Cell migration—The role of integrin glycosylation |
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Authors: | Marcelina E. Janik Anna Lityńska Pierre Vereecken |
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Affiliation: | 1. Department of Glycoconjugate Biochemistry, Institute of Zoology, Jagiellonian University, Krakow, Poland;2. Department of Dermatology, CHU-Brugmann, Belgium;3. Department of Dermatology, Erasme Hospital, Belgium;4. Department of Medical Oncology, Jules Bordet Institute, Brussels, Belgium;5. Laboratiore d''Oncologie Chirurgicale et Expérimentale (LOCE), Bordet Institute, Belgium |
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Abstract: | BackgroundCell migration is an essential process in organ homeostasis, in inflammation, and also in metastasis, the main cause of death from cancer. The extracellular matrix (ECM) serves as the molecular scaffold for cell adhesion and migration; in the first phase of migration, adhesion of cells to the ECM is critical. Engagement of integrin receptors with ECM ligands gives rise to the formation of complex multiprotein structures which link the ECM to the cytoplasmic actin skeleton. Both ECM proteins and the adhesion receptors are glycoproteins, and it is well accepted that N-glycans modulate their conformation and activity, thereby affecting cell–ECM interactions. Likely targets for glycosylation are the integrins, whose ability to form functional dimers depends upon the presence of N-linked oligosaccharides. Cell migratory behavior may depend on the level of expression of adhesion proteins, and their N-glycosylation that affect receptor-ligand binding.Scope of reviewThe mechanism underlying the effect of integrin glycosylation on migration is still unknown, but results gained from integrins with artificial or mutated N-glycosylation sites provide evidence that integrin function can be regulated by changes in glycosylation.General significanceA better understanding of the molecular mechanism of cell migration processes could lead to novel diagnostic and therapeutic approaches and applications. For this, the proteins and oligosaccharides involved in these events need to be characterized. |
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Keywords: | APC protein, adenomatous polyposis coli protein ATRA, all-trans retinoic acid BM, basal membrane CMP-NeuAc, cytidine monophosphate-sialic acid Csk, C-terminal Src kinase ECM, extracellular matrix EGF, epidermal growth factor ER, endoplasmic reticulum ERK, extracellular signal regulated kinase FA, focal adhesion FAK, focal adhesion kinase FN, fibronectin Fut8, α1,6-fucosyltransferase Gal, galactose GlcNAc, N-acetylglucosamine GnT, N-acetylglucosaminyltransferase GSK3β, glycogen synthase kinase-3β GTP, guanosine triphosphate HGF, hepatocyte growth factor ILK, integrin linked kinase JEB, junctional epidermolysis bullosa JNK, c-Jun protein kinase LEF-1, lymphoid enhancer-binding factor 1 LN-332, laminin 332 MAA, Maackia amurensis agglutinin Man, mannose MAPK, mitogen-activated protein kinase MMP, matrix metalloproteinase MT1-MMP, membrane type 1 matrix metalloproteinase p130Cas, Crk-associated substrate PAK, p21 activated kinase PHA-L, Phaseolus vulgaris leucoagglutinin PI3K, phosphatidylinositol 3-kinase PKC, protein kinase C PYK2, proline-rich tyrosine kinase-2 RGD, arginine-glycin-aspartic acid RTK, receptor tyrosine kinase SNA, Sambucus nigra lectin ST6GalI, α2-6 sialyltransferase I TCF, T-cell factor TGF-β1, transforming growth factor-β1 VN, vitronectin |
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