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Grape leaves polyphenols inhibit breast cancer malignancy

ABSTRACT: We tested the inhibitory effects of hydroalcoholic extracts from grape leaves in breast cancer malignancy using MCF-7 and SKBR-3 cell lines.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Breast Cancer

SUBMITTER: maria tomasi

LAB HEAD: Maria Lauda Tomasi

PROVIDER: PXD016748 | Pride | 2020-05-27

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	18_5_Human_DECOY.fasta	Fasta
	Lauda_DDA_Human_Publication.iprophet.pep.xml	Pepxml
	M1.raw	Raw
	M2.raw	Raw
	M3.raw	Raw

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1 - 5 of 8

Publications

SUMOylation Protects FASN Against Proteasomal Degradation in Breast Cancer Cells Treated with Grape Leaf Extract.

Floris Andrea A Mazarei Michael M Yang Xi X Robinson Aaron Elias AE Zhou Jennifer J Barberis Antonio A D'hallewin Guy G Azara Emanuela E Spissu Ylenia Y Iglesias-Ara Ainhoa A Orrù Sandro S Tomasi Maria Lauda ML

Biomolecules 20200331 4

Existing therapeutic strategies for breast cancer are limited by tumor recurrence and drug-resistance. Antioxidant plant-derived compounds such as flavonoids reduce adverse outcomes and have been identified as a potential source of antineoplastic agent with less undesirable side effects. Here, we describe the novel regulation of fatty-acid synthase (FASN), the key enzyme in de novo fatty-acid synthesis, whereby <i>Vitis vinifera</i> L. cv Vermentino leaf hydroalcoholic extract lowers its protein ...[more]

PMID: 32244364

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Proteome Dynamics Reveals Pro-inflammatory Remodeling of Plasma Proteome in a Mouse Model of NAFLD

Project description:Nonalcoholic fatty liver disease (NAFLD) is associated with an increased risk of cardiovascular disease (CVD). Liver is the major source of the circulatory proteins and alterations in plasma proteome have been implicated in atherosclerosis. We used a recently developed 2H2O-metabolic labeling method in combination with the label-free quantification to evaluate the effect of a Western diet (WD) on the dynamics of plasma proteins in LDL receptor-deficient (LDLR-/-) mice, a model of NAFLD and atherosclerosis. There were no significant changes in the expression level of total proteins due to the WD with a bulk protein mean half-life of 18.0±15.1 hours in control and 16.7±11.1 hours in WD groups. WD led to pro-inflammatory distribution of circulatory proteins analyzed in apoB-depleted plasma attributed to their increased production. The fractional catabolic rates of fast-turnover proteins with stress-response, lipid metabolism and transport functions were significantly increased with WD (P<0.05). The pathway analyses revealed that alterations in plasma proteome dynamics were related to the suppression of hepatic PPARα, which was confirmed based on reduced gene and protein expression of PPARα on WD. These changes were associated with ~4 fold increase (P<0.0001) in pro-inflammatory property of apoB-depleted plasma. In conclusion, the proteome dynamics method reveals pro-inflammatory remodeling of plasma proteome relevant to liver disease. As in vivo metrics of liver function, this approach can be used to test therapies in NAFLD and other diseases

2016-06-06 | PXD004270 | Pride

Validation of filter aided sample preparation (FASP) approach for quantitative plant shotgun proteomics

Project description:Gel-free LC-based shotgun proteomics represents the current gold standard of proteome analysis due to its outstanding throughput, analytical resolution and reproducibility. Thereby, the efficiency of sample preparation, i.e., protein isolation, solubilization and proteolysis, directly affects the correctness and reliability of quantification, being therefore the bottle neck of shotgun proteomics. The desired performance of the sample preparation protocols can be achieved by application of detergents. However, these ultimately compromise reverse phase chromatographic separation and disrupt electrospray ionization. Filter aided sample preparation (FASP) represents an elegant approach to overcome these limitations. Although this method is comprehensively validated for cell proteomics, its applicability to plants and compatibility with plant-specific protein isolation protocols is still unknown, i.e., no data on linearity of underlying protein quantification methods for plant matrices is available. To fill this gap, we address here the potential of FASP in combination with two protein isolation protocols for quantitative analysis of pea (Pisum sativum) seed and Arabidopsis thaliana leaf proteomes by the shotgun approach. For this, in comprehensive spiking experiments with bovine serum albumin (BSA), we evaluated the linear dynamic range (LDR) of protein quantification in the presence of plant matrices. Further, we addressed the interference of two different plant matrices in quantitative experiments, accomplished with two alternative sample preparation workflows in comparison to conventional FASP-based digestion of cell lysates, considered here as a reference. Our results indicate very good applicability of FASP to quantitative plant proteomics with an only limited impact of the protein isolation technique on the methods overall performance.

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Antisense oligonucleotides targeting nuclear RNA for in vivo correction of myotonic dystrophy

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Bovine protein glycation sites in different milk products

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