Glycosylation Changes in Brain Cancer

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dc.contributor.authorVeillon, Lucas J.
dc.contributor.authorFakih, Christina
dc.contributor.authorAbou-El-Hassan, Hadi
dc.contributor.authorKobeissy, Firas H.
dc.contributor.authorMechref, Yehia S.
dc.contributor.departmentBiochemistry and Molecular Genetics
dc.contributor.facultyFaculty of Medicine (FM)
dc.contributor.institutionAmerican University of Beirut
dc.date.accessioned2025-01-24T11:37:59Z
dc.date.available2025-01-24T11:37:59Z
dc.date.issued2018
dc.description.abstractProtein glycosylation is a posttranslational modification that affects more than half of all known proteins. Glycans covalently bound to biomolecules modulate their functions by both direct interactions, such as the recognition of glycan structures by binding partners, and indirect mechanisms that contribute to the control of protein conformation, stability, and turnover. The focus of this Review is the discussion of aberrant glycosylation related to brain cancer. Altered sialylation and fucosylation of N- and O-glycans play a role in the development and progression of brain cancer. Additionally, aberrant O-glycan expression has been implicated in brain cancer. This Review also addresses the clinical potential and applications of aberrant glycosylation for the detection and treatment of brain cancer. The viable roles glycans may play in the development of brain cancer therapeutics are addressed as well as cancer-glycoproteomics and personalized medicine. Glycoprotein alterations are considered as a hallmark of cancer while high expression in body fluids represents an opportunity for cancer assessment. © 2017 American Chemical Society.
dc.identifier.doihttps://doi.org/10.1021/acschemneuro.7b00271
dc.identifier.eid2-s2.0-85040645921
dc.identifier.pmid28982002
dc.identifier.urihttp://hdl.handle.net/10938/28947
dc.language.isoen
dc.publisherAmerican Chemical Society
dc.relation.ispartofACS Chemical Neuroscience
dc.sourceScopus
dc.subjectAberrant glycosylation
dc.subjectBone marrow-derived human mesenchymal stem cells
dc.subjectBrain cancer
dc.subjectCancer stem cells
dc.subjectCarcinoembryonic antigen
dc.subjectCentral nervous system
dc.subjectGlioblastoma
dc.subjectGlioma stem cells
dc.subjectGlycosylation
dc.subjectHuman mucin family
dc.subjectPosttranslational modification of proteins
dc.subjectSmall cell lung carcinomas
dc.subjectAnimals
dc.subjectBrain neoplasms
dc.subjectHumans
dc.subjectPolysaccharides
dc.subjectBiological marker
dc.subjectGlycan
dc.subjectGlycoprotein
dc.subjectPolysaccharide
dc.subjectCancer diagnosis
dc.subjectCancer growth
dc.subjectCancer therapy
dc.subjectDrug delivery system
dc.subjectFucosylation
dc.subjectHuman
dc.subjectNanotechnology
dc.subjectNonhuman
dc.subjectPersonalized medicine
dc.subjectPriority journal
dc.subjectProtein expression
dc.subjectProtein glycosylation
dc.subjectProteomics
dc.subjectReview
dc.subjectSialylation
dc.subjectAnimal
dc.subjectBrain tumor
dc.subjectMetabolism
dc.titleGlycosylation Changes in Brain Cancer
dc.typeReview

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