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N-Glycosylation at Asn695 might suppress inducible nitric oxide synthase activity by disturbing electron transfer

Acta Biochim Biophys Sin (Shanghai). 2020-11; 
Jianghong Yan, Fei-Fei Shang, An He, Shupeng Hu, Suxin Luo, Yong Xia
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Recombinant Proteins … For the experiment, cells were seeded at 5 × 10 5 cells/well in 6-well plates. At 36 h, 500 ng/ml LPS (Sigma, St Louis, USA) and 5 ng/ml IFN-γ (GenScript, Nanjing, China) were added into the induction group, and the same volume of PBS was added to the control group?… Get A Quote

摘要

Inducible nitric oxide synthase (iNOS) plays critical roles in the inflammatory response and host defense. Previous research on iNOS regulation mainly focused on its gene expression level, and much less is known about the regulation of iNOS function by N-glycosylation. In this study, we report for the first time that iNOS is N-glycosylated in vitro and in vivo. Mass spectrometry studies identified Asn695 as an N-glycosylation site of murine iNOS. Mutating Asn695 to Gln695 yields an iNOS that exhibits greater enzyme activity. The essence of nitric oxide synthase catalytic reaction is electron transfer process, which involves a series of conformational changes, and the linker between the flavin mononucleotide-bin... More

關鍵詞

N-glycosylation, electron transfer, iNOS, nitric oxide synthase, posttranslational modification
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