title: Functional hypotheses for aberrant glycosylation in tumor cells.
abstract: Aberrant glycosylation is a common feature of neoplastic cells. Although described for many years, the role of aberrant patterns of glycosylation is not fully understood. Our group has been focusing on the role of glycosylation in cell:matrix interactions, such as adhesion, spreading and migration on defined substrata (e.g., laminin and fibronectin). Animal lectins, such as galaptins, also seem to be involved in these processes.
authors.affiliation: Instituto Ludwig de Pesquisas sobre o Câncer, São Paulo, Brasil.
authors.forename: R
authors.initials: R
authors.lastname: Chammas
authors.forename: M G
authors.initials: MG
authors.lastname: Jasiulionis
authors.forename: P M
authors.initials: PM
authors.lastname: Cury
authors.forename: L R
authors.initials: LR
authors.lastname: Travassos
authors.forename: R R
authors.initials: RR
authors.lastname: Brentani
mesh_terms: D000818:Animals; D002448:Cell Adhesion / Q000502:physiology*; D005109:Extracellular Matrix / Q000502:physiology*; D006031:Glycosylation; D006388:Hemagglutinins / Q000378:metabolism; D006801:Humans; D016023:Integrins / Q000378:metabolism*; D007797:Laminin / Q000378:metabolism*; D037102:Lectins / Q000378:metabolism; D009369:Neoplasms / Q000378:metabolism*; D017469:Receptors, Fibronectin / Q000378:metabolism*; D014407:Tumor Cells, Cultured
chemical_list: D006388:Hemagglutinins; D016023:Integrins; D007797:Laminin; D037102:Lectins; D017469:Receptors, Fibronectin