کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1928173 | 1536772 | 2015 | 8 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: New insights into the posttranslational regulation of human cytosolic thioredoxin by S-palmitoylation New insights into the posttranslational regulation of human cytosolic thioredoxin by S-palmitoylation](/preview/png/1928173.png)
• S-palmitoylation occurs at Cys73 of Trx1 in living endothelial cells.
• Insulin signaling may regulate level of S-palmitoylated Trx1 in the cells.
• S-palmitoylation plays significant effects on Trx1 structure and functions.
High level of palmitate is associated with metabolic disorders. We recently showed that enhanced level of S-palmitoylated cytosolic thioredoxin (Trx1) in mouse liver was new characteristic feature of insulin resistance. However, our understanding of the effect of S-palmitoylation on Trx1 is limited, and the tissue specificity of Trx1 S-palmitoylation is unclear. Here we show that S-palmitoylation also occurs at Cys73 of Trx1 in living endothelial cells, and the level of S-palmitoylated Trx1 undergoes regulation by insulin signaling. Trx1 prefers thiol-thioester exchange with palmitoyl-CoA to acetyl-CoA. S-palmitoylation alters conformation or secondary structure of Trx1, as well as decreases the ability of Trx1 to transfer electrons from thioredoxin reductase to S-nitrosylated protein–tyrosine phosphatase 1B and S-nitroso-glutathione. Our results demonstrate that S-palmitoylation is an important post-translational modification of human Trx1.
Journal: Biochemical and Biophysical Research Communications - Volume 460, Issue 4, 15 May 2015, Pages 949–956