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Phosphoproteomic Analysis and Protein–Protein Interaction of Rat Aorta GJA1 and Rat Heart FKBP1A after Secoiridoid Consumption from Virgin Olive Oil: A Functional Proteomic Approach
Protein functional interactions could explain the biological response of secoiridoids (SECs), main phenolic compounds in virgin olive oil (VOO). The aim was to assess protein–protein interactions (PPIs) of the aorta gap junction alpha-1 (GJA1) and the heart peptidyl-prolyl cis-trans isomerase (FKBP1...
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Published in: | Journal of agricultural and food chemistry 2021-02, Vol.69 (5), p.1536-1554 |
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container_title | Journal of agricultural and food chemistry |
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creator | Pedret, Anna Catalán, Úrsula Rubió, Laura Baiges, Isabel Herrero, Pol Piñol, Carme Rodríguez-Calvo, Ricardo Canela, Núria Fernández-Castillejo, Sara Motilva, Maria-Jose Solà, Rosa |
description | Protein functional interactions could explain the biological response of secoiridoids (SECs), main phenolic compounds in virgin olive oil (VOO). The aim was to assess protein–protein interactions (PPIs) of the aorta gap junction alpha-1 (GJA1) and the heart peptidyl-prolyl cis-trans isomerase (FKBP1A), plus the phosphorylated heart proteome, to describe new molecular pathways in the cardiovascular system in rats using nanoliquid chromatography coupled with mass spectrometry. PPIs modified by SECs and associated with GJA1 in aorta rat tissue were calpain, TUBA1A, and HSPB1. Those associated with FKBP1A in rat heart tissue included SUCLG1, HSPE1, and TNNI3. In the heart, SECs modulated the phosphoproteome through the main canonical pathways PI3K/mTOR signaling (AKT1S1 and GAB2) and gap junction signaling (GAB2 and GJA1). PPIs associated with GJA1 and with FKBP1A, the phosphorylation of GAB2, and the dephosphorylation of GJA1 and AKT1S1 in rat tissues are promising protein targets promoting cardiovascular protection to explain the health benefits of VOO. |
doi_str_mv | 10.1021/acs.jafc.0c07164 |
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The aim was to assess protein–protein interactions (PPIs) of the aorta gap junction alpha-1 (GJA1) and the heart peptidyl-prolyl cis-trans isomerase (FKBP1A), plus the phosphorylated heart proteome, to describe new molecular pathways in the cardiovascular system in rats using nanoliquid chromatography coupled with mass spectrometry. PPIs modified by SECs and associated with GJA1 in aorta rat tissue were calpain, TUBA1A, and HSPB1. Those associated with FKBP1A in rat heart tissue included SUCLG1, HSPE1, and TNNI3. In the heart, SECs modulated the phosphoproteome through the main canonical pathways PI3K/mTOR signaling (AKT1S1 and GAB2) and gap junction signaling (GAB2 and GJA1). PPIs associated with GJA1 and with FKBP1A, the phosphorylation of GAB2, and the dephosphorylation of GJA1 and AKT1S1 in rat tissues are promising protein targets promoting cardiovascular protection to explain the health benefits of VOO.</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/acs.jafc.0c07164</identifier><identifier>PMID: 33502189</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Adaptor Proteins, Signal Transducing - genetics ; Adaptor Proteins, Signal Transducing - metabolism ; Animals ; Aorta - metabolism ; Bioactive Constituents, Metabolites, and Functions ; Connexin 43 - genetics ; Connexin 43 - metabolism ; Iridoids - metabolism ; Male ; Myocardium - metabolism ; Olive Oil - metabolism ; Phosphoproteins - genetics ; Phosphoproteins - metabolism ; Protein Binding ; Proteomics ; Rats ; Rats, Wistar ; TOR Serine-Threonine Kinases - genetics ; TOR Serine-Threonine Kinases - metabolism</subject><ispartof>Journal of agricultural and food chemistry, 2021-02, Vol.69 (5), p.1536-1554</ispartof><rights>2021 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a336t-118d4bc105f3cdc2b4edfac29dafeee22e565d2c192827c7bf72bd17488a8aa33</citedby><cites>FETCH-LOGICAL-a336t-118d4bc105f3cdc2b4edfac29dafeee22e565d2c192827c7bf72bd17488a8aa33</cites><orcidid>0000-0001-8884-9823 ; 0000-0002-8109-9713 ; 0000-0003-0261-2396 ; 0000-0002-5327-932X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33502189$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pedret, Anna</creatorcontrib><creatorcontrib>Catalán, Úrsula</creatorcontrib><creatorcontrib>Rubió, Laura</creatorcontrib><creatorcontrib>Baiges, Isabel</creatorcontrib><creatorcontrib>Herrero, Pol</creatorcontrib><creatorcontrib>Piñol, Carme</creatorcontrib><creatorcontrib>Rodríguez-Calvo, Ricardo</creatorcontrib><creatorcontrib>Canela, Núria</creatorcontrib><creatorcontrib>Fernández-Castillejo, Sara</creatorcontrib><creatorcontrib>Motilva, Maria-Jose</creatorcontrib><creatorcontrib>Solà, Rosa</creatorcontrib><title>Phosphoproteomic Analysis and Protein–Protein Interaction of Rat Aorta GJA1 and Rat Heart FKBP1A after Secoiridoid Consumption from Virgin Olive Oil: A Functional Proteomic Approach</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>Protein functional interactions could explain the biological response of secoiridoids (SECs), main phenolic compounds in virgin olive oil (VOO). The aim was to assess protein–protein interactions (PPIs) of the aorta gap junction alpha-1 (GJA1) and the heart peptidyl-prolyl cis-trans isomerase (FKBP1A), plus the phosphorylated heart proteome, to describe new molecular pathways in the cardiovascular system in rats using nanoliquid chromatography coupled with mass spectrometry. PPIs modified by SECs and associated with GJA1 in aorta rat tissue were calpain, TUBA1A, and HSPB1. Those associated with FKBP1A in rat heart tissue included SUCLG1, HSPE1, and TNNI3. In the heart, SECs modulated the phosphoproteome through the main canonical pathways PI3K/mTOR signaling (AKT1S1 and GAB2) and gap junction signaling (GAB2 and GJA1). PPIs associated with GJA1 and with FKBP1A, the phosphorylation of GAB2, and the dephosphorylation of GJA1 and AKT1S1 in rat tissues are promising protein targets promoting cardiovascular protection to explain the health benefits of VOO.</description><subject>Adaptor Proteins, Signal Transducing - genetics</subject><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Animals</subject><subject>Aorta - metabolism</subject><subject>Bioactive Constituents, Metabolites, and Functions</subject><subject>Connexin 43 - genetics</subject><subject>Connexin 43 - metabolism</subject><subject>Iridoids - metabolism</subject><subject>Male</subject><subject>Myocardium - metabolism</subject><subject>Olive Oil - metabolism</subject><subject>Phosphoproteins - genetics</subject><subject>Phosphoproteins - metabolism</subject><subject>Protein Binding</subject><subject>Proteomics</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>TOR Serine-Threonine Kinases - genetics</subject><subject>TOR Serine-Threonine Kinases - metabolism</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNp1Uclu2zAUJIoEjZP2nlPAYw6VQ1IbnZtq1FkBG92uwhOXmIEkKqRUwLf8Qz-m_5MvCW05ufVE4r2ZeYMZhE4pmVLC6AUIP30ELaZEkJxmyQc0oSkjUUopP0ATEjARTzN6hI69fySE8DQnH9FRHKdhxWcT9G-1tr5b287ZXtnGCFy0UG-88RhaiVfbsWlfnv_uf_im7ZUD0RvbYqvxd-hxYV0P-Oq2oDvOdnStwPV4cfd1RQsMOlDwDyWscUZaI_Hctn5oup2IdrbBv417COLL2vxReGnqS1zgxdDuzkA92hjddcEpiPUndKih9urz_j1Bvxbffs6vo_vl1c28uI8gjrM-CjnIpBKUpDoWUrAqUVKDYDMJWinFmEqzVDJBZ4yzXOSVzlklaZ5wDhyCxgk6H3XD2adB-b5sjBeqrqFVdvAlSzjNeBzCD1AyQoWz3july86ZBtympKTc1lWGusptXeW-rkA526sPVaPkO-GtnwD4MgJ2VDu4kIb_v94r4e-lAA</recordid><startdate>20210210</startdate><enddate>20210210</enddate><creator>Pedret, Anna</creator><creator>Catalán, Úrsula</creator><creator>Rubió, Laura</creator><creator>Baiges, Isabel</creator><creator>Herrero, Pol</creator><creator>Piñol, Carme</creator><creator>Rodríguez-Calvo, Ricardo</creator><creator>Canela, Núria</creator><creator>Fernández-Castillejo, Sara</creator><creator>Motilva, Maria-Jose</creator><creator>Solà, Rosa</creator><general>American Chemical Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-8884-9823</orcidid><orcidid>https://orcid.org/0000-0002-8109-9713</orcidid><orcidid>https://orcid.org/0000-0003-0261-2396</orcidid><orcidid>https://orcid.org/0000-0002-5327-932X</orcidid></search><sort><creationdate>20210210</creationdate><title>Phosphoproteomic Analysis and Protein–Protein Interaction of Rat Aorta GJA1 and Rat Heart FKBP1A after Secoiridoid Consumption from Virgin Olive Oil: A Functional Proteomic Approach</title><author>Pedret, Anna ; Catalán, Úrsula ; Rubió, Laura ; Baiges, Isabel ; Herrero, Pol ; Piñol, Carme ; Rodríguez-Calvo, Ricardo ; Canela, Núria ; Fernández-Castillejo, Sara ; Motilva, Maria-Jose ; Solà, Rosa</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a336t-118d4bc105f3cdc2b4edfac29dafeee22e565d2c192827c7bf72bd17488a8aa33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Adaptor Proteins, Signal Transducing - genetics</topic><topic>Adaptor Proteins, Signal Transducing - metabolism</topic><topic>Animals</topic><topic>Aorta - metabolism</topic><topic>Bioactive Constituents, Metabolites, and Functions</topic><topic>Connexin 43 - genetics</topic><topic>Connexin 43 - metabolism</topic><topic>Iridoids - metabolism</topic><topic>Male</topic><topic>Myocardium - metabolism</topic><topic>Olive Oil - metabolism</topic><topic>Phosphoproteins - genetics</topic><topic>Phosphoproteins - metabolism</topic><topic>Protein Binding</topic><topic>Proteomics</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>TOR Serine-Threonine Kinases - genetics</topic><topic>TOR Serine-Threonine Kinases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pedret, Anna</creatorcontrib><creatorcontrib>Catalán, Úrsula</creatorcontrib><creatorcontrib>Rubió, Laura</creatorcontrib><creatorcontrib>Baiges, Isabel</creatorcontrib><creatorcontrib>Herrero, Pol</creatorcontrib><creatorcontrib>Piñol, Carme</creatorcontrib><creatorcontrib>Rodríguez-Calvo, Ricardo</creatorcontrib><creatorcontrib>Canela, Núria</creatorcontrib><creatorcontrib>Fernández-Castillejo, Sara</creatorcontrib><creatorcontrib>Motilva, Maria-Jose</creatorcontrib><creatorcontrib>Solà, Rosa</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pedret, Anna</au><au>Catalán, Úrsula</au><au>Rubió, Laura</au><au>Baiges, Isabel</au><au>Herrero, Pol</au><au>Piñol, Carme</au><au>Rodríguez-Calvo, Ricardo</au><au>Canela, Núria</au><au>Fernández-Castillejo, Sara</au><au>Motilva, Maria-Jose</au><au>Solà, Rosa</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphoproteomic Analysis and Protein–Protein Interaction of Rat Aorta GJA1 and Rat Heart FKBP1A after Secoiridoid Consumption from Virgin Olive Oil: A Functional Proteomic Approach</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2021-02-10</date><risdate>2021</risdate><volume>69</volume><issue>5</issue><spage>1536</spage><epage>1554</epage><pages>1536-1554</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><abstract>Protein functional interactions could explain the biological response of secoiridoids (SECs), main phenolic compounds in virgin olive oil (VOO). The aim was to assess protein–protein interactions (PPIs) of the aorta gap junction alpha-1 (GJA1) and the heart peptidyl-prolyl cis-trans isomerase (FKBP1A), plus the phosphorylated heart proteome, to describe new molecular pathways in the cardiovascular system in rats using nanoliquid chromatography coupled with mass spectrometry. PPIs modified by SECs and associated with GJA1 in aorta rat tissue were calpain, TUBA1A, and HSPB1. Those associated with FKBP1A in rat heart tissue included SUCLG1, HSPE1, and TNNI3. In the heart, SECs modulated the phosphoproteome through the main canonical pathways PI3K/mTOR signaling (AKT1S1 and GAB2) and gap junction signaling (GAB2 and GJA1). PPIs associated with GJA1 and with FKBP1A, the phosphorylation of GAB2, and the dephosphorylation of GJA1 and AKT1S1 in rat tissues are promising protein targets promoting cardiovascular protection to explain the health benefits of VOO.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>33502189</pmid><doi>10.1021/acs.jafc.0c07164</doi><tpages>19</tpages><orcidid>https://orcid.org/0000-0001-8884-9823</orcidid><orcidid>https://orcid.org/0000-0002-8109-9713</orcidid><orcidid>https://orcid.org/0000-0003-0261-2396</orcidid><orcidid>https://orcid.org/0000-0002-5327-932X</orcidid></addata></record> |
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subjects | Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Signal Transducing - metabolism Animals Aorta - metabolism Bioactive Constituents, Metabolites, and Functions Connexin 43 - genetics Connexin 43 - metabolism Iridoids - metabolism Male Myocardium - metabolism Olive Oil - metabolism Phosphoproteins - genetics Phosphoproteins - metabolism Protein Binding Proteomics Rats Rats, Wistar TOR Serine-Threonine Kinases - genetics TOR Serine-Threonine Kinases - metabolism |
title | Phosphoproteomic Analysis and Protein–Protein Interaction of Rat Aorta GJA1 and Rat Heart FKBP1A after Secoiridoid Consumption from Virgin Olive Oil: A Functional Proteomic Approach |
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