JPOST Repositoryapplication/xmlhttps://storage.jpostdb.org/JPST003883/files/230512_yagiRatF2_4_001.rawhttps://storage.jpostdb.org/JPST003883/files/230512_yagiRatF1_5_001.rawhttps://storage.jpostdb.org/JPST003883/files/230512_yagiRatF1_2_002.rawhttps://storage.jpostdb.org/JPST003883/files/230512_yagiRatF2_1_002.rawhttps://storage.jpostdb.org/JPST003883/files/230511_yagiRatF1_1_002.rawhttps://storage.jpostdb.org/JPST003883/files/230512_yagiRatF2_2_002.rawhttps://storage.jpostdb.org/JPST003883/files/230512_yagiRatF1_3_002.rawhttps://storage.jpostdb.org/JPST003883/files/230512_yagiRatF2_3_002.rawhttps://storage.jpostdb.org/JPST003883/files/230512_yagiRatF1_4_002.rawhttps://storage.jpostdb.org/JPST003883/files/230511_yagiRatM1_3_002.rawhttps://storage.jpostdb.org/JPST003883/files/230512_yagiRatF2_4_002.rawhttps://storage.jpostdb.org/JPST003883/files/230512_yagiRatF1_5_002.rawhttps://storage.jpostdb.org/JPST003883/files/230511_yagiRatF1_1_001.rawhttps://storage.jpostdb.org/JPST003883/files/230512_yagiRatF2_2_001.rawhttps://storage.jpostdb.org/JPST003883/files/230512_yagiRatF1_3_001.rawhttps://storage.jpostdb.org/JPST003883/files/230511_yagiRatM1_3_001.rawhttps://storage.jpostdb.org/JPST003883/files/230512_yagiRatF2_1_001.rawhttps://storage.jpostdb.org/JPST003883/files/230512_yagiRatF1_2_001.rawhttps://storage.jpostdb.org/JPST003883/files/230512_yagiRatF2_3_001.rawhttps://storage.jpostdb.org/JPST003883/files/230512_yagiRatF1_4_001.rawprimaryOK200ProteomicsHirokazu YagiCellular Organismshttps://repository.jpostdb.org/entry/JPST003883Nagoya City UniversityjPOSTWe conducted systematic glycomic and glycoproteomic profiling to characterize the dynamic <i>N</i>-glycosylation landscape of rat serum, with particular focus on sex- and time-dependent variations. MALDI-TOF-MS analysis revealed that rat serum <i>N</i>-glycans are predominantly biantennary, disialylated complex-type structures with extensive <i>O</i>-acetylation of Neu5Ac residues, especially in females. LC-MS/MS-based glycoproteomic analysis of albumin/IgG-depleted serum identified 87 glycoproteins enriched in protease inhibitors (e.g., serine protease inhibitor A3K) and immune-related proteins such as complement C3. Temporal analyses revealed stable sialylation in males but pronounced daily fluctuations in females, suggesting hormonal influence. Neu5Gc-containing glycans were rare and mainly derived from residual IgG, as confirmed by glycomic analysis. In contrast to liver-derived glycoproteins, purified IgG exhibited Neu5Gc-only sialylation without <i>O</i>-acetylation, underscoring distinct sialylation profiles characteristic of B cell-derived glycoproteins. Region-specific glycosylation patterns were observed in IgG, with the Fab region carrying more disialylated structures than Fc. These findings highlight cell-type and sex-specific differences in sialylation patterns between hepatic and immune tissues, with implications for hormonal regulation and biomarker research. This study provides a valuable dataset on rat serum glycoproteins and underscores the distinctive glycosylation features of rats, reinforcing their utility as model organisms in glycobiology and disease research.Temporal and Sex-Dependent <i>N</i>-Glycosylation Dynamics in Rat Serum.Yagi Hirokazu H, Kondo Sachiko S, Murakami Reiko R, Yogo Rina R, Yanaka Saeko S, Umezawa Fumiko F, Yagi-Utsumi Maho M, Fujita Akihiro A, Okina Masako M, Hashimoto Yutaka Y, Hotta Yuji Y, Kato Yoichi Y, Nakajima Kazuki K, Furukawa Jun-Ichi JI, Kato Koichi KfalseGlycoprpteomics for Albumin & IgG depletedGlycoprpteomics for Albumin & IgG depleted rat serumMon Oct 20 00:00:00 BST 2025PXD06520913156740806398