01776nas a2200205   4500008004100000245012700041210006900168260000800237300001400245490000700259520101100266100002301277700002501300700002401325700002001349700002101369700002501390700002401415856013101439       2017                        eng d00aMass spectrometry based identification of galectin-3 interacting proteins potentially involved in lung melanoma metastasis0 aMass spectrometry based identification of galectin3 interacting   cNOV  a2303-23090 v133 aAdhesive interactions between molecules on tumor cells and those on target organs play a key role in organ specific metastasis. Poly-N-acetyl-lactosamine (polyLacNAc) substituted N-oligosaccharides on melanoma cell surface glycoproteins promote lung specific metastasis via galectin-3 by facilitating their arrest and extravasation. This study reports the identification and characterization of galectin-3 interacting proteins using a combination of galectin-3 sepharose affinity and leucoagglutinating phytohemagglutinin (L-PHA) columns. A total of 83 proteins were identified as galectin-3 interacting glycoproteins, of which 35 were constituents of the L-PHA bound fraction, suggesting that these proteins carry polyLacNAc substituted beta 1,6 branched N-glycans. The identities of some of these proteins, like LAMP-1, LAMP-3, basigin, embigin, and alpha 5 and beta 1 Integrin, have been confirmed by western blotting, and functional relevance with respect to metastatic properties has been established.1 aDange, Manohar, C.1 aBhonsle, Hemangi, S.1 aGodbole, Rashmi, K.1 aMore, Shyam, K.1 aBane, Sanjay, M.1 aKulkarni, Mahesh, J.1 aKalraiya, Rajiv, D.  uhttps://library.ncl.res.in/content/mass-spectrometry-based-identification-galectin-3-interacting-proteins-potentially-involved