Comprehensive Analysis of the Glycome and Glycoproteome of Bovine Milk-Derived Exosomes

Chen, Wenyan; Wang, Rong; Li, Dan; Zuo, Chenyang; Wen, Piaopiao; Liu, Haili; Chen, Yong Q.; Fujita, Morihisa; Wu, Zhimeng; Yang, Ganglong

doi:10.1021/acs.jafc.0c04605

Cited by 31 publications

(25 citation statements)

References 50 publications

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“…In total, 30, 42, 32, 34, and 35 OSs were identified in bovine, caprine, ovine, camel, and human milk, respectively. Most of the OSs found in different species were consistent with previous studies, ,,,,,,,− ,− and some OSs that have not been reported before were also found in our study, which were marked in Table . It is worth mentioning that almost all the reported OSs in the ovine milk were also detected in our study, besides these, the other 13 OSs detected in our study were discovered for the first time.…”

Section: Resultssupporting

confidence: 93%

Comprehensive Identification and Absolute Quantification of Milk Oligosaccharides in Different Species

Shi

Han

Zhang

et al. 2021

J. Agric. Food Chem.

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Human and animal milk contains a rich variety of oligosaccharides (OSs), which are of great interest due to a similar biological efficacy. In this study, the OSs were identified and the concentrations of eight specific OSs in human and four animal milk (cow, goat, sheep, and camel) were analyzed. In general, 30, 42, 32, 34, and 35 OSs were identified in bovine, caprine, ovine, camel, and human milk, respectively. Camel milk was the most similar in type to human milk than other four animal milk. The concentration of eight OSs in human milk was approximately six times higher than that in camel milk, 20 times higher than that in bovine and caprine milk, and 75 times higher than that in ovine milk. Collectively, these findings revealed the characteristics and concentrations of OSs in the milk of different species, providing insights into the potential application of OSs in medical and functional foods.

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Section: Resultssupporting

confidence: 93%

Comprehensive Identification and Absolute Quantification of Milk Oligosaccharides in Different Species

Shi

Han

Zhang

et al. 2021

J. Agric. Food Chem.

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“…For global peptides, the elution gradient was set as follows: 0–8 min, 3% B; 8–88 min, 8% B; 88–110 min, 28% B; 110–115 min, 32% B; 115–120 min, 80% B. Other mass spectrometry parameters were performed according to methods previously established in our laboratory [ 19 ]. For glycopeptides, the gradient elution was 2–6% B, 1 min; 6–30% B, 90 min; 30–38% B, 22 min; 38–80% B, 5 min; and 80% B, 5 min.…”

Section: Methodsmentioning

confidence: 99%

Proteome and Glycoproteome Analyses Reveal the Protein N-Linked Glycosylation Specificity of STT3A and STT3B

Wen

Chen

Zuo

et al. 2022

Cells

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STT3A and STT3B are the main catalytic subunits of the oligosaccharyltransferase complex (OST-A and OST-B in mammalian cells), which primarily mediate cotranslational and post-translocational N-linked glycosylation, respectively. To determine the specificity of STT3A and STT3B, we performed proteomic and glycoproteomic analyses in the gene knock-out (KO) and wild-type HEK293 cells. In total, 3961 proteins, 4265 unique N-linked intact glycopeptides and 629 glycosites representing 349 glycoproteins were identified from all these cells. Deletion of the STT3A gene had a greater impact on the protein expression than deletion of STT3B, especially on glycoproteins. In addition, total mannosylated N-glycans were reduced and fucosylated N-glycans were increased in STT3A-KO cells, which were caused by the differential expression of glycan-related enzymes. Interestingly, hyperglycosylated proteins were identified in KO cells, and the hyperglycosylation of ENPL was caused by the endoplasmic reticulum (ER) stress due to the STT3A deletion. Furthermore, the increased expression of the ATF6 and PERK indicated that the unfolded protein response also happened in STT3A-KO cells. Overall, the specificity of STT3A and STT3B revealed that defects in the OST subunit not only broadly affect N-linked glycosylation of the protein but also affect protein expression.

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“…Intact glycopeptides (IGPs) were enriched as described previously [ 44 ]. IGPs were desalted, resuspended and then analyzed using nanoLC-MS system.…”

Section: Methodsmentioning

confidence: 99%

“…IGPs were desalted, resuspended and then analyzed using nanoLC-MS system. LC conditions and MS parameters for IGPs were described previously [ 44 ]. Results were filtered based on the following criteria: (1) a false discovery rate (FDR) less than 1% for glycoproteins and (2) each peptide spectra matches (PSM) annotated by at least one N-linked glycan.…”

Section: Methodsmentioning

confidence: 99%

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N-glycosylation of GDF15 abolishes its inhibitory effect on EGFR in AR inhibitor-resistant prostate cancer cells

et al. 2022

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Castration-resistance of prostate cancer is one of the most challenging clinical problems. In the present study, we have performed proteomics and glycomics using LNCaP model. Growth differentiation factor-15 (GDF15) level is increased in androgen receptor (AR) inhibitor-resistant cells and the inhibitory effect of GDF15 on epithelial growth factor receptor (EGFR) pathway is relieved by GDF15 N70 glycosylation. Interference of GDF15 (siRNA or N70Q dominant negative) or EGFR pathway (inhibitor or siRNA for EGFR, SRC or ERK) decreases the resistant-cell survival in culture and tumor growth in mice. Our study reveals a novel regulatory mechanism of prostate cancer AR inhibitor resistance, raises the possibility of AR/SRC dual-targeting of castration-resistance of prostate cancer, and lays foundation for the future development of selective inhibitors of GDF15 glycosylation.

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Comprehensive Analysis of the Glycome and Glycoproteome of Bovine Milk-Derived Exosomes

Cited by 31 publications

References 50 publications

Comprehensive Identification and Absolute Quantification of Milk Oligosaccharides in Different Species

Comprehensive Identification and Absolute Quantification of Milk Oligosaccharides in Different Species

Proteome and Glycoproteome Analyses Reveal the Protein N-Linked Glycosylation Specificity of STT3A and STT3B

N-glycosylation of GDF15 abolishes its inhibitory effect on EGFR in AR inhibitor-resistant prostate cancer cells

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