scholarly journals Defining cutaneous molecular pathobiology of arsenicals using phenylarsine oxide as a prototype

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Ritesh K. Srivastava ◽  
Changzhao Li ◽  
Zhiping Weng ◽  
Anupam Agarwal ◽  
Craig A. Elmets ◽  
...  
Keyword(s):  
Phenylarsine Oxide

Phenylarsine oxide inhibits ex vivo HIV-1 expression

1997 ◽  
Vol 51 (10) ◽  
pp. 430-438 ◽  
Author(s):  
S Arbault ◽  
M Edeas ◽  
S Legrand-Poels ◽  
N Sojic ◽  
C Amatore ◽  
...  
Keyword(s):  
Ex Vivo ◽  
Phenylarsine Oxide ◽  
Hiv 1

Phenylarsine Oxide Increases Intracellular Calcium Mobility and Inhibits Ca2+-Dependent ATPase Activity in Thymocytes

1999 ◽  
Vol 68 (3) ◽  
pp. 363-370 ◽  
Author(s):  
A. Hmadcha ◽  
M. Carballo ◽  
M. Conde ◽  
G. Márquez ◽  
J. Monteseirı́n ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Intracellular Calcium ◽  
Phenylarsine Oxide ◽  
Dependent Atpase

Evidence that tyrosine phosphorylation may increase tight junction permeability

1995 ◽  
Vol 108 (2) ◽  
pp. 609-619 ◽  
Author(s):  
J.M. Staddon ◽  
K. Herrenknecht ◽  
C. Smales ◽  
L.L. Rubin
Keyword(s):  
Endothelial Cells ◽  
Tight Junction ◽  
Tyrosine Phosphorylation ◽  
Mdck Cells ◽  
Tyrosine Phosphatase ◽  
Adherens Junction ◽  
Brain Endothelial Cells ◽  
Phenylarsine Oxide ◽  
Phosphatase Inhibitor ◽  
Tight Junction Permeability

Tight junction permeability control is important in a variety of physiological and pathological processes. We have investigated the role of tyrosine phosphorylation in the regulation of tight junction permeability. MDCK epithelial cells and brain endothelial cells were grown on filters and tight junction permeability was determined by transcellular electrical resistance (TER). The tyrosine phosphatase inhibitor pervanadate caused a concentration- and time-dependent decrease in TER in both MDCK and brain endothelial cells. However, as expected, pervanadate resulted in the tyrosine phosphorylation of many proteins; hence interpretation of its effects are extremely difficult. Phenylarsine oxide, a more selective tyrosine phosphatase inhibitor, caused the tyrosine phosphorylation of relatively few proteins as analyzed by immunoblotting of whole cell lysates. This inhibitor, like pervanadate, also elicited a decrease in TER in the two cell types. In the MDCK cells, the action of phenylarsine oxide could be reversed by the subsequent addition of the reducing agent 2,3-dimercaptopropanol. Immunocytochemistry revealed that phenylarsine oxide rapidly stimulated the tyrosine phosphorylation of proteins associated with intercellular junctions. Because of the known influence of the adherens junction on tight junctions, we analyzed immunoprecipitates of the E-cadherin/catenin complex from MDCK cells treated with phenylarsine oxide. This revealed an increase in the tyrosine phosphorylation of beta-catenin, but not of alpha-catenin. However, the tight junction associated protein ZO-1 was also tyrosine phosphorylated after PAO treatment. These data indicate that tight junction permeability may be regulated via mechanisms involving tyrosine phosphorylation of adherens junction and tight junction proteins.

Activation of potassium-dependent H+ efflux from mitochondria by cadmium and phenylarsine oxide

1981 ◽  
Vol 13 (5-6) ◽  
pp. 425-431 ◽  
Author(s):  
D. Rao Sanadi ◽  
James B. Hughes ◽  
Saroj Joshi
Keyword(s):  
Phenylarsine Oxide

scholarly journals Regulation of the thyroid NADPH-dependent H2O2 generator by Ca2+: studies with phenylarsine oxide in thyroid plasma membrane

1997 ◽  
Vol 321 (2) ◽  
pp. 383-388 ◽  
Author(s):  
Yves GORIN ◽  
Anne Marie LESENEY ◽  
Renée OHAYON ◽  
Corinne DUPUY ◽  
Jacques POMMIER ◽  
...  
Keyword(s):  
Nadph Oxidase ◽  
Plasma Membranes ◽  
Direct Action ◽  
Native Enzyme ◽  
Thiol Groups ◽  
Phenylarsine Oxide ◽  
Oxidoreductase Activity ◽  
H2o2 Formation ◽  
Partial Inactivation ◽  
Dose Dependent

Pig thyroid plasma membranes contain a Ca2+-dependent NADPH:O2 oxidoreductase, the thyroid NADPH-dependent H2O2 generator. This provided the H2O2 for the peroxidase-catalysed synthesis of thyroid hormones. The effect of the tervalent arsenical, phenylarsine oxide (PAO), on the NADPH oxidase was studied. PAO caused two directly related dose-dependent effects with similar half-effect concentrations of PAO (3 nmol of PAO/mg of protein): (i) partial inactivation of H2O2 formation by the Ca2+-stimulated enzyme, and (ii) desensitization of the enzyme activity to Ca2+. PAO had no effect on membranes that had been Ca2+-desensitized by α-chymotrypsin treatment. The NADPH oxidase in membranes treated with excess PAO had the same Vmax with and without Ca2+. This value was half the Vmax of the native enzyme. However, the Km for NADPH determined with Ca2+ (18 ƁM, identical with that of the native enzyme) was approx. one-third of the Km measured without Ca2+, showing the direct action of Ca2+ on the PAOŐenzyme complex. PAO had the same effects, partial inactivation and Ca2+ desensitization, on the NADPH:ferricyanide oxidoreductase activity of the NADPH oxidase, suggesting that PAO acts on the flavodehydrogenase entity of the enzyme. Both partial inactivation and Ca2+ desensitization were completely and specifically reversed by 2,3-dimercaptopropanol, partly reversed by dithiothreitol and not reversed by 2-mercaptoethanol, indicating that PAO binds to vicinal thiol groups. These results suggest that thiol groups are involved in the control of thyroid NADPH oxidase by Ca2+; PAO bound to vicinal thiols might alter the structure of the enzyme so that electron transfer occurs without Ca2+ but more slowly.

scholarly journals Shifting the Specificity of E. coli Biosensor from Inorganic Arsenic to Phenylarsine Oxide through Genetic Engineering

Sensors ◽  
2020 ◽  
Vol 20 (11) ◽  
pp. 3093
Author(s):  
Hyojin Kim ◽  
Yangwon Jeon ◽  
Woonwoo Lee ◽  
Geupil Jang ◽  
Youngdae Yoon
Keyword(s):  
Genetic Engineering ◽  
Inorganic Arsenic ◽  
Arsenic Species ◽  
Coli Cell ◽  
Biological Processes ◽  
Phenylarsine Oxide ◽  
Covalent Bonds ◽  
E Coli ◽  
Organic Arsenic ◽  
The Moment

It has recently been discovered that organic and inorganic arsenics could be detrimental to human health. Although organic arsenic is less toxic than inorganic arsenic, it could form inorganic arsenic through chemical and biological processes in environmental systems. In this regard, the availability of tools for detecting organic arsenic species would be beneficial. Because As-sensing biosensors employing arsenic responsive genetic systems are regulated by ArsR which detects arsenics, the target selectivity of biosensors could be obtained by modulating the selectivity of ArsR. In this study, we demonstrated a shift in the specificity of E. coli cell-based biosensors from the detection of inorganic arsenic to that of organic arsenic, specifically phenylarsine oxide (PAO), through the genetic engineering of ArsR. By modulating the number and location of cysteines forming coordinate covalent bonds with arsenic species, an E. coli cell-based biosensor that was specific to PAO was obtained. Despite its restriction to PAO at the moment, it offers invaluable evidence of the potential to generate new biosensors for sensing organic arsenic species through the genetic engineering of ArsR.

scholarly journals Trafficking of glucose transporters in 3T3-L1 cells. Inhibition of trafficking by phenylarsine oxide implicates a slow dissociation of transporters from trafficking proteins

1992 ◽  
Vol 281 (3) ◽  
pp. 809-817 ◽  
Author(s):  
J Yang ◽  
A E Clark ◽  
R Harrison ◽  
I J Kozka ◽  
G D Holman
Keyword(s):  
Cell Surface ◽  
Glucose Transport ◽  
Glucose Transporter ◽  
Fluid Phase ◽  
Transport Activity ◽  
Phenylarsine Oxide ◽  
Fluid Phase Endocytosis ◽  
Surface Labelling ◽  
Slow Dissociation ◽  
Stimulation Of

We have compared the rates of insulin stimulation of cell-surface availability of glucose-transporter isoforms (GLUT1 and GLUT4) and the stimulation of 2-deoxy-D-glucose transport in 3T3-L1 cells. The levels of cell-surface transporters have been assessed by using the bismannose compound 2-N-[4-(1-azi-2,2,2-trifluoroethyl)benzoyl]-1,3-bis(D-mannos -4-yloxy) propyl-2-amine (ATB-BMPA). At 27 degrees C the half-times for the appearance of GLUT1 and GLUT4 at the cell surface were 5.7 and 5.4 min respectively and were slightly shorter than that for the observed stimulation of transport activity (t 1/2 8.6 min). This lag may be due to a slow dissociation of surface transporters from trafficking proteins responsible for translocation. When fully-insulin-stimulated cells were subjected to a low-pH washing procedure to remove insulin at 37 degrees C, the cell-surface levels of GLUT1 and GLUT4 decreased, with half-times of 9.2 and 6.8 min respectively. These times correlated well with decrease in 2-deoxy-D-glucose transport activity that occurred during this washing procedure (t1/2 6.5 min). When fully-insulin-stimulated cells were treated with phenylarsine oxide (PAO), a similar decrease in transport activity occurred (t1/2 9.8 min). However, surface labelling showed that this corresponded with a decrease in GLUT4 only (t1/2 7.8 min). The cell-surface level of GLUT1 remained high throughout the PAO treatment. Light-microsome membranes were isolated from cells which had been cell-surface-labelled with ATB-BMPA. Internalization of both transporter isoforms to this pool occurred when cells were maintained in the presence of insulin for 60 min. In contrast with the surface-labelling results, we have shown that the transfer to the light-microsome pool of both transporters occurred in cells treated with insulin and PAO. These results suggest that both transporters are recycled by fluid-phase endocytosis and exocytosis. PAO may inhibit this recycling at a stage which involves the re-emergence of internalized transporters at the plasma membrane. The GLUT1 transporters that are recycled to the surface in insulin- and PAO-treated cells appear to have low transport activity. This may be because of a failure to dissociate fully from trafficking proteins at the cell surface. GLUT4 transporters appear to have a greater tendency to remain internalized if the normal mechanisms that commit transporters to the cell surface, such as dissociation from trafficking proteins, are uncoupled.

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