A comprehensive glycome profiling of Huntington's disease transgenic mice

Gizaw, Solomon Tebeje; Koda, Toshiaki; Amano, Maho; Kamimura, Keiko; Ohashi, Tetsu; Hinou, Hiroshi; Nishimura, Shin‐Ichiro

doi:10.1016/j.bbagen.2015.04.006

Cited by 50 publications

(50 citation statements)

References 72 publications

(100 reference statements)

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“…The GSL‐glycan profile of mouse serum was completely different from that of human, although the serum levels of total GSL‐glycans were almost the same (11.6 ± 4.7 μM in human serum and 11.8 ± 2.1 μM in mouse serum). In mouse serum, 92.8% of the serum GSL‐glycans were GM2 (Hex 2 HexNAc 1 Neu5Gc 1 (GSL‐10)), which agrees well with previous observations . Other components detected in mouse serum include Lc3/asialo‐GM2 (Hex 2 HexNAc 1 , (GSL‐3)), GM3 (Hex 2 Neu5Gc 1 (GSL‐6)), and GSL‐7.…”

Section: Resultssupporting

confidence: 90%

“…The serum level of total O‐glycans in mice (C57BL/6J) was estimated to be 33.7 ± 8.24 μM, which is more than 100 times higher than the value recently reported for B6CBAF1 mice (0.32 μM), where O‐glycans were released from glycoproteins by ammonium carbamate . To evaluate this inconsistency, the serum O‐glycome of C57BL/6J mice was analyzed by the method reported in . We found that the amount of O‐glycans released by ammonium carbamate was approximately 100 times lower than that by microwave‐assisted BEP (data not shown).…”

Section: Resultsmentioning

confidence: 71%

“…In this study, we estimated the level of total O‐glycans in human serum to be 71.6 ± 8.31 μM, which is in good agreement with a previously reported value , where O‐glycans were recovered by reductive β‐elimination. The serum level of total O‐glycans in mice (C57BL/6J) was estimated to be 33.7 ± 8.24 μM, which is more than 100 times higher than the value recently reported for B6CBAF1 mice (0.32 μM), where O‐glycans were released from glycoproteins by ammonium carbamate . To evaluate this inconsistency, the serum O‐glycome of C57BL/6J mice was analyzed by the method reported in .…”

Section: Resultsmentioning

confidence: 88%

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Quantitative analysis of total serum glycome in human and mouse

et al. 2016

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Model mice are frequently used in drug discovery research. Knowledge of similarities and differences between the mouse and human glycomes is critical when model mice are used for the discovery of glycan-related biomarkers and targets for therapeutic intervention. Since few comparative glycomic studies between human and mouse have been conducted, we performed a comprehensive comparison of the major classes of glycans in human and mouse sera using mass spectrometric and liquid chromatographic analyses. Up to 131 serum glycans, including N-glycans, free oligosaccharides (fOSs), glycosaminoglycans, O-glycans, and glycosphingolipid (GSL)-glycans, were quantified. In both serum samples, N-glycans were the most abundant in the total serum glycome, while fOSs were the least abundant. As expected, the diversity of sialic acid (i.e. Neu5Ac vs. Neu5Gc) was the major species difference between human and mouse in terms of N- and O-glycosylation, while GSL-glycomic profiles were completely different, even when the sialic acid diversity was taken into consideration. Furthermore, total serum glycomics of STAM mouse were unveiled as an initial step to identify novel biomarkers of liver diseases, with which we could identify several glycans with expression significantly increased or decreased expression.

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Section: Resultssupporting

confidence: 90%

Section: Resultsmentioning

confidence: 71%

Section: Resultsmentioning

confidence: 88%

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Quantitative analysis of total serum glycome in human and mouse

et al. 2016

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“…On a more global scale, proteomic analyses of AD brains revealed altered glycosylation of 131 GlcNacylation sites in 81 proteins. Another global study comparing brains and sera from HD transgenic mice to controls reveals differences in the levels and pattern of glycans [86]. Aberrant glycosylation of an additional ten glycosylated proteins in several NDs (AD, PD, and HD) was summarized previously [87].…”

Section: Glycosylation/glycationmentioning

confidence: 99%

Minimotifs dysfunction is pervasive in neurodegenerative disorders

Sharma

Young²,

Chen

et al. 2018

A&D Transl Res & Clin Interv

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Minimotifs are modular contiguous peptide sequences in proteins that are important for posttranslational modifications, binding to other molecules, and trafficking to specific subcellular compartments. Some molecular functions of proteins in cellular pathways can be predicted from minimotif consensus sequences identified through experimentation. While a role for minimotifs in regulating signal transduction and gene regulation during disease pathogenesis (such as infectious diseases and cancer) is established, the therapeutic use of minimotif mimetic drugs is limited. In this review, we discuss a general theme identifying a pervasive role of minimotifs in the pathomechanism of neurodegenerative diseases. Beyond their longstanding history in the genetics of familial neurodegeneration, minimotifs are also major players in neurotoxic protein aggregation, aberrant protein trafficking, and epigenetic regulation. Generalizing the importance of minimotifs in neurodegenerative diseases offers a new perspective for the future study of neurodegenerative mechanisms and the investigation of new therapeutics.

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“…64 O-Glycans were removed with ammonium carbamate at 60 °C for 40 h, followed by washing steps and chemoselective capture on BlotGlyco H hydrazide beads and subsequent derivatizations. The original protocol was developed previously and the authors claim that no significant loss due to peeling was observed.…”

Section: Glycan Release Proceduresmentioning

confidence: 99%