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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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Main Authors: Michalak, Malwina (Author) , Warnken, Uwe (Author) , André, Sabine (Author) , Schnölzer, Martina (Author) , Gabius, Hans-Joachim (Author) , Kopitz, Jürgen (Author)
Format: Article (Journal)
Language:English
Published: 1 November 2016
In: Journal of proteome research
Year: 2016, Volume: 15, Issue: 12, Pages: 4412-4422
ISSN:1535-3907
DOI:10.1021/acs.jproteome.6b00473
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1021/acs.jproteome.6b00473
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Author Notes:Malwina Michalak, Uwe Warnken, Sabine André, Martina Schnölzer, Hans-Joachim Gabius, and Juergen Kopitz
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Summary: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.
Item Description:Gesehen am 30.04.2020
Physical Description:Online Resource
ISSN:1535-3907
DOI:10.1021/acs.jproteome.6b00473

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