Detection of proteome changes in human colon cancer induced by cell surface binding of growth-inhibitory human galectin-4 using quantitative SILAC-based proteomics
Endogenous lectins have the capacity to translate glycan-encoded information on the cell surface into effects on cell growth. As test cases to examine changes in protein presence associated with tumor growth inhibition, we applied SILAC-based proteomics on human colon carcinoma cells treated with ga...
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| Hauptverfasser: | , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
1 November 2016
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| In: |
Journal of proteome research
Year: 2016, Jahrgang: 15, Heft: 12, Pages: 4412-4422 |
| ISSN: | 1535-3907 |
| DOI: | 10.1021/acs.jproteome.6b00473 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1021/acs.jproteome.6b00473
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| Verfasserangaben: | Malwina Michalak, Uwe Warnken, Sabine André, Martina Schnölzer, Hans-Joachim Gabius, and Juergen Kopitz |
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| 245 | 1 | 0 | |a Detection of proteome changes in human colon cancer induced by cell surface binding of growth-inhibitory human galectin-4 using quantitative SILAC-based proteomics |c Malwina Michalak, Uwe Warnken, Sabine André, Martina Schnölzer, Hans-Joachim Gabius, and Juergen Kopitz |
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| 520 | |a Endogenous lectins have the capacity to translate glycan-encoded information on the cell surface into effects on cell growth. As test cases to examine changes in protein presence associated with tumor growth inhibition, we applied SILAC-based proteomics on human colon carcinoma cells treated with galectin-4 (Gal-4). The five tested lines—LS 180, Vaco 432, Colo 205, CX 1, and HCT 116—responded with differentiation and reduced proliferation to Gal-4 binding. In proteomic analysis (mass spectral data deposited with PRIDE, PXD003489), 2654 proteins were quantified, of which 190 were down-regulated and 115 were up-regulated (>2-fold). 1D annotation analysis of the results indicated down-regulation of DNA replication-associated processes, while protein presence for secretory and transport functions appeared increased. The strongest induction was found for CALB2 (calretinin; ∼24-fold), TGM2 (protein-glutamine γ-glutamyltransferase 2; ∼11-fold), S100A3 (∼10-fold), and GSN (gelsolin; 9.5-fold), and the most pronounced decreases were seen for CDKN2A (tumor suppressor ARF; ∼6-fold), EPCAM (epithelial cell adhesion molecule; ∼6-fold), UBE2C (ubiquitin-conjugating enzyme E2 C; ∼5-fold), KIF2C (kinesin-like protein KIF2C; 5-fold), and LMNB1 (lamin-B1; ∼5-fold). The presence of the common proliferation marker Ki-67 was diminished about 4-fold. By tracing significant alterations of protein expression likely relevant for the observed phenotypic effects, the capacity of a galectin to affect the proteome of human colon cancer cells at multiple sites is revealed. | ||
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