Integrins are the major cell adhesion glycoproteins involved in cell-extracellular matrix (ECM) interaction and metastasis. Further, glycosylation on integrin is necessary for its proper folding and functionality. Herein, differential expression of integrins viz., alpha v beta 3 and alpha v beta 6 was examined in MDA-MB-231, MDA-MB-468 and MCF-10A cells, which signify three different stages of breast cancer development from highly, metastatic to non-tumorigenic stage. The expression of alpha v beta 3 and alpha v beta 6 integrins at mRNA and protein levels was observed in all three cell lines and the results displayed a distinct pattern of expression. Highly metastatic cells showed enhanced expression of alpha v beta 3 than moderate metastatic and non-tumorigenic cells. The scenario was reversed in case of alpha v beta 6 integrin, which was strongly expressed in moderate metastatic and non-tumorigenic cells. N-glycosylation of alpha v beta 3 and alpha v beta 6 integrins is required for the attachment of cells to ECM proteins like fibronectin. The cell adhesion properties were found to be different in these cancer cells with respect to the type of integrins expressed. The results testify that alpha v beta 3 integrin in highly metastatic cells, alpha v beta 6 integrin in both moderate metastatic and non-tumorigenic cells play an important role in cell adhesion. The investigation typify that N-glycosylation on integrins is also necessary for cell-ECM interaction. Further, glycosylation inhibition by Swainsonine is found to be more detrimental to invasive property of moderate metastatic cells. Conclusively, types of integrins expressed as well as their N-glycosylation pattern alter during the course of breast cancer progression. (C) 2018 Elsevier Inc. All rights reserved.