Green fluorescent protein expression triggers proteome changes in breast cancer cells

Coumans, Joëlle V. F.; Gau, David; Poljak, Anne; Wasinger, Valerie C.; Roy, Partha; Moens, Pierre

doi:10.1016/j.yexcr.2013.07.019

Cited by 35 publications

(39 citation statements)

References 37 publications

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“…Alpha-actinin-4 is upregulated in some types of cancer and promotes proliferation of luminal MCF-7 breast cancer cells [37,38]. Profilin is a ubiquitously expressed actin-binding protein that can regulate invadopodia maturation [39] and is overexpressed in breast cancer cells [40]. To our knowledge, profilin-1 has not been previously shown to be associated with NHE1, and this interaction is intriguing considering its role in invadopodia maturation [39].…”

Section: Nhe1 and Cytoskeletal Proteinsmentioning

confidence: 89%

Defining the Na+/H+ exchanger NHE1 interactome in triple-negative breast cancer cells

Amith

Vincent

Wilkinson

et al. 2017

Cellular Signalling

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Section: Nhe1 and Cytoskeletal Proteinsmentioning

confidence: 89%

Defining the Na+/H+ exchanger NHE1 interactome in triple-negative breast cancer cells

Amith

Vincent

Wilkinson

et al. 2017

Cellular Signalling

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“…Synthetic SPP24 peptide, or SPP24 Antibody was bound to the magnetic beads. Pooled whole serum samples grouped into IBD (10 patients) and healthy controls (5 patients) were analyzed for binding partners following trypsin digestion of eluted proteins using an Orbi-trap MS instrument (Thermo Electron, Bremen, Germany)as described by Coumans et.al (29). MS ion abundance was analyzed using QI for proteomics (nonlinear dynamics) as previously described.…”

Section: Methodsmentioning

confidence: 99%

Low Mass Blood Peptides Discriminative of Inflammatory Bowel Disease (IBD) Severity: A Quantitative Proteomic Perspective

Wasinger

Yau

Duo

et al. 2016

Molecular & Cellular Proteomics

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Breakdown of the protective gut barrier releases effector molecules and degradation products into the blood stream making serum and plasma ideal as a diagnostic medium. The enriched low mass proteome is unexplored as a source of differentiators for diagnosing and monitoring inflammatory bowel disease (IBD) activity, that is less invasive than colonoscopy. Differences in the enriched low mass plasma proteome (<25 kDa) were assessed by label-free quantitative mass-spectrometry. A panel of marker candidates were progressed to validation phase and "Tier-2" FDA-level validated quantitative assay. Proteins important in maintaining gut barrier function and homeostasis at the epithelial interface have been quantitated by multiple reaction monitoring in plasma and serum including both inflammatory; rheumatoid arthritis controls, and non-inflammatory healthy controls; ulcerative colitis (UC), and Crohn's disease (CD) patients. Detection by immunoblot confirmed presence at the protein level in plasma. Correlation analysis and receiver operator characteristics were used to report the sensitivity and specificity. Peptides differentiating controls from IBD originate from secreted phosphoprotein 24 (SPP24, p ‫؍‬ 0.000086, 0.009); whereas those in remission and healthy can be differentiated in UC by SPP24 (p ‫؍‬ 0.00023, 0.001), ␣-1-microglobulin (AMBP, p ‫؍‬ 0.006) and CD by SPP24 (p ‫؍‬ 0.019, 0.05). UC and CD can be differentiated by Guanylin (GUC2A, p ‫؍‬ 0.001), and Secretogranin-1 (CHGB p ‫؍‬ 0.035). Active and quiescent disease can also be differentiated in UC and CD by CHGB (p < 0.023) SPP24 (p < 0.023) and AMBP (UC p ‫؍‬ 0.046). Five peptides discriminating IBD activity and severity had very little-to-no correlation to erythrocyte sedimentation rate, C-reactive protein, white cell or platelet counts. Three of these peptides were found to be binding partners to SPP24 protein alongside other known matrix proteins. These proteins have the potential to improve diagnosis and evaluate IBD activity, reducing the need for more invasive techniques. Data are available via ProteomeXchange with identifier

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“…Parental MDA-MB-231 breast cancer cells (referred to as wild-type (WT) cells from here on) and stable MDA-MB-231 clones expressing green fluorescent protein (GFP) and GFP-PFN1 were generated as previously described (Coumans et al, 2014;Zou et al, 2007).…”

Section: Cell Culturementioning

confidence: 99%

“…Protein extraction and quantification were performed as previously described (Coumans et al, 2014). Briefly, cells at 90% of confluence, in 175 cm 2 flasks, were washed twice with PBS, detached from the culture flask by 5 min incubation at 37°C in citric saline solution (1.35 M KCl, 0.15 M sodium citrate), and the cell pellet was used for protein extraction.…”

Section: Protein Extraction and Quantificationmentioning

confidence: 99%

Profilin-1 Overexpression in MDA-MB-231 Breast Cancer Cells Is Associated with Alterations in Proteomics Biomarkers of Cell Proliferation, Survival, and Motility as Revealed by Global Proteomics Analyses

Coumans

Gau

Poljak

et al. 2014

OMICS: A Journal of Integrative Biology

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Despite early screening programs and new therapeutic strategies, metastatic breast cancer is still the leading cause of cancer death in women in industrialized countries and regions. There is a need for novel biomarkers of susceptibility, progression, and therapeutic response. Global analyses or systems science approaches with omics technologies offer concrete ways forward in biomarker discovery for breast cancer. Previous studies have shown that expression of profilin-1 (PFN1), a ubiquitously expressed actin-binding protein, is downregulated in invasive and metastatic breast cancer. It has also been reported that PFN1 overexpression can suppress tumorigenic ability and motility/invasiveness of breast cancer cells. To obtain insights into the underlying molecular mechanisms of how elevating PFN1 level induces these phenotypic changes in breast cancer cells, we investigated the alteration in global protein expression profiles of breast cancer cells upon stable overexpression of PFN1 by a combination of three different proteome analysis methods (2-DE, iTRAQ, label-free). Using MDA-MB-231 as a model breast cancer cell line, we provide evidence that PFN1 overexpression is associated with alterations in the expression of proteins that have been functionally linked to cell proliferation (FKPB1A, HDGF, MIF, PRDX1, TXNRD1, LGALS1, STMN1, LASP1, S100A11, S100A6), survival (HSPE1, HSPB1, HSPD1, HSPA5 and PPIA, YWHAZ, CFL1, NME1) and motility (CFL1, CORO1B, PFN2, PLS3, FLNA, FLNB, NME2, ARHGDIB). In view of the pleotropic effects of PFN1 overexpression in breast cancer cells as suggested by these new findings, we propose that PFN1-induced phenotypic changes in cancer cells involve multiple mechanisms. Our data reported here might also offer innovative strategies for identification and validation of novel therapeutic targets and companion diagnostics for persons with, or susceptibility to, breast cancer.

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Green fluorescent protein expression triggers proteome changes in breast cancer cells

Cited by 35 publications

References 37 publications

Defining the Na+/H+ exchanger NHE1 interactome in triple-negative breast cancer cells

Defining the Na+/H+ exchanger NHE1 interactome in triple-negative breast cancer cells

Low Mass Blood Peptides Discriminative of Inflammatory Bowel Disease (IBD) Severity: A Quantitative Proteomic Perspective

Profilin-1 Overexpression in MDA-MB-231 Breast Cancer Cells Is Associated with Alterations in Proteomics Biomarkers of Cell Proliferation, Survival, and Motility as Revealed by Global Proteomics Analyses

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