N‐Glycosylation is essential for the secretion of extracellular superoxide dismutase. Issue 19 (15th September 2016)

• Record Type: Journal Article
• Authors: Ota, Fumi; Kizuka, Yasuhiko; Kitazume, Shinobu; Adachi, Tetsuo; Taniguchi, Naoyuki
• Is Part Of: FEBS letters. Volume 590:Issue 19(2016)
• Page Start: 3357
• Page End: 3367
• Publication Date: 2016-09-15
• Subjects: extracellular superoxide dismutase -- glycan -- secretion; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12378
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Extracellular superoxide dismutase (EC‐SOD or SOD3) protects against various oxidative stress‐related diseases by scavenging reactive superoxides in the extracellular space. It is the only SOD isozyme that is secreted and glycosylated (at asparagine 89). However, the physiological roles of its glycosylation are poorly understood. In this study, we found that the glycosylation site on EC‐SOD is well conserved and that a glycosylation‐deficient EC‐SOD mutant retains its enzymatic activity, but is not secreted. This impairment in secretion may, in part, be due to the ability of the mutants to form unusual higher order oligomers. Our findings reveal that the glycan modification is a key regulator of EC‐SOD secretion and contributes to the understanding of the roles of glycans in EC‐SOD‐related diseases. Abstract :