The effect of streptozotocin-induced hyperglycemia on N-and O-linked protein glycosylation in mouse ovary
2018
Post-translational modification of proteins namely glycosylation influences cellular behavior,
structural properties and interactions including during ovarian follicle development and atresia.
However, little is known about protein glycosylation changes occurring in diabetes mellitus in
ovarian tissues despite the well-known influence of diabetes on the outcome of successful embryo
implantation. In our study, the use of PGC chromatography–ESI mass spectrometry in negative
ion mode enabled the identification of 138 N-glycans and 6 O-glycans on the proteins of
Streptozotocin-induced (STZ) diabetic mouse ovarian tissues (n = 3). Diabetic mouse ovaries
exhibited a relative decrease in sialylation, fucosylation and, to a lesser extent, branched N-linked
glycan structures, as well as an increase in oligomannose structures on their proteins, compared
with nondiabetic mouse ovaries. Changes in N-glycans occurred in the diabetic liver tissue but
were more evident in diabetic ovarian tissue of the same mouse, suggesting an organ-specific
effect of diabetes mellitus on protein glycosylation. Although at a very low amount, O-GalNAc glycans of mice ovaries were present as core type 1 and core type 2 glycans; with a relative increase
in the NeuGc:NeuAc ratio as the most significant difference between control and diabetic ovarian
tissues. STZ-treated mice also showed a trend towards an increase in TNF-α and IL1-B inflammatory cytokines, which have previously been shown to influence protein glycosylation.
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