNA in HP50-2 and HP100-1 cells was only a few percent of that in HL-60 cells. Furthermore, fluorescent in situ hybridization of a catalase cDNA probe to chromosomes indicated that the catalase gene in HP100-1 was amplified in the p13 region of a derivative chromosome 11. These results indicate that the increased synthesis of catalase in these resistant cells is mainly due to increased expression of the catalase gene, and that the lack of myeloperoxidase synthesis in these cells is due to the absence of its mRNA.
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PMID:Expression of catalase and myeloperoxidase genes in hydrogen peroxide-resistant HL-60 cells. 166 Feb 77

We administered iloprost, a stable prostacyclin mimetic, 27 nM, to isolated and perfused rabbit hearts submitted, after 60 min of equilibration, to an ischaemic period (60 min at a coronary flow of 1 ml/min) followed by a period of reperfusion (30 min at a coronary flow of 25 ml/min). Iloprost was delivered at different times during the experimental protocol: 60 min before ischaemia, at the onset and after 30 min of ischaemia and only during reperfusion. The iloprost cardioprotective effect was evaluated in terms of recovery of left ventricular pressure developed during reperfusion, creatine phosphokinase (CPK) and noradrenaline release, mitochondrial function (expressed as yield, RCI (respiratory control index), QO2, ADP/O), ATP and creatine phosphate (CP) tissue contents, calcium homeostasis and by measuring several parameters of oxidative stress: reduced and oxidized glutathione release and tissue contents, Mn and Cu-Zn superoxide dismutase activities; glutathione reductase and peroxidase activities. Our data show that the cytoprotective action of iloprost is closely related to the time of administration. Optimal myocardial preservation was achieved when it was given before or at the onset of ischaemia. Iloprost administration 30 min after the onset of ischaemia was still beneficial, although to a lesser extent. Iloprost lost its protective effect when given only on reperfusion. The data suggest that the iloprost cardioprotective effect is related to maintainance of membrane integrity.
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PMID:Role of timing of administration in the cardioprotective effect of iloprost, a stable prostacyclin mimetic. 172 98

In Japanese black cattle with large and long-existing hematomas, platelets was impaired in collagen aggregation function in vitro. There was no statistically significant difference from control animals in the tests of PT (prothrombin time) and PTT (partial thromboplastin time) for extrinsic and intrinsic blood coagulation system. Aside from impaired collagen aggregation function, platelets in the hematoma cattle showed the similar aggregation patterns as the normal cattle, when ADP, serotonin (5-HT), thrombin, arachidonic acid, epinephrine and ristocetin were used as agents for inducing aggregation. Decreased aggregation function as well as impaired collagen-induced release response in platelets suggested the hematoma cattle to be of storage pool disease (SPD). The impaired platelet was postulated to be a main cause of the large and long-existing hematomas. All of the hematoma cattle with impaired platelet functions had the eosinophils in peripheral blood of which granules were fewer and larger than normal ones. These large eosinophil granules were peroxidase positive and periodic acid Schiff (PAS) staining negative as typical eosinophil granules.
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PMID:Persistent hematomas in Japanese black cattle with impaired platelet aggregation function and large granule eosinophils. 183 Jul 60

We examined the effects of isoproterenol and carbachol on fluid-phase endocytosis by Chinese hamster ovary (CHO) cells transfected with beta-adrenergic, M1, or M3 cholinergic receptors. Isoproterenol increased cAMP production and carbachol increased intracellular Ca, indicating successful expression of the receptor genes and coupling to typical signal transduction pathways. Carbachol inhibited the uptake of horseradish peroxidase (HRP) or Lucifer yellow (markers of fluid-phase endocytosis) in both M1- and M3-containing cells but not in wild-type cells, whereas isoproterenol did not affect pinocytosis in cells transfected with beta-adrenergic receptors. Carbachol inhibited the transit of HRP from an exchangeable pool to a nonexchangeable pool by a latent process requiring minimally 5 min of incubation. During the latent period, only one peak of low-density HRP-containing vesicles was found on Percoll gradients; after 5 min, HRP appeared in both high- and low-density vesicles. Carbachol-treated cells contained less HRP in the high-density fraction enriched in lysosomal markers. Early endosomes from CHO cells labeled for 5 min with HRP underwent fusion to make a more dense population of vesicles in the presence of ATP and KCl at 37 degrees C but not at 4 degrees C. The fused material contained increased levels of G proteins as detected either by ADP ribosylation with appropriate toxins or by immunoblotting with specific antibodies. These findings suggest that GTP binding proteins are internalized in endocytic vesicles and enter into a complex trafficking process involving fusion with other vesicular compartments. Trafficking of endosomes to these compartments is inhibited by activated M1 and M3 muscarinic receptors in CHO cells.
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PMID:Carbachol-activated muscarinic (M1 and M3) receptors transfected into Chinese hamster ovary cells inhibit trafficking of endosomes. 190 73

Oxidants, generated by stimulated leukocytes, induce a variety of distinct biochemical changes in target cells. Hypochlorous acid (HOCl), produced by the action of peroxidase on hydrogen peroxide (H2O2) in the presence of chloride ions, acts at low molar concentrations (10-20 microM) to damage proteins on cell membranes and destroy their function. H2O2 rapidly permeates cells and causes inhibition of adenosine triphosphate (ATP) synthesis via both glycolytic and oxidative phosphorylation (mitochondrial) pathways. In the glycolytic pathway, damage is limited to the step involving glyceraldehyde-3-PO4 dehydrogenase (GAPDH). This results from both an attack of H2O2 on GAPDH and, indirectly, by a reduction in concentration of the GAPDH cofactor, nicotinamide adenine dinucleotide (NAD). This latter effect was found to result from activation of the enzyme, poly(adenosine diphosphate) (ADP)-ribose polymerase, an enzyme involved in deoxyribonucleic acid (DNA) repair. DNA damage in target cells was found at low concentrations of H2O2 (20-80 microM) in many cell types. Strand breaks and base hydroxylation were observed, resulting in the generation of hydroxyl radicals (.OH) from H2O2, in the presence of a transition metal. DNA damage resulted in either cell injury and death or mutations of the base sequence and amino acid residues. These latter effects led to malignant transformations in cultured cells in both tissue cultures of the cells, and in vivo in athymic mice. Exposure of a proto-oncogene, K-ras 4B, also led to the development of a malignant transformation by virtue of mutations in codon positions 12 and 61. Thus, oxidant effects on target cells can damage multiple functional pathways inside the cells, as well as give rise to malignant transformation via DNA damage.
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PMID:Cellular injury by oxidants. 192 8

H2O2, in addition to producing highly reactive molecules through hydroxyl radicals or peroxidase action, can exert a number of direct effects on cells, organelles and enzymes. The stimulations include glucose transport, glucose incorporation into glycogen, HMP shunt pathway, lipid synthesis, release of calcium from mitochondria and of arachidonate from phospholipids, poly ADP ribosylation, and insulin receptor tyrosine kinase and pyruvate dehydrogenase activities. The inactivations include glycolysis, lipolysis, reacylation of lysophospholipids, ATP synthesis, superoxide dismutase and protein kinase C. Damages to DNA and proteoglycan and general cytotoxicity possibly through oxygen radicals were also observed. A whole new range of effects will be opened by the finding that H2O2 can act as a signal transducer in oxidative stress by oxidizing a dithiol protein to disulphide form which then activates transcription of the stress inducible genes. Many of these direct effects seem to be obtained by dithiol-disulphide modification of proteins and their active sites, as part of adaptive responses in oxidative stress.
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PMID:H2O2 has a role in cellular regulation. 207 30

We studied the effects of various 111In-water soluble chelates and incubation media on labeling efficiency of platelets and in vitro platelet aggregability. High labeling efficiency of platelets in ACD-saline was achieved with 111In-oxine sulfate, 111In-tropolone and 111In-MPO (2-mercaptopyridine-N-oxide). In the condition with 4.8 x 10(6)/mm3 platelets in ACD-plasma, 111In-oxine-sulfate had low labeling efficiency and inconsistent labeling, while 111In-tropolone and 111In-MPO had high labeling efficiency. In vitro platelet aggregability (ADP 2 microM) was reduced when platelets were labeled in the absence of plasma. However, there was no significant difference in platelet aggregability among 111In-platelets labeled by three different chelates. In conclusion, to maintain aggregation activity of the platelets with relatively high labeling efficiency, the best result was obtained by using MPO or tropolone chelate in plasma at 4.8 x 10(6)/microliters platelet concentration.
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PMID:[Functional alterations of human platelets following 111In labeling with different ligands and incubation media]. 211 76


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