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Mesenchymal Stromal Cells Regulate Sialylations of N-Glycans, Affecting Cell Migration and Survival

N-Glycomics of Human Erythrocytes

CNR, Institute for Polymers, Composites and Biomaterials (IPCB), 95126 Catania, Italy
Laboratorio di Sanità Pubblica, Sezione Tossicologia, Azienda Sanitaria Provinciale (ASP), 95124 Catania, Italy
Child Neurology and Psychiatry, Department of Clinical and Experimental Medicine, University of Catania, 95123 Catania, Italy
Authors to whom correspondence should be addressed.
These authors have contributed equally to this work.
Academic Editor: Hartmut Schlüter
Int. J. Mol. Sci. 2021, 22(15), 8063;
Received: 6 July 2021 / Revised: 22 July 2021 / Accepted: 26 July 2021 / Published: 28 July 2021
(This article belongs to the Special Issue Glycomics: Implications for Metabolic Health and Disease)
Glycosylation is a complex post-translational modification that conveys functional diversity to glycoconjugates. Cell surface glycosylation mediates several biological activities such as induction of the intracellular signaling pathway and pathogen recognition. Red blood cell (RBC) membrane N-glycans determine blood type and influence cell lifespan. Although several proteomic studies have been carried out, the glycosylation of RBC membrane proteins has not been systematically investigated. This work aims at exploring the human RBC N-glycome by high-sensitivity MALDI-MS techniques to outline a fingerprint of RBC N-glycans. To this purpose, the MALDI-TOF spectra of healthy subjects harboring different blood groups were acquired. Results showed the predominant occurrence of neutral and sialylated complex N-glycans with bisected N-acetylglucosamine and core- and/or antennary fucosylation. In the higher mass region, these species presented with multiple N-acetyllactosamine repeating units. Amongst the detected glycoforms, the presence of glycans bearing ABO(H) antigens allowed us to define a distinctive spectrum for each blood group. For the first time, advanced glycomic techniques have been applied to a comprehensive exploration of human RBC N-glycosylation, providing a new tool for the early detection of distinct glycome changes associated with disease conditions as well as for understanding the molecular recognition of pathogens. View Full-Text
Keywords: red blood cells; N-glycosylation; MALDI-TOF; ABO(H) blood groups red blood cells; N-glycosylation; MALDI-TOF; ABO(H) blood groups
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MDPI and ACS Style

Bua, R.O.; Messina, A.; Sturiale, L.; Barone, R.; Garozzo, D.; Palmigiano, A. N-Glycomics of Human Erythrocytes. Int. J. Mol. Sci. 2021, 22, 8063.

AMA Style

Bua RO, Messina A, Sturiale L, Barone R, Garozzo D, Palmigiano A. N-Glycomics of Human Erythrocytes. International Journal of Molecular Sciences. 2021; 22(15):8063.

Chicago/Turabian Style

Bua, Rosaria O., Angela Messina, Luisa Sturiale, Rita Barone, Domenico Garozzo, and Angelo Palmigiano. 2021. "N-Glycomics of Human Erythrocytes" International Journal of Molecular Sciences 22, no. 15: 8063.

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