8 results on '"Sanchez-Rivera L"'
Search Results
2. Role of intestinal brush border peptidases in the simulated digestion of milk proteins
- Author
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Laura Sánchez-Rivera, Francesco Addeo, Isidra Recio, Gianluca Picariello, Pasquale Ferranti, Beatriz Miralles, Gianfranco Mamone, Picariello, G., Miralles, B., Mamone, G., Sanchez Rivera, L., Recio, I., Addeo, Francesco, Ferranti, Pasquale, and European Commission
- Subjects
Proteases ,food.ingredient ,Brush border ,Swine ,Biology ,Brush border membrane hydrolases ,Whey protein isolate ,Degree of hydrolysi ,food ,Degree of hydrolysis ,In vivo ,Skimmed milk ,medicine ,Animals ,Food science ,Brush border membrane hydrolase ,Chromatography, High Pressure Liquid ,Chromatography, Reverse-Phase ,Microvilli ,In vitro digestion model ,Gastrointestinal digestion ,Milk proteins ,Small intestine ,Bioavailability ,medicine.anatomical_structure ,Jejunum ,Biochemistry ,biology.protein ,In vitro digestion models ,Digestion ,Food Science ,Biotechnology ,Peptide Hydrolases - Abstract
[Scope]: This study aimed to assess the impact of the 'often neglected' intestinal brush border membranes (BBMs) hydrolases on dietary peptides, exploring the possibility that the disintegration of proteins progressed in the small intestine up to a >core> of intrinsically stable oligopeptides, persisting independently on the up-stream breakdown. [Methods and results]: Samples of sodium caseinate, skim milk powder, and whey protein isolate were submitted to in vitro simulated gastropancreatic digestion using two different procedures: (i) a simplified model involving the main compartmental specific proteases; (ii) a static digestion method based on a frameset of parameters inferred from in vivo. The gastroduodenal digesta were further hydrolyzed with peptidases from porcine jejunal BBM. The peptidomes arising from the two digestion models, characterized by combined HPLC and MS techniques, differed to some extent. However, only specific protein domains survived digestion, among which are potential bioactive or immunogenic (food allergy) peptides. The degree of hydrolysis (DH) after BBM digestion (70-77%) practically did not differ between the digestion models and significantly increased the DH after duodenal steps. [Conclusion]: Any in vitro digestion model should be supplemented with a jejunal phase to realistically determine the bioaccessibility and bioavailability of dietary peptides., The research was in part supported by the EU Infogest COST (European Cooperation in Science and Technology) Action FA 1005 “Improving health properties of food by sharing our knowledge on the digestive process” by funding a short scientific mission of G. P. in the laboratories at CIAL-CSIC (Madrid, Spain).
- Published
- 2015
3. Author Correction: Elevated plasma complement factor H related 5 protein is associated with venous thromboembolism.
- Author
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Iglesias MJ, Sanchez-Rivera L, Ibrahim-Kosta M, Naudin C, Munsch G, Goumidi L, Farm M, Smith PM, Thibord F, Kral-Pointner JB, Hong MG, Suchon P, Germain M, Schrottmaier W, Dusart P, Boland A, Kotol D, Edfors F, Koprulu M, Pietzner M, Langenberg C, Damrauer SM, Johnson AD, Klarin DM, Smith NL, Smadja DM, Holmström M, Magnusson M, Silveira A, Uhlén M, Renné T, Martinez-Perez A, Emmerich J, Deleuze JF, Antovic J, Soria Fernandez JM, Assinger A, Schwenk JM, Souto Andres JC, Morange PE, Butler LM, Trégouët DA, and Odeberg J
- Published
- 2023
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4. Elevated plasma complement factor H related 5 protein is associated with venous thromboembolism.
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Iglesias MJ, Sanchez-Rivera L, Ibrahim-Kosta M, Naudin C, Munsch G, Goumidi L, Farm M, Smith PM, Thibord F, Kral-Pointner JB, Hong MG, Suchon P, Germain M, Schrottmaier W, Dusart P, Boland A, Kotol D, Edfors F, Koprulu M, Pietzner M, Langenberg C, Damrauer SM, Johnson AD, Klarin DM, Smith NL, Smadja DM, Holmström M, Magnusson M, Silveira A, Uhlén M, Renné T, Martinez-Perez A, Emmerich J, Deleuze JF, Antovic J, Soria Fernandez JM, Assinger A, Schwenk JM, Souto Andres JC, Morange PE, Butler LM, Trégouët DA, and Odeberg J
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- Humans, Biomarkers, Complement Activation, Complement Factor H genetics, Complement System Proteins metabolism, Factor V, Venous Thromboembolism genetics
- Abstract
Venous thromboembolism (VTE) is a common, multi-causal disease with potentially serious short- and long-term complications. In clinical practice, there is a need for improved plasma biomarker-based tools for VTE diagnosis and risk prediction. Here we show, using proteomics profiling to screen plasma from patients with suspected acute VTE, and several case-control studies for VTE, how Complement Factor H Related 5 protein (CFHR5), a regulator of the alternative pathway of complement activation, is a VTE-associated plasma biomarker. In plasma, higher CFHR5 levels are associated with increased thrombin generation potential and recombinant CFHR5 enhanced platelet activation in vitro. GWAS analysis of ~52,000 participants identifies six loci associated with CFHR5 plasma levels, but Mendelian randomization do not demonstrate causality between CFHR5 and VTE. Our results indicate an important role for the regulation of the alternative pathway of complement activation in VTE and that CFHR5 represents a potential diagnostic and/or risk predictive plasma biomarker., (© 2023. The Author(s).)
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- 2023
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5. Identification of Endothelial Proteins in Plasma Associated With Cardiovascular Risk Factors.
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Iglesias MJ, Kruse LD, Sanchez-Rivera L, Enge L, Dusart P, Hong MG, Uhlén M, Renné T, Schwenk JM, Bergstrom G, Odeberg J, and Butler LM
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- Biomarkers blood, Cardiovascular Diseases pathology, Endothelium, Vascular pathology, Female, Heart Disease Risk Factors, Humans, Male, Middle Aged, Cardiovascular Diseases blood, Endothelium, Vascular metabolism, Proteomics methods
- Abstract
Objective: Endothelial cell (EC) dysfunction is a well-established response to cardiovascular disease risk factors, such as smoking and obesity. Risk factor exposure can modify EC signaling and behavior, leading to arterial and venous disease development. Here, we aimed to identify biomarker panels for the assessment of EC dysfunction, which could be useful for risk stratification or to monitor treatment response. Approach and Results: We used affinity proteomics to identify EC proteins circulating in plasma that were associated with cardiovascular disease risk factor exposure. Two hundred sixteen proteins, which we previously predicted to be EC-enriched across vascular beds, were measured in plasma samples (N=1005) from the population-based SCAPIS (Swedish Cardiopulmonary Bioimage Study) pilot. Thirty-eight of these proteins were associated with body mass index, total cholesterol, low-density lipoprotein, smoking, hypertension, or diabetes. Sex-specific analysis revealed that associations predominantly observed in female- or male-only samples were most frequently with the risk factors body mass index, or total cholesterol and smoking, respectively. We show a relationship between individual cardiovascular disease risk, calculated with the Framingham risk score, and the corresponding biomarker profiles., Conclusions: EC proteins in plasma could reflect vascular health status.
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- 2021
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6. Systematic assessment of antibody selectivity in plasma based on a resource of enrichment profiles.
- Author
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Fredolini C, Byström S, Sanchez-Rivera L, Ioannou M, Tamburro D, Pontén F, Branca RM, Nilsson P, Lehtiö J, and Schwenk JM
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- Animals, Antibodies, Monoclonal chemistry, CHO Cells, Chromatography, Liquid, Cricetinae, Cricetulus, Edetic Acid chemistry, Female, Hot Temperature, Humans, Immunoassay, Immunomagnetic Separation, Male, Protein Interaction Mapping, Proteome, Recombinant Proteins chemistry, Tandem Mass Spectrometry, Antibodies chemistry, Blood Proteins analysis, Complement System Proteins chemistry, Plasma chemistry
- Abstract
There is a strong need for procedures that enable context and application dependent validation of antibodies. Here, we applied a magnetic bead assisted workflow and immunoprecipitation mass spectrometry (IP-MS/MS) to assess antibody selectivity for the detection of proteins in human plasma. A resource was built on 414 IP experiments using 157 antibodies (targeting 120 unique proteins) in assays with heat-treated or untreated EDTA plasma. For each protein we determined their antibody related degrees of enrichment using z-scores and their frequencies of identification across all IP assays. Out of 1,313 unique endogenous proteins, 426 proteins (33%) were detected in >20% of IPs, and these background components were mainly comprised of proteins from the complement system. For 45% (70/157) of the tested antibodies, the expected target proteins were enriched (z-score ≥ 3). Among these 70 antibodies, 59 (84%) co-enriched other proteins beside the intended target and mainly due to sequence homology or protein abundance. We also detected protein interactions in plasma, and for IGFBP2 confirmed these using several antibodies and sandwich immunoassays. The protein enrichment data with plasma provide a very useful and yet lacking resource for the assessment of antibody selectivity. Our insights will contribute to a more informed use of affinity reagents for plasma proteomics assays.
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- 2019
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7. Novel Multiomics Profiling of Human Carotid Atherosclerotic Plaques and Plasma Reveals Biliverdin Reductase B as a Marker of Intraplaque Hemorrhage.
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Matic LP, Jesus Iglesias M, Vesterlund M, Lengquist M, Hong MG, Saieed S, Sanchez-Rivera L, Berg M, Razuvaev A, Kronqvist M, Lund K, Caidahl K, Gillgren P, Pontén F, Uhlén M, Schwenk JM, Hansson GK, Paulsson-Berne G, Fagman E, Roy J, Hultgren R, Bergström G, Lehtiö J, Odeberg J, and Hedin U
- Abstract
Clinical tools to identify individuals with unstable atherosclerotic lesions are required to improve prevention of myocardial infarction and ischemic stroke. Here, a systems-based analysis of atherosclerotic plaques and plasma from patients undergoing carotid endarterectomy for stroke prevention was used to identify molecular signatures with a causal relationship to disease. Local plasma collected in the lesion proximity following clamping prior to arteriotomy was profiled together with matched peripheral plasma. This translational workflow identified biliverdin reductase B as a novel marker of intraplaque hemorrhage and unstable carotid atherosclerosis, which should be investigated as a potential predictive biomarker for cardiovascular events in larger cohorts.
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- 2018
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8. PDGFB, a new candidate plasma biomarker for venous thromboembolism: results from the VEREMA affinity proteomics study.
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Bruzelius M, Iglesias MJ, Hong MG, Sanchez-Rivera L, Gyorgy B, Souto JC, Frånberg M, Fredolini C, Strawbridge RJ, Holmström M, Hamsten A, Uhlén M, Silveira A, Soria JM, Smadja DM, Butler LM, Schwenk JM, Morange PE, Trégouët DA, and Odeberg J
- Subjects
- Biomarkers blood, DNA-Binding Proteins blood, Female, Glutathione Peroxidase blood, Humans, Male, Risk Factors, Transcription Factors blood, von Willebrand Factor metabolism, Proteomics, Proto-Oncogene Proteins c-sis blood, Venous Thromboembolism blood
- Abstract
There is a clear clinical need for high-specificity plasma biomarkers for predicting risk of venous thromboembolism (VTE), but thus far, such markers have remained elusive. Utilizing affinity reagents from the Human Protein Atlas project and multiplexed immuoassays, we extensively analyzed plasma samples from 2 individual studies to identify candidate protein markers associated with VTE risk. We screened plasma samples from 88 VTE cases and 85 matched controls, collected as part of the Swedish "Venous Thromboembolism Biomarker Study," using suspension bead arrays composed of 755 antibodies targeting 408 candidate proteins. We identified significant associations between VTE occurrence and plasma levels of human immunodeficiency virus type I enhancer binding protein 1 (HIVEP1), von Willebrand factor (VWF), glutathione peroxidase 3 (GPX3), and platelet-derived growth factor β (PDGFB). For replication, we profiled plasma samples of 580 cases and 589 controls from the French FARIVE study. These results confirmed the association of VWF and PDGFB with VTE after correction for multiple testing, whereas only weak trends were observed for HIVEP1 and GPX3. Although plasma levels of VWF and PDGFB correlated modestly (ρ ∼ 0.30) with each other, they were independently associated with VTE risk in a joint model in FARIVE (VWF P < .001; PDGFB P = .002). PDGFΒ was verified as the target of the capture antibody by immunocapture mass spectrometry and sandwich enzyme-linked immunosorbent assay. In conclusion, we demonstrate that high-throughput affinity plasma proteomic profiling is a valuable research strategy to identify potential candidate biomarkers for thrombosis-related disorders, and our study suggests a novel association of PDGFB plasma levels with VTE., (© 2016 by The American Society of Hematology.)
- Published
- 2016
- Full Text
- View/download PDF
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