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10.1016/j.bbrep.2015.11.012 http://scihub22266oqcxt.onion/10.1016/j.bbrep.2015.11.012 C5600461!5600461!28955804     free     free     free       Biochem+Biophys+Rep 2016 ; 5 (ä): 27-34 Nephropedia Template TP {{tp|p=28955804|t=2016. Thioredoxin 1 regulation of protein S-desulfhydration |pdf=|usr=}}{{28955804}} gab.com Text Thioredoxin 1 regulation of protein S-desulfhydration JO: Biochem Biophys Rep http://www.kidney.de/pget.php?&tw=1&pmid=28955804 #FOAvip The importance of H2S in biology and medicine has been widely recognized in recent years, and protein S-sulfhydration is proposed to mediate the direct actions of H2S bioactivity in the body. Thioredoxin 1 (Trx1) is an important reducing enzyme that cleaves disulfides in proteins and acts as an S-denitrosylase. The regulation of Trx1 on protein S-sulfhydration is unclear. Here we showed that Trx1 facilitates protein S-desulfhydration. Overexpression of Trx1 attenuated the basal level and H2S-induced protein S-sulfhydration by direct interaction with S-sulfhydrated proteins, i.e., glyceraldehyde 3-phosphate dehydrogenase and pyruvate carboxylase. In contrast, knockdown of Trx1 mRNA expression by short interfering RNA or blockage of Trx1 redox activity with PX12 or 2,4-dinitrochlorobenzene enhanced protein S-sulfhydration. Mutation of cysteine-32 but not cysteine-35 in the Trp?Cys32?Gly?Pro?Cys35 motif eliminated the binding of Trx1 with S-sulfhydrated proteins and abolished the S-desulfhydrating effect of Trx1. All these data suggest that Trx1 acts as an S-desulfhydrase. Twit Text FOAVip Thioredoxin 1 regulation of protein S-desulfhydration ????Biochem Biophys Rep http://www.kidney.de/pget.php?&tw=1&pmid=28955804 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28955804 #FOAvip English Wikipedia <ref>{{Cite pmid|28955804}}</ref> Thioredoxin 1 regulation of protein S-desulfhydration #MMPMID28955804 Ju Y; Wu L; Yang G Biochem Biophys Rep 2016[Mar]; 5 (ä): 27-34 PMID28955804show ga The importance of H2S in biology and medicine has been widely recognized in recent years, and protein S-sulfhydration is proposed to mediate the direct actions of H2S bioactivity in the body. Thioredoxin 1 (Trx1) is an important reducing enzyme that cleaves disulfides in proteins and acts as an S-denitrosylase. The regulation of Trx1 on protein S-sulfhydration is unclear. Here we showed that Trx1 facilitates protein S-desulfhydration. Overexpression of Trx1 attenuated the basal level and H2S-induced protein S-sulfhydration by direct interaction with S-sulfhydrated proteins, i.e., glyceraldehyde 3-phosphate dehydrogenase and pyruvate carboxylase. In contrast, knockdown of Trx1 mRNA expression by short interfering RNA or blockage of Trx1 redox activity with PX12 or 2,4-dinitrochlorobenzene enhanced protein S-sulfhydration. Mutation of cysteine-32 but not cysteine-35 in the Trp?Cys32?Gly?Pro?Cys35 motif eliminated the binding of Trx1 with S-sulfhydrated proteins and abolished the S-desulfhydrating effect of Trx1. All these data suggest that Trx1 acts as an S-desulfhydrase. äThioredoxin 1 regulation of protein S-desulfhydration (epmc).pdf DeepDyve Pubget Overpricing