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10.1039/c6mb00175k

http://scihub22266oqcxt.onion/10.1039/c6mb00175k
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C4955733!4955733!27216279
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suck abstract from ncbi


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pmid27216279      Mol+Biosyst 2016 ; 12 (8): 2471-80
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  • Clickable Glutathione Approach for Identification of Protein Glutathionylation in Response to Glucose Metabolism? #MMPMID27216279
  • Samarasinghe KTG; Munkanatta Godage DNP; Zhou Y; Ndombera FT; Weerapana E; Ahn YH
  • Mol Biosyst 2016[Jul]; 12 (8): 2471-80 PMID27216279show ga
  • Glucose metabolism and mitochondrial function are closely interconnected with cellular redox-homeostasis. Although glucose starvation, which mimics ischemic condition or insufficient vascularization, is known to perturb redox-homeostasis, global and individual protein glutathionylation in response to glucose metabolism or mitochondrial activity remains largely unknown. In this report, we use our clickable glutathione approach, which form clickable glutathione (azido-glutathione) by using a mutant of glutathione synthetase (GS M4), for detection and identification of protein glutathionylation in response to glucose starvation. We found that protein glutathionylation is readily induced in HEK293 cells in response to low glucose concentrations when mitochondrial reactive oxygen species (ROS) are elevated in cells, and glucose is the major determinant for inducing reversible glutathionylation. Proteomic and biochemical analysis identified over 1,300 proteins, including SMYD2, PP2C?, and catalase. We further showed that PP2C? is glutathionylated at C314 in a C-terminal domain, and PP2C? C314 glutathionylation disrupts the interaction with mGluR3, an important glutamate receptor associated with synaptic plasticity
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