Mass spectrometry based identification of galectin-3 interacting proteins potentially involved in lung melanoma metastasis
Title | Mass spectrometry based identification of galectin-3 interacting proteins potentially involved in lung melanoma metastasis |
Publication Type | Journal Article |
Year of Publication | 2017 |
Authors | Dange, MC, Bhonsle, HS, Godbole, RK, More, SK, Bane, SM, Kulkarni, MJ, Kalraiya, RD |
Journal | Molecular Biosystems |
Volume | 13 |
Issue | 11 |
Pagination | 2303-2309 |
Date Published | NOV |
Type of Article | Article |
Abstract | Adhesive 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. |
DOI | 10.1039/c7mb00260b |
Type of Journal (Indian or Foreign) | Foreign |
Impact Factor (IF) | 2.781 |
Divison category:
Biochemical Sciences
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