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N ‐Glycosylation is essential for the secretion of extracellular superoxide dismutase
Author(s) -
Ota Fumi,
Kizuka Yasuhiko,
Kitazume Shinobu,
Adachi Tetsuo,
Taniguchi Naoyuki
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12378
Subject(s) - glycosylation , superoxide dismutase , secretion , extracellular , glycan , biochemistry , chemistry , superoxide , reactive oxygen species , dismutase , glycoprotein , enzyme , asparagine , n linked glycosylation , microbiology and biotechnology , biology
Extracellular superoxide dismutase ( EC ‐ SOD or SOD 3) 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.