All trans-retinoic acid analogs promote cancer cell apoptosis through non-genomic Crabp1 mediating ERK1/2 phosphorylation
All trans retinoic acid (atRA) is one of the most potent therapeutic agents, but extensive toxicity caused by nuclear RA receptors (RARs) limits its clinical application in treating cancer. AtRA also exerts non-genomic activities for which the mechanism remains poorly understood. We determine that c...
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| Veröffentlicht in: | Scientific reports 2016-03, Vol.6 (1), p.22396-22396, Article 22396 |
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| creator | Persaud, Shawna D. Park, Sung Wook Ishigami-Yuasa, Mari Koyano-Nakagawa, Naoko Kagechika, Hiroyuki Wei, Li-Na |
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trans
retinoic acid (atRA) is one of the most potent therapeutic agents, but extensive toxicity caused by nuclear RA receptors (RARs) limits its clinical application in treating cancer. AtRA also exerts non-genomic activities for which the mechanism remains poorly understood. We determine that cellular retinoic acid binding protein 1 (Crabp1) mediates the non-genomic activity of atRA, and identify two compounds as the ligands of Crabp1 to rapidly and RAR-independently activate extracellular signal regulated kinase 1/2 (ERK1/2). Non-canonically activated ERK activates protein phosphatase 2A (PP2A) and lengthens cell cycle duration in embryonic stem cells (ESC). This is abolished in Crabp1-null ESCs. Re-expressing Crabp1 in Crabp1-negative cancer cells also sensitizes their apoptotic induction by atRA. This study reveals a physiological relevance of the non-genomic action of atRA, mediated by Crabp1, in modulating cell cycle progression and apoptosis induction, and provides a new cancer therapeutic strategy whereby compounds specifically targeting Crabp1 can modulate cell cycle and cancer cell apoptosis in a RAR-independent fashion, thereby avoiding atRA’s toxicity caused by its genomic effects. |
| doi_str_mv | 10.1038/srep22396 |
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trans
retinoic acid (atRA) is one of the most potent therapeutic agents, but extensive toxicity caused by nuclear RA receptors (RARs) limits its clinical application in treating cancer. AtRA also exerts non-genomic activities for which the mechanism remains poorly understood. We determine that cellular retinoic acid binding protein 1 (Crabp1) mediates the non-genomic activity of atRA, and identify two compounds as the ligands of Crabp1 to rapidly and RAR-independently activate extracellular signal regulated kinase 1/2 (ERK1/2). Non-canonically activated ERK activates protein phosphatase 2A (PP2A) and lengthens cell cycle duration in embryonic stem cells (ESC). This is abolished in Crabp1-null ESCs. Re-expressing Crabp1 in Crabp1-negative cancer cells also sensitizes their apoptotic induction by atRA. This study reveals a physiological relevance of the non-genomic action of atRA, mediated by Crabp1, in modulating cell cycle progression and apoptosis induction, and provides a new cancer therapeutic strategy whereby compounds specifically targeting Crabp1 can modulate cell cycle and cancer cell apoptosis in a RAR-independent fashion, thereby avoiding atRA’s toxicity caused by its genomic effects.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep22396</identifier><identifier>PMID: 26935534</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/80/86 ; 631/80/86/2363 ; Animals ; Apoptosis ; Apoptosis - drug effects ; Cancer ; Cell cycle ; Cell Line, Tumor ; Cercopithecus aethiops ; COS Cells ; Embryo cells ; Extracellular signal-regulated kinase ; Genomics ; Humanities and Social Sciences ; Kinases ; Mice ; Mitogen-Activated Protein Kinase 3 - genetics ; Mitogen-Activated Protein Kinase 3 - metabolism ; multidisciplinary ; Neoplasm Proteins - genetics ; Neoplasm Proteins - metabolism ; Neoplasms - genetics ; Neoplasms - metabolism ; Neoplasms - pathology ; Phosphoprotein phosphatase ; Phosphorylation ; Phosphorylation - drug effects ; Protein phosphatase ; Receptors, Retinoic Acid - genetics ; Receptors, Retinoic Acid - metabolism ; Retinoic acid ; Retinoic acid receptors ; Science ; Science (multidisciplinary) ; Stem cells ; Toxicity ; Tretinoin - pharmacology</subject><ispartof>Scientific reports, 2016-03, Vol.6 (1), p.22396-22396, Article 22396</ispartof><rights>The Author(s) 2016</rights><rights>Copyright Nature Publishing Group Mar 2016</rights><rights>Copyright © 2016, Macmillan Publishers Limited 2016 Macmillan Publishers Limited</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c504t-25d78701c35f2cd16ac585c94434d3e46008fa2e6c78b98a5f3db6cc164e75413</citedby><cites>FETCH-LOGICAL-c504t-25d78701c35f2cd16ac585c94434d3e46008fa2e6c78b98a5f3db6cc164e75413</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4776112/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4776112/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27923,27924,41119,42188,51575,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26935534$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Persaud, Shawna D.</creatorcontrib><creatorcontrib>Park, Sung Wook</creatorcontrib><creatorcontrib>Ishigami-Yuasa, Mari</creatorcontrib><creatorcontrib>Koyano-Nakagawa, Naoko</creatorcontrib><creatorcontrib>Kagechika, Hiroyuki</creatorcontrib><creatorcontrib>Wei, Li-Na</creatorcontrib><title>All trans-retinoic acid analogs promote cancer cell apoptosis through non-genomic Crabp1 mediating ERK1/2 phosphorylation</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>All
trans
retinoic acid (atRA) is one of the most potent therapeutic agents, but extensive toxicity caused by nuclear RA receptors (RARs) limits its clinical application in treating cancer. AtRA also exerts non-genomic activities for which the mechanism remains poorly understood. We determine that cellular retinoic acid binding protein 1 (Crabp1) mediates the non-genomic activity of atRA, and identify two compounds as the ligands of Crabp1 to rapidly and RAR-independently activate extracellular signal regulated kinase 1/2 (ERK1/2). Non-canonically activated ERK activates protein phosphatase 2A (PP2A) and lengthens cell cycle duration in embryonic stem cells (ESC). This is abolished in Crabp1-null ESCs. Re-expressing Crabp1 in Crabp1-negative cancer cells also sensitizes their apoptotic induction by atRA. This study reveals a physiological relevance of the non-genomic action of atRA, mediated by Crabp1, in modulating cell cycle progression and apoptosis induction, and provides a new cancer therapeutic strategy whereby compounds specifically targeting Crabp1 can modulate cell cycle and cancer cell apoptosis in a RAR-independent fashion, thereby avoiding atRA’s toxicity caused by its genomic effects.</description><subject>631/80/86</subject><subject>631/80/86/2363</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Apoptosis - drug effects</subject><subject>Cancer</subject><subject>Cell cycle</subject><subject>Cell Line, Tumor</subject><subject>Cercopithecus aethiops</subject><subject>COS Cells</subject><subject>Embryo cells</subject><subject>Extracellular signal-regulated kinase</subject><subject>Genomics</subject><subject>Humanities and Social Sciences</subject><subject>Kinases</subject><subject>Mice</subject><subject>Mitogen-Activated Protein Kinase 3 - genetics</subject><subject>Mitogen-Activated Protein Kinase 3 - 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drug effects</topic><topic>Cancer</topic><topic>Cell cycle</topic><topic>Cell Line, Tumor</topic><topic>Cercopithecus aethiops</topic><topic>COS Cells</topic><topic>Embryo cells</topic><topic>Extracellular signal-regulated kinase</topic><topic>Genomics</topic><topic>Humanities and Social Sciences</topic><topic>Kinases</topic><topic>Mice</topic><topic>Mitogen-Activated Protein Kinase 3 - genetics</topic><topic>Mitogen-Activated Protein Kinase 3 - metabolism</topic><topic>multidisciplinary</topic><topic>Neoplasm Proteins - genetics</topic><topic>Neoplasm Proteins - metabolism</topic><topic>Neoplasms - genetics</topic><topic>Neoplasms - metabolism</topic><topic>Neoplasms - pathology</topic><topic>Phosphoprotein phosphatase</topic><topic>Phosphorylation</topic><topic>Phosphorylation - drug effects</topic><topic>Protein phosphatase</topic><topic>Receptors, Retinoic Acid - genetics</topic><topic>Receptors, Retinoic Acid - metabolism</topic><topic>Retinoic acid</topic><topic>Retinoic acid receptors</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Stem cells</topic><topic>Toxicity</topic><topic>Tretinoin - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Persaud, Shawna D.</creatorcontrib><creatorcontrib>Park, Sung Wook</creatorcontrib><creatorcontrib>Ishigami-Yuasa, Mari</creatorcontrib><creatorcontrib>Koyano-Nakagawa, Naoko</creatorcontrib><creatorcontrib>Kagechika, Hiroyuki</creatorcontrib><creatorcontrib>Wei, Li-Na</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection (ProQuest)</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database (ProQuest)</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Persaud, Shawna D.</au><au>Park, Sung Wook</au><au>Ishigami-Yuasa, Mari</au><au>Koyano-Nakagawa, Naoko</au><au>Kagechika, Hiroyuki</au><au>Wei, Li-Na</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>All trans-retinoic acid analogs promote cancer cell apoptosis through non-genomic Crabp1 mediating ERK1/2 phosphorylation</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2016-03-03</date><risdate>2016</risdate><volume>6</volume><issue>1</issue><spage>22396</spage><epage>22396</epage><pages>22396-22396</pages><artnum>22396</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>All
trans
retinoic acid (atRA) is one of the most potent therapeutic agents, but extensive toxicity caused by nuclear RA receptors (RARs) limits its clinical application in treating cancer. AtRA also exerts non-genomic activities for which the mechanism remains poorly understood. We determine that cellular retinoic acid binding protein 1 (Crabp1) mediates the non-genomic activity of atRA, and identify two compounds as the ligands of Crabp1 to rapidly and RAR-independently activate extracellular signal regulated kinase 1/2 (ERK1/2). Non-canonically activated ERK activates protein phosphatase 2A (PP2A) and lengthens cell cycle duration in embryonic stem cells (ESC). This is abolished in Crabp1-null ESCs. Re-expressing Crabp1 in Crabp1-negative cancer cells also sensitizes their apoptotic induction by atRA. This study reveals a physiological relevance of the non-genomic action of atRA, mediated by Crabp1, in modulating cell cycle progression and apoptosis induction, and provides a new cancer therapeutic strategy whereby compounds specifically targeting Crabp1 can modulate cell cycle and cancer cell apoptosis in a RAR-independent fashion, thereby avoiding atRA’s toxicity caused by its genomic effects.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>26935534</pmid><doi>10.1038/srep22396</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/80/86 631/80/86/2363 Animals Apoptosis Apoptosis - drug effects Cancer Cell cycle Cell Line, Tumor Cercopithecus aethiops COS Cells Embryo cells Extracellular signal-regulated kinase Genomics Humanities and Social Sciences Kinases Mice Mitogen-Activated Protein Kinase 3 - genetics Mitogen-Activated Protein Kinase 3 - metabolism multidisciplinary Neoplasm Proteins - genetics Neoplasm Proteins - metabolism Neoplasms - genetics Neoplasms - metabolism Neoplasms - pathology Phosphoprotein phosphatase Phosphorylation Phosphorylation - drug effects Protein phosphatase Receptors, Retinoic Acid - genetics Receptors, Retinoic Acid - metabolism Retinoic acid Retinoic acid receptors Science Science (multidisciplinary) Stem cells Toxicity Tretinoin - pharmacology |
| title | All trans-retinoic acid analogs promote cancer cell apoptosis through non-genomic Crabp1 mediating ERK1/2 phosphorylation |
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