vicinal dithiols
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2020 ◽  
Vol 92 (6) ◽  
pp. 4371-4378 ◽  
Author(s):  
Guodong Hu ◽  
Huiyi Jia ◽  
Yanan Hou ◽  
Xiao Han ◽  
Lu Gan ◽  
...  

Biomolecules ◽  
2020 ◽  
Vol 10 (2) ◽  
pp. 235 ◽  
Author(s):  
Valeria M. Nurchi ◽  
Aleksandra Buha Djordjevic ◽  
Guido Crisponi ◽  
Jan Alexander ◽  
Geir Bjørklund ◽  
...  

High arsenic (As) levels in food and drinking water, or under some occupational conditions, can precipitate chronic toxicity and in some cases cancer. Millions of people are exposed to unacceptable amounts of As through drinking water and food. Highly exposed individuals may develop acute, subacute, or chronic signs of poisoning, characterized by skin lesions, cardiovascular symptoms, and in some cases, multi-organ failure. Inorganic arsenite(III) and organic arsenicals with the general formula R-As2+ are bound tightly to thiol groups, particularly to vicinal dithiols such as dihydrolipoic acid (DHLA), which together with some seleno-enzymes constitute vulnerable targets for the toxic action of As. In addition, R-As2+-compounds have even higher affinity to selenol groups, e.g., in thioredoxin reductase that also possesses a thiol group vicinal to the selenol. Inhibition of this and other ROS scavenging seleno-enzymes explain the oxidative stress associated with arsenic poisoning. The development of chelating agents, such as the dithiols BAL (dimercaptopropanol), DMPS (dimercapto-propanesulfonate) and DMSA (dimercaptosuccinic acid), took advantage of the fact that As had high affinity towards vicinal dithiols. Primary prevention by reducing exposure of the millions of people exposed to unacceptable As levels should be the prioritized strategy. However, in acute and subacute and even some cases with chronic As poisonings chelation treatment with therapeutic dithiols, in particular DMPS appears promising as regards alleviation of symptoms. In acute cases, initial treatment with BAL combined with DMPS should be considered.


2019 ◽  
Vol 30 (10) ◽  
pp. 1704-1716 ◽  
Author(s):  
Guodong Hu ◽  
Huiyi Jia ◽  
Lanning Zhao ◽  
Dong-Hyung Cho ◽  
Jianguo Fang

2014 ◽  
Vol 136 (40) ◽  
pp. 14237-14244 ◽  
Author(s):  
Chusen Huang ◽  
Ti Jia ◽  
Mengfang Tang ◽  
Qin Yin ◽  
Weiping Zhu ◽  
...  

2010 ◽  
Vol 504 (2) ◽  
pp. 228-235 ◽  
Author(s):  
Raquel Requejo ◽  
Edward T. Chouchani ◽  
Andrew M. James ◽  
Tracy A. Prime ◽  
Kathryn S. Lilley ◽  
...  

2007 ◽  
Vol 77 (4) ◽  
pp. 604-606
Author(s):  
M. G. Voronkov ◽  
S. G. D’yachkova ◽  
I. P. Lebedeva ◽  
A. V. Evart ◽  
L. G. Shagun
Keyword(s):  

1996 ◽  
Vol 271 (11) ◽  
pp. 6283-6291 ◽  
Author(s):  
Ramila S. Patel-King ◽  
Sharon E. Benashski ◽  
Alistair Harrison ◽  
Stephen M. King
Keyword(s):  

Blood ◽  
1995 ◽  
Vol 85 (9) ◽  
pp. 2559-2569 ◽  
Author(s):  
H Kutsumi ◽  
K Kawai ◽  
RB Jr Johnston ◽  
K Rokutan

Phenylarsine oxide (PAO) specifically forms a stable ring complex with vicinal dithiols that can be reversed with 2,3-dimercaptopropanol (DMP). Pretreatment of human neutrophils with micromolar concentrations of PAO inhibited release of superoxide anion (O2-) stimulated by N- formyl-methionyl-leucyl-phenylalanine (FMLP) or phorbol 12-myristate 13-acetate (PMA); the inhibition was reversed with DMP, but not with 2-mercaptoethanol. PAO did not affect O2-release in previously stimulated cells. PAO did not affect the FMLP-induced Ca2+ response, suggesting that PAO affects a postreceptor event that does not modulate the Ca2+ transient. Treatment of isolated membrane or cytosolic fractions with PAO did not change the rates of arachidonate-stimulated O2-production in a cell-free system. Pretreatment of unstimulated neutrophils with PAO inactivated cytosolic protein kinase C (PKC); the inactivation was reversed with DMP. However, PAO did not affect PMA-induced translocation of beta-PKC protein or reduce the PKC activity translocated to the membrane. PAO had no effect on tyrosine kinase activity but inactivated phosphotyrosine phosphatase; stimulus-induced tyrosine phosphorylation of several proteins was markedly enhanced. These results suggest that vicinal dithiols play an essential role in activation of the respiratory burst oxidase. Possible sites for the activity of these essential vicinal dithiols include PKC and the regulatory balance of tyrosine phosphatase activity and tyrosine phosphorylation.


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