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Abstract
In recent years, plasma N-glycans have emerged as biomarkers for health and disease. Here, we studied N-glycomic changes in Down Syndrome (DS). Because of the progeroid phenotype of DS, we focused on the dissection of syndrome- and aging-associated glycomic changes, as well as the interaction thereof. We analyzed the plasma N-glycome of 76 DS persons, 37 siblings (DSS), and 42 mothers (DSM) of DS persons by DNA-sequencer-aided, fluorophore-assisted-carbohydrate-electrophoresis, as well as by matrix-assisted laser desorption ionization-time-of-flight-mass spectrometry (MALDI-TOF-MS). The results showed an overall decrease of galactosylation and alpha 2,3 sialylation, a concomitant increase of the level of fucosylated N-glycans as well as of monogalactosylated diantennary N-glycans in DS, while the GlycoAgeTest and the ratio of the two core-fucosylated, monogalactosylated diantennary isomers (galactose positioned on alpha 1,6 arm versus alpha 1,3 arm) were the strongest DS discriminators Hypogalactosylation is a characteristic of both DS and aging of control individuals. A decrease in alpha 2,3-sialylated species is also common to DS and aging of controls. However, regarding to alpha 2,6-sialylated tri- and tetragalactosylated N-glycan species, we found those to be lowered in DS but showed an increase with age in the same persons, while these glycans were not affected by aging in control individuals. In conclusion, we identified specific glycomic changes associated with DS, aging in DS, as well as aging in controls, identifying glycomic features in line with accelerated aging in DS. Notably, our data demonstrate an aging phenotype in DS which only in part overlaps with aging in controls but reveals DS-specificity.
Keywords
GLYCAN PROFILES, CHRONIC INFLAMMATION, GLYCOSYLATION, PROTEIN, IGG, AGE, DISEASE, ADULTS, ethyl esterification, MALDI-TOF-MS, DSA-FACE, aging, N-glycome, Down Syndrome, RHEUMATOID-ARTHRITIS, HUMAN SERUM, GlycoAgeTest

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Chicago
Borelli, Vincenzo, Valerie Vanhooren, Emanuela Lonardi, Karli R Reiding, Miriam Capri, Claude Libert, Paolo Garagnani, Stefano Salvioli, Claudio Franceschi, and Manfred Wuhrer. 2015. “Plasma N-glycome Signature of Down Syndrome.” Journal of Proteome Research 14 (10): 4232–4245.
APA
Borelli, V., Vanhooren, V., Lonardi, E., Reiding, K. R., Capri, M., Libert, C., Garagnani, P., et al. (2015). Plasma N-glycome signature of Down syndrome. JOURNAL OF PROTEOME RESEARCH, 14(10), 4232–4245.
Vancouver
1.
Borelli V, Vanhooren V, Lonardi E, Reiding KR, Capri M, Libert C, et al. Plasma N-glycome signature of Down syndrome. JOURNAL OF PROTEOME RESEARCH. 2015;14(10):4232–45.
MLA
Borelli, Vincenzo, Valerie Vanhooren, Emanuela Lonardi, et al. “Plasma N-glycome Signature of Down Syndrome.” JOURNAL OF PROTEOME RESEARCH 14.10 (2015): 4232–4245. Print.
@article{6973749,
  abstract     = {In recent years, plasma N-glycans have emerged as biomarkers for health and disease. Here, we studied N-glycomic changes in Down Syndrome (DS). Because of the progeroid phenotype of DS, we focused on the dissection of syndrome- and aging-associated glycomic changes, as well as the interaction thereof. We analyzed the plasma N-glycome of 76 DS persons, 37 siblings (DSS), and 42 mothers (DSM) of DS persons by DNA-sequencer-aided, fluorophore-assisted-carbohydrate-electrophoresis, as well as by matrix-assisted laser desorption ionization-time-of-flight-mass spectrometry (MALDI-TOF-MS). The results showed an overall decrease of galactosylation and alpha 2,3 sialylation, a concomitant increase of the level of fucosylated N-glycans as well as of monogalactosylated diantennary N-glycans in DS, while the GlycoAgeTest and the ratio of the two core-fucosylated, monogalactosylated diantennary isomers (galactose positioned on alpha 1,6 arm versus alpha 1,3 arm) were the strongest DS discriminators Hypogalactosylation is a characteristic of both DS and aging of control individuals. A decrease in alpha 2,3-sialylated species is also common to DS and aging of controls. However, regarding to alpha 2,6-sialylated tri- and tetragalactosylated N-glycan species, we found those to be lowered in DS but showed an increase with age in the same persons, while these glycans were not affected by aging in control individuals. In conclusion, we identified specific glycomic changes associated with DS, aging in DS, as well as aging in controls, identifying glycomic features in line with accelerated aging in DS. Notably, our data demonstrate an aging phenotype in DS which only in part overlaps with aging in controls but reveals DS-specificity.},
  author       = {Borelli, Vincenzo and Vanhooren, Valerie and Lonardi, Emanuela and Reiding, Karli R and Capri, Miriam and Libert, Claude and Garagnani, Paolo and Salvioli, Stefano and Franceschi, Claudio and Wuhrer, Manfred},
  issn         = {1535-3893},
  journal      = {JOURNAL OF PROTEOME RESEARCH},
  keyword      = {GLYCAN PROFILES,CHRONIC INFLAMMATION,GLYCOSYLATION,PROTEIN,IGG,AGE,DISEASE,ADULTS,ethyl esterification,MALDI-TOF-MS,DSA-FACE,aging,N-glycome,Down Syndrome,RHEUMATOID-ARTHRITIS,HUMAN SERUM,GlycoAgeTest},
  language     = {eng},
  number       = {10},
  pages        = {4232--4245},
  title        = {Plasma N-glycome signature of Down syndrome},
  url          = {http://dx.doi.org/10.1021/acs.jproteome.5b00356},
  volume       = {14},
  year         = {2015},
}

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