Emilio Camafeita

Centro de Investigación en Red en Enfermedades Cardiovasculares

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Juan Antonio López

Spanish National Centre for Cardiovascular Research

Jesús Vázquez

Spanish National Centre for Cardiovascular Research

Inmaculada Jorge

Centro de Investigación en Red en Enfermedades Cardiovasculares

Enrique Calvo

Spanish National Centre for Cardiovascular Research

José Luis Martín‐Ventura

Hospital Universitario Fundación Jiménez Díaz

Enrique Méndez

Universidad de Cuautitlán Izcalli

Belén Peral

Instituto de Investigaciones Biomédicas Sols-Morreale

María Gómez‐Serrano

Spanish National Centre for Cardiovascular Research

Jesús Egido

Hospital Universitario Fundación Jiménez Díaz

Patricia Alfonso

Centro de Investigación y Tecnología Agroalimentaria de Aragón

Cooperative Institutions

Spanish National Centre for Cardiovascular Research

175

Universidad Autónoma de Madrid

142

Instituto de Salud Carlos III

119

Consejo Superior de Investigaciones Científicas

116

Centro de Investigación Biomédica en Red

108

Centro de Investigación en Red en Enfermedades Cardiovasculares

Universidad Complutense de Madrid

Hospital Universitario Fundación Jiménez Díaz

Centro de Biología Molecular Severo Ochoa

Centro Nacional de Biotecnología

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Proteomic Analysis of Polymorphonuclear Neutrophils Identifies Catalase as a Novel Biomarker of Abdominal Aortic Aneurysm: Potential Implication of Oxidative Stress in Abdominal Aortic Aneurysm Progression

Arteriosclerosis Thrombosis and Vascular Biology (2011)

Priscila Ramos‐Mozo Julio Madrigal‐Matute Roxana Martínez-Pinna Luis Miguel Blanco‐Colio Juan Antonio López

Polymorphonuclear neutrophils (PMNs) play a main role in abdominal aortic aneurysm (AAA) progression. We have analyzed circulating PMNs isolated from AAA patients and controls by a proteomic approach to identify proteins potentially involved in AAA pathogenesis.PMNs from 8 AAA patients (4 large AAA >5 cm and 4 small AAA 3-5 cm) and 4 controls were analyzed by 2D differential in-gel electrophoresis. Among differentially expressed spots, several proteins involved in redox balance were identified by mass spectrometry (eg, cyclophilin, thioredoxin reductase, catalase). Diminished catalase expression and activity were observed in PMNs from AAA patients compared with controls. In contrast, PMNs from AAA patients displayed higher H(2)O(2) and myeloperoxidase levels than PMNs from controls. Moreover, a significant decrease in catalase mRNA levels was observed in PMNs after phorbol 12-myristate 13-acetate incubation. Catalase plasma levels were also decreased in large (n=47) and small (n=56) AAA patients compared with controls (n=34). We observed catalase expression in AAA thrombus and thrombus-conditioned medium, associated with PMN infiltration. Furthermore, increased H(2)O(2) levels were observed in AAA thrombus-conditioned medium compared with the media layer.Diminished catalase levels in circulating PMNs and plasma are observed in AAA patients, supporting an important role of oxidative stress in AAA evolution.

10.1161/atvbaha.111.237537

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Citations (76)

Uncovering sexual dimorphism in type 2 diabetes by redox proteomics.

IBJ Plus (2019)

María Gómez‐Serrano Emilio Camafeita Jesús Vázquez María Gómez‐Serrano Emilio Camafeita

Sexual dimorphism

10.24217/2531-0151.19v1s3.00021

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Técnicas de proteómica en la investigación endometrial y embriónica

Emilio Camafeita Enrique Calvo Juan Antonio López García

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A new approach for systems biology analysis of high-throughput quantitative proteomics experiments

Proteómica: revista de la Sociedad Española de Proteómica (2013)

Marco Trevisán Herraz Elena Bonzón‐Kulichenko Juan Carlos Silla-Castro Emilio Camafeita Inmaculada Jorge

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Quantification of Farnesylated Progerin in Hutchinson-Gilford Progeria Patient Cells by Mass Spectrometry

International Journal of Molecular Sciences (2022)

Emilio Camafeita Inmaculada Jorge José Rivera Vicente Andrés Jesús Vázquez

Hutchinson-Gilford progeria syndrome (HGPS) is a rare fatal disorder characterized by premature aging and death at a median age of 14.5 years. The most common cause of HGPS (affecting circa 90% of patients) is a de novo heterozygous synonymous single-base substitution (c.1824C>T; p.G608G) in the LMNA gene that results in the accumulation of progerin, an aberrant form of lamin A that, unlike mature lamin A, remains permanently farnesylated. The ratio of progerin to mature lamin A correlates with disease severity in HGPS patients, and can be used to assess the effectiveness of therapies aimed at lessening aberrant splicing or progerin farnesylation. We recently showed that the endogenous content of lamin A and progerin can be measured by mass spectrometry (MS), providing an alternative to immunological methods, which lack the necessary specificity and quantitative accuracy. Here, we present the first non-immunological method that reliably quantifies the levels of wild-type lamin A and farnesylated progerin in cells from HGPS patients. This method, which is based on a targeted MS approach and the use of isotope-labeled internal standards, could be applied in ongoing clinical trials evaluating the efficacy of drugs that inhibit progerin farnesylation.

Progeria

LMNA

10.3390/ijms231911733

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Protein phosphorylation analysis in archival clinical cancer samples by shotgun and targeted proteomics approaches

Molecular BioSystems (2011)

Angelo Gámez‐Pozo Iker Sánchez‐Navarro Enrique Calvo Esther Díaz María Miguel-Martín

Protein phosphorylation affects most eukaryotic cellular processes and its deregulation is considered a hallmark of cancer and other diseases. Phosphoproteomics may enable monitoring of altered signaling pathways as a means of stratifying tumors and facilitating the discovery of new drugs. Unfortunately, the development of molecular tests for clinical use is constrained by the limited availability of fresh frozen, clinically annotated samples. Here we report phosphopeptide analysis in human archival formalin-fixed, paraffin-embedded (FFPE) cancer samples based on immobilized metal affinity chromatography followed by liquid chromatography coupled with tandem mass spectrometry and selected reaction monitoring techniques. Our results indicate the equivalence of detectable phosphorylation rates in archival FFPE and fresh frozen tissues. Moreover, we demonstrate the applicability of targeted assays for phosphopeptide analysis in clinical archival FFPE samples, using an experimental workflow suitable for processing and analyzing large sample series. This work paves the way for the application of shotgun and targeted phosphoproteomics approaches in clinically relevant studies using archival clinical samples.

Phosphoproteomics

Phosphopeptide

Shotgun proteomics

Shotgun

10.1039/c1mb05113j

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Differential shotgun analysis of mesenchymal stem cells from osteoarthritis patients

Proteómica: revista de la Sociedad Española de Proteómica (2011)

Emilio Camafeita P. Tornero Enrique Calvo E. Villafuertes Jania Acosta López

Osteoarthritis (OA) is a chronic, degenerative disease with multifactorial etiology which constitutes the most common cause of pain and disability in older adults, as well as the leading cause of joint replacement surgery. The degradation of articular cartilage in osteoarthritis is related to changes in the composition of the extracelular matrix and the alteration of protein expression by chondrocytes, the only cell component of cartilage, along with well-defined changes in the subchondral and periarticular bone. Since the application of therapies based on cells with regenerative potential like mesenchymal stem cells (MSCs), progenitor cells with the capacity to differentiate into distinct connective tissues including cartilage, represent a promising strategy for the treatment of OA, we have searched in this work for altered proteins in bone marrow MSCs obtained from osteoarthritis patients using a shotgun approach.

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Vascular Proteomics

Springer eBooks (2016)

José Luis Martı́n-Ventura Elena Burillo Roxana Martínez-Pinna Diego Martínez-López Luis Miguel Blanco‐Colio

Extracellular Vesicles

10.1007/978-3-319-31828-8_5

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SARS-CoV-2 protein Nsp1 alters actomyosin cytoskeleton and phenocopies arrhythmogenic cardiomyopathy-related PKP2 mutant

bioRxiv (Cold Spring Harbor Laboratory) (2020)

Cristina Márquez-López Marta Roche-Molina Nieves García-Quintáns Silvia Sacristán David Siniscalco

Abstract Mutations in desmosomal Plakophilin-2 (PKP2) are the most prevalent drivers of arrhythmogenic cardiomyopathy (ACM) and a common cause of sudden cardiac death in young athletes. However, partner proteins that elucidate PKP2 cellular mechanism to understand cardiac dysfunction in ACM are mostly unknown. Here we identify the actin-based motor proteins Myh9 and Myh10 as key PKP2 interactors, and demonstrate that the expression of the ACM-related PKP2 mutant R735X alters actin fiber organization and cell mechanical stiffness. We also show that SARS-CoV-2 Nsp1 protein acts similarly to this known pathogenic R735X mutant, altering the actomyosin component distribution on cardiac cells. Our data reveal that the viral Nsp1 hijacks PKP2 into the cytoplasm and mimics the effect of delocalized R735X mutant. These results demonstrate that cytoplasmic PKP2, wildtype or mutant, induces the collapse of the actomyosin network, since shRNA- PKP2 knockdown maintains the cell structure, validating a critical role of PKP2 localization in the regulation of actomyosin architecture. The fact that Nsp1 and PKP2 mutant R735X share similar phenotypes also suggests that direct SARS-CoV-2 heart infection could induce a transient ACM-like disease in COVID-19 patients, which may contribute to right ventricle dysfunction, observed in patients with poor survival prognosis. Highlights The specific cardiac isoform Plakophilin-2a (PKP2) interacts with Myh9 and Myh10. PKP2 delocalization alters actomyosin cytoskeleton component organization. SARS-CoV-2 Nsp1 protein hijacks PKP2 from the desmosome into the soluble fraction where it is downregulated. Viral Nsp1 collapses the actomyosin cytoskeleton and phenocopies the arrhythmogenic cardiomyopathy-related mutant R735X.

Phenocopy

Plakoglobin

10.1101/2020.09.14.296178

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Uncovering Suitable Reference Proteins for Expression Studies in Human Adipose Tissue with Relevance to Obesity

PLoS ONE (2012)

Rafael Pérez‐Pérez Juan Antonio López Eva García‐Santos Emilio Camafeita María Gómez‐Serrano

Background Protein expression studies based on the two major intra-abdominal human fat depots, the subcutaneous and the omental fat, can shed light into the mechanisms involved in obesity and its co-morbidities. Here we address, for the first time, the identification and validation of reference proteins for data standardization, which are essential for accurate comparison of protein levels in expression studies based on fat from obese and non-obese individuals. Methodology and Findings To uncover adipose tissue proteins equally expressed either in omental and subcutaneous fat depots (study 1) or in omental fat from non-obese and obese individuals (study 2), we have reanalyzed our previously published data based on two-dimensional fluorescence difference gel electrophoresis. Twenty-four proteins (12 in study 1 and 12 in study 2) with similar expression levels in all conditions tested were selected and identified by mass spectrometry. Immunoblotting analysis was used to confirm in adipose tissue the expression pattern of the potential reference proteins and three proteins were validated: PARK7, ENOA and FAA. Western Blot analysis was also used to test customary loading control proteins. ENOA, PARK7 and the customary loading control protein Beta-actin showed steady expression profiles in fat from non-obese and obese individuals, whilst FAA maintained steady expression levels across paired omental and subcutaneous fat samples. Conclusions ENOA, PARK7 and Beta-actin are proper reference standards in obesity studies based on omental fat, whilst FAA is the best loading control for the comparative analysis of omental and subcutaneous adipose tissues either in obese and non-obese subjects. Neither customary loading control proteins GAPDH and TBB5 nor CALX are adequate standards in differential expression studies on adipose tissue. The use of the proposed reference proteins will facilitate the adequate analysis of proteins differentially expressed in the context of obesity, an aim difficult to achieve before this study.

10.1371/journal.pone.0030326

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Citations (26)