Modifications in rat plasma proteome after remote ischemic preconditioning (RIPC) stimulus: identification by a SELDI-TOF-MS approach
Remote ischemic preconditioning's (RIPC) ability to render the myocardium resistant to subsequent prolonged ischemia is now clearly established in different species, including humans. Strong evidence suggests that circulating humoral mediators play a key role in signal transduction, but their i...
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description | Remote ischemic preconditioning's (RIPC) ability to render the myocardium resistant to subsequent prolonged ischemia is now clearly established in different species, including humans. Strong evidence suggests that circulating humoral mediators play a key role in signal transduction, but their identities still need to be established. Our study sought to identify potential circulating RIPC mediators using a proteomic approach. Rats were exposed to 10-min limb ischemia followed by 5- (RIPC 5') or 10-min (RIPC 10') reperfusion prior to blood sampling. The control group only underwent blood sampling. Plasma samples were isolated for proteomic analysis using surface-enhanced laser desorption and ionization - time of flight - mass spectrometry (SELDI-TOF-MS). A total of seven proteins, including haptoglobin and transthyretin, were detected as up- or down-regulated in response to RIPC. These proteins had previously been identified as associated with organ protection, anti-inflammation, and various cellular and molecular responses to ischemia. In conclusion, this study indicates that RIPC results in significant modulations of plasma proteome. |
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Strong evidence suggests that circulating humoral mediators play a key role in signal transduction, but their identities still need to be established. Our study sought to identify potential circulating RIPC mediators using a proteomic approach. Rats were exposed to 10-min limb ischemia followed by 5- (RIPC 5') or 10-min (RIPC 10') reperfusion prior to blood sampling. The control group only underwent blood sampling. Plasma samples were isolated for proteomic analysis using surface-enhanced laser desorption and ionization - time of flight - mass spectrometry (SELDI-TOF-MS). A total of seven proteins, including haptoglobin and transthyretin, were detected as up- or down-regulated in response to RIPC. These proteins had previously been identified as associated with organ protection, anti-inflammation, and various cellular and molecular responses to ischemia. In conclusion, this study indicates that RIPC results in significant modulations of plasma proteome.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0085669</identifier><identifier>PMID: 24454915</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Sequence ; Animals ; Apolipoproteins ; Atherosclerosis ; Biology ; Blood ; Blood tests ; Cardiology and cardiovascular system ; Cardiovascular disease ; Cell adhesion & migration ; Cellular signal transduction ; Chromatography ; Haptoglobin ; Heart ; Human health and pathology ; Ionization ; Ischemia ; Ischemic Preconditioning ; Laboratory animals ; Life Sciences ; Male ; Mass spectrometry ; Mass spectroscopy ; Medicine ; Molecular Sequence Data ; Myocardium ; Peptides ; Plasma - metabolism ; Preconditioning ; Proteins ; Proteome - metabolism ; Rats ; Rats, Wistar ; Reperfusion ; Rodents ; Sampling ; Scientific imaging ; Signal transduction ; Skin ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods ; Studies ; Surgery ; Transduction ; Transthyretin</subject><ispartof>PloS one, 2014-01, Vol.9 (1), p.e85669-e85669</ispartof><rights>COPYRIGHT 2014 Public Library of Science</rights><rights>2014 Hibert et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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Strong evidence suggests that circulating humoral mediators play a key role in signal transduction, but their identities still need to be established. Our study sought to identify potential circulating RIPC mediators using a proteomic approach. Rats were exposed to 10-min limb ischemia followed by 5- (RIPC 5') or 10-min (RIPC 10') reperfusion prior to blood sampling. The control group only underwent blood sampling. Plasma samples were isolated for proteomic analysis using surface-enhanced laser desorption and ionization - time of flight - mass spectrometry (SELDI-TOF-MS). A total of seven proteins, including haptoglobin and transthyretin, were detected as up- or down-regulated in response to RIPC. These proteins had previously been identified as associated with organ protection, anti-inflammation, and various cellular and molecular responses to ischemia. In conclusion, this study indicates that RIPC results in significant modulations of plasma proteome.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Apolipoproteins</subject><subject>Atherosclerosis</subject><subject>Biology</subject><subject>Blood</subject><subject>Blood tests</subject><subject>Cardiology and cardiovascular system</subject><subject>Cardiovascular disease</subject><subject>Cell adhesion & migration</subject><subject>Cellular signal transduction</subject><subject>Chromatography</subject><subject>Haptoglobin</subject><subject>Heart</subject><subject>Human health and pathology</subject><subject>Ionization</subject><subject>Ischemia</subject><subject>Ischemic Preconditioning</subject><subject>Laboratory animals</subject><subject>Life Sciences</subject><subject>Male</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Medicine</subject><subject>Molecular Sequence 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in rat plasma proteome after remote ischemic preconditioning (RIPC) stimulus: identification by a SELDI-TOF-MS approach</title><author>Hibert, Pierre ; Prunier-Mirebeau, Delphine ; Beseme, Olivia ; Chwastyniak, Maggy ; Tamareille, Sophie ; Pinet, Florence ; Prunier, Fabrice</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c627t-474ed752fa470c97d4dbd196c5fada48045997d743634845d90a39c4b31866573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Apolipoproteins</topic><topic>Atherosclerosis</topic><topic>Biology</topic><topic>Blood</topic><topic>Blood tests</topic><topic>Cardiology and cardiovascular system</topic><topic>Cardiovascular disease</topic><topic>Cell adhesion & migration</topic><topic>Cellular signal transduction</topic><topic>Chromatography</topic><topic>Haptoglobin</topic><topic>Heart</topic><topic>Human 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in different species, including humans. Strong evidence suggests that circulating humoral mediators play a key role in signal transduction, but their identities still need to be established. Our study sought to identify potential circulating RIPC mediators using a proteomic approach. Rats were exposed to 10-min limb ischemia followed by 5- (RIPC 5') or 10-min (RIPC 10') reperfusion prior to blood sampling. The control group only underwent blood sampling. Plasma samples were isolated for proteomic analysis using surface-enhanced laser desorption and ionization - time of flight - mass spectrometry (SELDI-TOF-MS). A total of seven proteins, including haptoglobin and transthyretin, were detected as up- or down-regulated in response to RIPC. These proteins had previously been identified as associated with organ protection, anti-inflammation, and various cellular and molecular responses to ischemia. 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subjects | Amino Acid Sequence Animals Apolipoproteins Atherosclerosis Biology Blood Blood tests Cardiology and cardiovascular system Cardiovascular disease Cell adhesion & migration Cellular signal transduction Chromatography Haptoglobin Heart Human health and pathology Ionization Ischemia Ischemic Preconditioning Laboratory animals Life Sciences Male Mass spectrometry Mass spectroscopy Medicine Molecular Sequence Data Myocardium Peptides Plasma - metabolism Preconditioning Proteins Proteome - metabolism Rats Rats, Wistar Reperfusion Rodents Sampling Scientific imaging Signal transduction Skin Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods Studies Surgery Transduction Transthyretin |
title | Modifications in rat plasma proteome after remote ischemic preconditioning (RIPC) stimulus: identification by a SELDI-TOF-MS approach |
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