RT Journal Article
SR Electronic
T1 Aberrant Glycosylation of α<sub>v</sub>β<sub>3</sub> Integrin is Associated with Melanoma Progression
JF Anticancer Research
JO Anticancer Res
FD International Institute of Anticancer Research
SP 2093
OP 2103
VO 35
IS 4
A1 EWA POCHEĆ
A1 MONIKA BUBKA
A1 MAGDALENA RYDLEWSKA
A1 MARCELINA JANIK
A1 MAŁGORZATA POKRYWKA
A1 ANNA LITYŃSKA
YR 2015
UL http://ar.iiarjournals.org/content/35/4/2093.abstract
AB N-glycosylation of integrins plays an important role in cancer progression. Increased αvβ3 integrin expression during melanoma progression is well-documented but the role of its glycans in tumorigenesis is still poorly understood. In the present study we used the WM793 primary melanoma cell line and its highly metastatic variant, WM1205Lu, to examine αvβ3 glycosylation. Lectin precipitation, enzyme digestion and the use of swainsonine (SW) showed that αvβ3 integrin glycosylation differs significantly between primary and metastatic melanoma cells. High-mannose structures and complex glycans with bisecting N-acetylglucosamine (GlcNAc) were more abundant in both subunits of primary cells. We also observed a shift in the sialylation of αvβ3 integrin related to reduction of α2-6-linked sialic acid expression and an increase of α2-3 sialylation of both subunits in melanoma progression. Metastatic melanoma migration on vitronectin (VN) was reduced in the presence of antibody against αvβ3 and the lectins phytohemagglutinin-L (PHA-L), Sambucus nigra agglutinin (SNA) and Maackia amurensis (MAA) in woundhealing assays. Our results show that the acquisition of metastatic competence by melanoma cells is accompanied by alteration of αvβ3 integrin glycosylation and that both αvβ3 and β1-6-branched sialylated complex-type N-glycans promote metastatic melanoma migration on VN.