Premium
Swainsonine affects the processing of glycoproteins in vivo
Author(s) -
Abraham David J.,
Sidebothom Ramon,
Winchester Bryan G.,
Dorling Peter R.,
Dell Anne
Publication year - 1983
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 - 10.1016/0014-5793(83)81174-0
Subject(s) - swainsonine , glycoprotein , glycan , oligosaccharide , golgi apparatus , mannosidase , in vivo , biochemistry , guinea pig , asparagine , chemistry , mannose , mucoproteins , biology , enzyme , endoplasmic reticulum , endocrinology , microbiology and biotechnology
Rats, sheep and guinea pigs treated with swainsonine excrete ‘high mannose’ oligosaccharides in urine. The major rat and guinea pig oligosaccharide is (Man) 5 GlcNAc whereas sheep excrete a mixture of oligosaccharides of composition (Man) 2–5 GlcNAc 2 and (Man) 3–5 GlcNAc. The presence of these oligosaccharides suggests that Golgi α‐D‐mannosidase II as well as lysosomal α‐D‐mannosidase is inhibited by swainsonine resulting in storage of abnormally processed asparagine‐linked glycans from glycoproteins. Altered glycoprotein processing appears to have little effect on the health of the intoxicated animal, but the accompanying lysosomal storage produces a disease state.