A short synthetic peptide inhibits signal transduction, migration and angiogenesis mediated by Tie2 receptor
Tie2, an endothelial cell‐specific receptor kinase, has an important role in tumour angiogenesis. In an attempt to identify peptides that specifically interact with and block the Tie2 pathway, a phage‐displayed peptide library was screened on a recombinant Tie2 receptor. One peptide, NLLMAAS, comple...
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| Veröffentlicht in: | EMBO reports 2004-03, Vol.5 (3), p.262-267 |
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| creator | Tournaire, Roselyne Simon, Marie-Pierre Noble, Ferdinand le Eichmann, Anne England, Patrick Pouysségur, Jacques |
| description | Tie2, an endothelial cell‐specific receptor kinase, has an important role in tumour angiogenesis. In an attempt to identify peptides that specifically interact with and block the Tie2 pathway, a phage‐displayed peptide library was screened on a recombinant Tie2 receptor. One peptide, NLLMAAS, completely abolished the binding to Tie2 of both angiopoietin 2 and angiopoietin 1 (Ang1). We further show that NLLMAAS specifically suppresses both Ang1‐induced ERK activity and migration in human umbilical endothelial cells. Moreover,
in vivo
, this peptide inhibits angiogenesis in the chick chorioallantoic membrane assay. NLLMAAS is the first peptide described to interact with Tie2. Our results demonstrate that it is an efficient and specific antagonist of the binding of Tie2 ligands, and suggest that this peptide or its derivates may have potential applications in the treatment of angiogenesis diseases. It also represents a potent tool to dissect the molecular mechanisms involved in the Tie2 pathway. |
| doi_str_mv | 10.1038/sj.embor.7400100 |
| format | Article |
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in vivo
, this peptide inhibits angiogenesis in the chick chorioallantoic membrane assay. NLLMAAS is the first peptide described to interact with Tie2. Our results demonstrate that it is an efficient and specific antagonist of the binding of Tie2 ligands, and suggest that this peptide or its derivates may have potential applications in the treatment of angiogenesis diseases. It also represents a potent tool to dissect the molecular mechanisms involved in the Tie2 pathway.</description><identifier>ISSN: 1469-221X</identifier><identifier>EISSN: 1469-3178</identifier><identifier>DOI: 10.1038/sj.embor.7400100</identifier><identifier>PMID: 14978510</identifier><identifier>CODEN: ERMEAX</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>angiogenesis ; angiopoietin ; Angiotensin I ; Angiotensin I - antagonists & inhibitors ; Angiotensin II ; Angiotensin II - antagonists & inhibitors ; Animals ; antagonist peptides ; Binding, Competitive ; Biochemistry, Molecular Biology ; Biological Assay ; Cancer ; Cell Behavior ; Cell Movement ; Cell Movement - drug effects ; Cells, Cultured ; Cellular Biology ; Chick Embryo ; Consensus Sequence ; Endothelial Cells ; Endothelial Cells - metabolism ; Enzyme Inhibitors ; Enzyme Inhibitors - chemistry ; Enzyme Inhibitors - pharmacology ; ERK signalling ; Humans ; Life Sciences ; Mitogen-Activated Protein Kinase Kinases ; Mitogen-Activated Protein Kinase Kinases - metabolism ; Neovascularization, Physiologic ; Neovascularization, Physiologic - drug effects ; Oligopeptides ; Oligopeptides - chemistry ; Oligopeptides - pharmacology ; Peptide Library ; Peptides ; phage display ; Receptor, TIE-2 ; Receptor, TIE-2 - antagonists & inhibitors ; Scientific Report ; Signal Transduction ; Signal Transduction - drug effects ; Subcellular Processes ; Tie2 ; Umbilical Veins ; Umbilical Veins - cytology ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factor A - metabolism</subject><ispartof>EMBO reports, 2004-03, Vol.5 (3), p.262-267</ispartof><rights>European Molecular Biology Organization 2004</rights><rights>Copyright © 2004 European Molecular Biology Organization</rights><rights>Copyright Nature Publishing Group Mar 2004</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>Copyright © 2004, European Molecular Biology Organization 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6730-2e0ad0e535c5bcaa6386b168a9974a5635c6cdadce2ef0a7b1aedde4607ae8673</citedby><cites>FETCH-LOGICAL-c6730-2e0ad0e535c5bcaa6386b168a9974a5635c6cdadce2ef0a7b1aedde4607ae8673</cites><orcidid>0000-0001-6410-5918</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1299011/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1299011/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14978510$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00322392$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Tournaire, Roselyne</creatorcontrib><creatorcontrib>Simon, Marie-Pierre</creatorcontrib><creatorcontrib>Noble, Ferdinand le</creatorcontrib><creatorcontrib>Eichmann, Anne</creatorcontrib><creatorcontrib>England, Patrick</creatorcontrib><creatorcontrib>Pouysségur, Jacques</creatorcontrib><title>A short synthetic peptide inhibits signal transduction, migration and angiogenesis mediated by Tie2 receptor</title><title>EMBO reports</title><addtitle>EMBO Rep</addtitle><addtitle>EMBO Rep</addtitle><description>Tie2, an endothelial cell‐specific receptor kinase, has an important role in tumour angiogenesis. In an attempt to identify peptides that specifically interact with and block the Tie2 pathway, a phage‐displayed peptide library was screened on a recombinant Tie2 receptor. One peptide, NLLMAAS, completely abolished the binding to Tie2 of both angiopoietin 2 and angiopoietin 1 (Ang1). We further show that NLLMAAS specifically suppresses both Ang1‐induced ERK activity and migration in human umbilical endothelial cells. Moreover,
in vivo
, this peptide inhibits angiogenesis in the chick chorioallantoic membrane assay. NLLMAAS is the first peptide described to interact with Tie2. Our results demonstrate that it is an efficient and specific antagonist of the binding of Tie2 ligands, and suggest that this peptide or its derivates may have potential applications in the treatment of angiogenesis diseases. It also represents a potent tool to dissect the molecular mechanisms involved in the Tie2 pathway.</description><subject>angiogenesis</subject><subject>angiopoietin</subject><subject>Angiotensin I</subject><subject>Angiotensin I - antagonists & inhibitors</subject><subject>Angiotensin II</subject><subject>Angiotensin II - antagonists & inhibitors</subject><subject>Animals</subject><subject>antagonist peptides</subject><subject>Binding, Competitive</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biological Assay</subject><subject>Cancer</subject><subject>Cell Behavior</subject><subject>Cell Movement</subject><subject>Cell Movement - drug effects</subject><subject>Cells, Cultured</subject><subject>Cellular Biology</subject><subject>Chick Embryo</subject><subject>Consensus Sequence</subject><subject>Endothelial Cells</subject><subject>Endothelial Cells - metabolism</subject><subject>Enzyme Inhibitors</subject><subject>Enzyme Inhibitors - chemistry</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>ERK signalling</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Mitogen-Activated Protein Kinase Kinases</subject><subject>Mitogen-Activated Protein Kinase Kinases - metabolism</subject><subject>Neovascularization, Physiologic</subject><subject>Neovascularization, Physiologic - drug effects</subject><subject>Oligopeptides</subject><subject>Oligopeptides - chemistry</subject><subject>Oligopeptides - pharmacology</subject><subject>Peptide Library</subject><subject>Peptides</subject><subject>phage display</subject><subject>Receptor, TIE-2</subject><subject>Receptor, TIE-2 - antagonists & inhibitors</subject><subject>Scientific Report</subject><subject>Signal Transduction</subject><subject>Signal Transduction - drug effects</subject><subject>Subcellular Processes</subject><subject>Tie2</subject><subject>Umbilical Veins</subject><subject>Umbilical Veins - cytology</subject><subject>Vascular Endothelial Growth Factor A</subject><subject>Vascular Endothelial Growth Factor A - 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Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>EMBO reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tournaire, Roselyne</au><au>Simon, Marie-Pierre</au><au>Noble, Ferdinand le</au><au>Eichmann, Anne</au><au>England, Patrick</au><au>Pouysségur, Jacques</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A short synthetic peptide inhibits signal transduction, migration and angiogenesis mediated by Tie2 receptor</atitle><jtitle>EMBO reports</jtitle><stitle>EMBO Rep</stitle><addtitle>EMBO Rep</addtitle><date>2004-03</date><risdate>2004</risdate><volume>5</volume><issue>3</issue><spage>262</spage><epage>267</epage><pages>262-267</pages><issn>1469-221X</issn><eissn>1469-3178</eissn><coden>ERMEAX</coden><abstract>Tie2, an endothelial cell‐specific receptor kinase, has an important role in tumour angiogenesis. In an attempt to identify peptides that specifically interact with and block the Tie2 pathway, a phage‐displayed peptide library was screened on a recombinant Tie2 receptor. One peptide, NLLMAAS, completely abolished the binding to Tie2 of both angiopoietin 2 and angiopoietin 1 (Ang1). We further show that NLLMAAS specifically suppresses both Ang1‐induced ERK activity and migration in human umbilical endothelial cells. Moreover,
in vivo
, this peptide inhibits angiogenesis in the chick chorioallantoic membrane assay. NLLMAAS is the first peptide described to interact with Tie2. Our results demonstrate that it is an efficient and specific antagonist of the binding of Tie2 ligands, and suggest that this peptide or its derivates may have potential applications in the treatment of angiogenesis diseases. It also represents a potent tool to dissect the molecular mechanisms involved in the Tie2 pathway.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>14978510</pmid><doi>10.1038/sj.embor.7400100</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0001-6410-5918</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | EMBO reports, 2004-03, Vol.5 (3), p.262-267 |
| issn | 1469-221X 1469-3178 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Free Content; Access via Wiley Online Library; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | angiogenesis angiopoietin Angiotensin I Angiotensin I - antagonists & inhibitors Angiotensin II Angiotensin II - antagonists & inhibitors Animals antagonist peptides Binding, Competitive Biochemistry, Molecular Biology Biological Assay Cancer Cell Behavior Cell Movement Cell Movement - drug effects Cells, Cultured Cellular Biology Chick Embryo Consensus Sequence Endothelial Cells Endothelial Cells - metabolism Enzyme Inhibitors Enzyme Inhibitors - chemistry Enzyme Inhibitors - pharmacology ERK signalling Humans Life Sciences Mitogen-Activated Protein Kinase Kinases Mitogen-Activated Protein Kinase Kinases - metabolism Neovascularization, Physiologic Neovascularization, Physiologic - drug effects Oligopeptides Oligopeptides - chemistry Oligopeptides - pharmacology Peptide Library Peptides phage display Receptor, TIE-2 Receptor, TIE-2 - antagonists & inhibitors Scientific Report Signal Transduction Signal Transduction - drug effects Subcellular Processes Tie2 Umbilical Veins Umbilical Veins - cytology Vascular Endothelial Growth Factor A Vascular Endothelial Growth Factor A - metabolism |
| title | A short synthetic peptide inhibits signal transduction, migration and angiogenesis mediated by Tie2 receptor |
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