Screening, characterization and the novo sequencing of broccoli plasma membrane aquaporins by high resolution mass spectrometry

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Parallel use of CID, HCD and ETD for characterization of proteic allergens found in pollensomes

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iTRAQ-based quantitative analysis of protein mixtures with large fold change and dynamic range

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Top-down and bottom-up quantitative proteomic approaches to characteriza the development of grape berry tissues

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Analysis of directionality effects in magnetodielectric core-shell nanoparticles by means of polarimetric techniques

The influence of increasing the core size of a Ag-Si core-shell nanoparticle has been investigated by using the values of the linear polarization degree at right angle scattering configuration, PL(90º). Changes in dipolar resonances and Scattering Directionality Conditions as a function of the core radius (Rint) for a fixed shell size (Rext = 230 nm) have been analyzed. An empirical formula to obtain the ratio Rint/Rext by monitoring the influence of the magnetic dipolar resonance in PL(90º) has been found.This research was supported by MICINN (FIS2013-45854-P). Ángela I. Barreda and Y. Gutiérrez want to express their gratitude to the University of Cantabria for their FPU grant

Label.-free differential quantitative proteomics of grapevine cell cultures: performanc of two different mass spectrometric platform

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Disección del metabolismo de la baya de vid durante el desarrollo mediante las técnicas de Proteómica cuantitativa DIGE e iTRAQ

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Endoglin Protein Interactome Profiling Identifies TRIM21 and Galectin-3 as New Binding Partners

This article belongs to the Special Issue TGF-beta/BMP Signaling PathwayEndoglin is a 180-kDa glycoprotein receptor primarily expressed by the vascular endothelium and involved in cardiovascular disease and cancer. Heterozygous mutations in the endoglin gene (ENG) cause hereditary hemorrhagic telangiectasia type 1, a vascular disease that presents with nasal and gastrointestinal bleeding, skin and mucosa telangiectases, and arteriovenous malformations in internal organs. A circulating form of endoglin (alias soluble endoglin, sEng), proteolytically released from the membrane-bound protein, has been observed in several inflammation-related pathological conditions and appears to contribute to endothelial dysfunction and cancer development through unknown mechanisms. Membrane-bound endoglin is an auxiliary component of the TGF-ß receptor complex and the extracellular region of endoglin has been shown to interact with types I and II TGF-ß receptors, as well as with BMP9 and BMP10 ligands, both members of the TGF-ß family. To search for novel protein interactors, we screened a microarray containing over 9000 unique human proteins using recombinant sEng as bait. We find that sEng binds with high affinity, at least, to 22 new proteins. Among these, we validated the interaction of endoglin with galectin-3, a secreted member of the lectin family with capacity to bind membrane glycoproteins, and with tripartite motif-containing protein 21 (TRIM21), an E3 ubiquitin-protein ligase. Using human endothelial cells and Chinese hamster ovary cells, we showed that endoglin co-immunoprecipitates and co-localizes with galectin-3 or TRIM21. These results open new research avenues on endoglin function and regulation.This work was supported by grants from Ministerio de Ciencia, Innovación y Universidades of Spain (SAF2013-43421-R to CB and SAF2017-84183-R to MQ), Centro de Investigación Biomédica en Red de Enfermedades Raras (CIBERER; ISCIII-CB06/07/0038 to CB and contract CNV-234-PRF-360 to LR-L) and Consejo Superior de Investigaciones Científicas (CSIC; 201920E022 to CB). JC-V was supported by a postdoctoral contract co-funded by Consejo Superior de Investigaciones Científicas, Ministerio de Ciencia, Innovación y Universidades and the European Social Fund (ESF). CIBERER and CIBERNED are initiatives of the Instituto de Salud Carlos III (ISCIII) of Spain supported by European Regional Development (FEDER) funds

Novel Snail1 Target Proteins in Human Colon Cancer Identified by Proteomic Analysis

This is an open-access article distributed under the terms of the Creative Commons Attribution License.-- et al.[Background]: The transcription factor Snail1 induces epithelial-to-mesenchymal transition (EMT), a process responsible for the acquisition of invasiveness during tumorigenesis. Several transcriptomic studies have reported Snail1-regulated genes in different cell types, many of them involved in cell adhesion. However, only a few studies have used proteomics as a tool for the characterization of proteins mediating EMT. [Methodology/Principal Findings]: We identified by proteomic analysis using 2D-DIGE electrophoresis combined with MALDI-TOF-TOF and ESI-linear ion trap mass spectrometry a number of proteins with variable functions whose expression is modulated by Snail1 in SW480-ADH human colon cancer cells. Validation was performed by Western blot and immunofluorescence analyses. Snail1 repressed several members of the 14-3-3 family of phosphoserine/phosphothreonine binding proteins and also the expression of the Proliferation-associated protein 2G4 (PA2G4) that was mainly localized at the nuclear Cajal bodies. In contrast, the expression of two proteins involved in RNA processing, the Cleavage and polyadenylation specificity factor subunit 6 (CPSF6) and the Splicing factor proline/glutamine-rich (SFPQ), was higher in Snail1-expressing cells than in controls. The regulation of 14-3-3 epsilon, 14-3-3 tau, 14-3-3 zeta and PA2G4 by Snail1 was reproduced in HT29 colon cancer cells. In addition, we found an inverse correlation between 14-3-3 sigma and Snail1 expression in human colorectal tumors. [Conclusions/Significance]: We have identified a set of novel Snail1 target proteins in colon cancer that expand the cellular processes affected by Snail1 and thus its relevance for cell function and phenotype.Peer reviewe