Inhibition of tumor growth by systemic treatment with thrombospondin‐1 peptide mimetics
Many normal human cells produce thrombospondin‐1 (TSP‐1), a potent antiangiogenic protein that promotes vascular quiescence. In various organ systems, including the brain, breast and bladder and in fibroblasts, TSP‐1 secretion is reduced during tumorigenesis, thereby allowing induction of the vigoro...
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container_title | International journal of cancer |
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description | Many normal human cells produce thrombospondin‐1 (TSP‐1), a potent antiangiogenic protein that promotes vascular quiescence. In various organ systems, including the brain, breast and bladder and in fibroblasts, TSP‐1 secretion is reduced during tumorigenesis, thereby allowing induction of the vigorous neovascularization required for tumor growth and metastasis. Full‐length and short TSP‐1–derived peptides inhibit angiogenesis by inducing endothelial cell apoptosis and thus disrupting the vasculature of the growing tumor. CD36 expressed on the surface of endothelial cells functions as the primary antiangiogenic receptor for TSP‐1. A D‐isoleucyl enantiomer of a TSP‐1 heptapeptide specifically inhibits the proliferation and migration of capillary endothelial cells. DI‐TSP, an approximately 1 kDa capped version of this peptide, is also antiangiogenic in vitro, with a specific activity approaching that of the 450 kDa parental molecule. Here, we show that DI‐TSP delivered systemically dose‐dependently inhibits the growth of murine melanoma metastases in syngeneic animals and that its more soluble isomer, DI‐TSPa, similarly blocks the progression of primary human bladder tumors in an orthotopic model in immune‐deficient mice. Like intact TSP‐1, these peptide mimetics had no effect on cancer cells growing in vitro but markedly suppressed the growth of endothelial cells by inducing receptor‐dependent apoptosis. Antibodies raised against CD36 blocked the ability of peptides to induce apoptosis in endothelial cells but had no effect on tumor necrosis factor‐α–induced apoptosis. In vivo, the peptide mimetics were associated with a significantly reduced microvessel density and increased apoptotic indices in both the endothelial and tumor cell compartments. Such short peptides targeted to a specific antiangiogenic receptor, potent and easy to synthesize, show great promise as lead compounds in clinical antiangiogenic strategies. © 2002 Wiley‐Liss, Inc. |
doi_str_mv | 10.1002/ijc.10247 |
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In various organ systems, including the brain, breast and bladder and in fibroblasts, TSP‐1 secretion is reduced during tumorigenesis, thereby allowing induction of the vigorous neovascularization required for tumor growth and metastasis. Full‐length and short TSP‐1–derived peptides inhibit angiogenesis by inducing endothelial cell apoptosis and thus disrupting the vasculature of the growing tumor. CD36 expressed on the surface of endothelial cells functions as the primary antiangiogenic receptor for TSP‐1. A D‐isoleucyl enantiomer of a TSP‐1 heptapeptide specifically inhibits the proliferation and migration of capillary endothelial cells. DI‐TSP, an approximately 1 kDa capped version of this peptide, is also antiangiogenic in vitro, with a specific activity approaching that of the 450 kDa parental molecule. Here, we show that DI‐TSP delivered systemically dose‐dependently inhibits the growth of murine melanoma metastases in syngeneic animals and that its more soluble isomer, DI‐TSPa, similarly blocks the progression of primary human bladder tumors in an orthotopic model in immune‐deficient mice. Like intact TSP‐1, these peptide mimetics had no effect on cancer cells growing in vitro but markedly suppressed the growth of endothelial cells by inducing receptor‐dependent apoptosis. Antibodies raised against CD36 blocked the ability of peptides to induce apoptosis in endothelial cells but had no effect on tumor necrosis factor‐α–induced apoptosis. In vivo, the peptide mimetics were associated with a significantly reduced microvessel density and increased apoptotic indices in both the endothelial and tumor cell compartments. Such short peptides targeted to a specific antiangiogenic receptor, potent and easy to synthesize, show great promise as lead compounds in clinical antiangiogenic strategies. © 2002 Wiley‐Liss, Inc.</description><identifier>ISSN: 0020-7136</identifier><identifier>EISSN: 1097-0215</identifier><identifier>DOI: 10.1002/ijc.10247</identifier><identifier>PMID: 11920636</identifier><identifier>CODEN: IJCNAW</identifier><language>eng</language><publisher>New York: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Animals ; Antineoplastic agents ; Apoptosis - drug effects ; Biological and medical sciences ; bladder cancer ; CD36 Antigens - metabolism ; Cell Division - drug effects ; Cell Division - physiology ; Chemotherapy ; Dose-Response Relationship, Drug ; Endothelium, Vascular - drug effects ; Endothelium, Vascular - pathology ; Humans ; In Situ Nick-End Labeling ; Lung Neoplasms - blood supply ; Lung Neoplasms - metabolism ; Lung Neoplasms - prevention & control ; Male ; Medical sciences ; melanoma ; Melanoma, Experimental - drug therapy ; Melanoma, Experimental - pathology ; Mice ; Mice, Inbred C57BL ; Mice, Nude ; Molecular Mimicry ; Neovascularization, Pathologic - drug therapy ; Neovascularization, Pathologic - metabolism ; Peptide Fragments - therapeutic use ; peptide mimetics ; Pharmacology. Drug treatments ; Platelet Endothelial Cell Adhesion Molecule-1 - metabolism ; Proliferating Cell Nuclear Antigen - metabolism ; Thrombospondin 1 - therapeutic use ; thrombospondin‐1 ; tumor angiogenesis ; Urinary Bladder Neoplasms - blood supply ; Urinary Bladder Neoplasms - metabolism ; Urinary Bladder Neoplasms - prevention & control</subject><ispartof>International journal of cancer, 2002-04, Vol.98 (5), p.682-689</ispartof><rights>Copyright © 2002 Wiley‐Liss, Inc.</rights><rights>2002 INIST-CNRS</rights><rights>Copyright 2002 Wiley-Liss, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3517-feb117a7f59f3c2caff385b5a7b67c2f2c5390e474957c6320cc8e909058ef463</citedby><cites>FETCH-LOGICAL-c3517-feb117a7f59f3c2caff385b5a7b67c2f2c5390e474957c6320cc8e909058ef463</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fijc.10247$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fijc.10247$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,782,786,1419,27931,27932,45581,45582</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13587351$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11920636$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Reiher, Frank K.</creatorcontrib><creatorcontrib>Volpert, Olga V.</creatorcontrib><creatorcontrib>Jimenez, Benilde</creatorcontrib><creatorcontrib>Crawford, Susan E.</creatorcontrib><creatorcontrib>Dinney, Colin P.</creatorcontrib><creatorcontrib>Henkin, Jack</creatorcontrib><creatorcontrib>Haviv, Fortuna</creatorcontrib><creatorcontrib>Bouck, Noel P.</creatorcontrib><creatorcontrib>Campbell, Steven C.</creatorcontrib><title>Inhibition of tumor growth by systemic treatment with thrombospondin‐1 peptide mimetics</title><title>International journal of cancer</title><addtitle>Int J Cancer</addtitle><description>Many normal human cells produce thrombospondin‐1 (TSP‐1), a potent antiangiogenic protein that promotes vascular quiescence. In various organ systems, including the brain, breast and bladder and in fibroblasts, TSP‐1 secretion is reduced during tumorigenesis, thereby allowing induction of the vigorous neovascularization required for tumor growth and metastasis. Full‐length and short TSP‐1–derived peptides inhibit angiogenesis by inducing endothelial cell apoptosis and thus disrupting the vasculature of the growing tumor. CD36 expressed on the surface of endothelial cells functions as the primary antiangiogenic receptor for TSP‐1. A D‐isoleucyl enantiomer of a TSP‐1 heptapeptide specifically inhibits the proliferation and migration of capillary endothelial cells. DI‐TSP, an approximately 1 kDa capped version of this peptide, is also antiangiogenic in vitro, with a specific activity approaching that of the 450 kDa parental molecule. Here, we show that DI‐TSP delivered systemically dose‐dependently inhibits the growth of murine melanoma metastases in syngeneic animals and that its more soluble isomer, DI‐TSPa, similarly blocks the progression of primary human bladder tumors in an orthotopic model in immune‐deficient mice. Like intact TSP‐1, these peptide mimetics had no effect on cancer cells growing in vitro but markedly suppressed the growth of endothelial cells by inducing receptor‐dependent apoptosis. Antibodies raised against CD36 blocked the ability of peptides to induce apoptosis in endothelial cells but had no effect on tumor necrosis factor‐α–induced apoptosis. In vivo, the peptide mimetics were associated with a significantly reduced microvessel density and increased apoptotic indices in both the endothelial and tumor cell compartments. Such short peptides targeted to a specific antiangiogenic receptor, potent and easy to synthesize, show great promise as lead compounds in clinical antiangiogenic strategies. © 2002 Wiley‐Liss, Inc.</description><subject>Animals</subject><subject>Antineoplastic agents</subject><subject>Apoptosis - drug effects</subject><subject>Biological and medical sciences</subject><subject>bladder cancer</subject><subject>CD36 Antigens - metabolism</subject><subject>Cell Division - drug effects</subject><subject>Cell Division - physiology</subject><subject>Chemotherapy</subject><subject>Dose-Response Relationship, Drug</subject><subject>Endothelium, Vascular - drug effects</subject><subject>Endothelium, Vascular - pathology</subject><subject>Humans</subject><subject>In Situ Nick-End Labeling</subject><subject>Lung Neoplasms - blood supply</subject><subject>Lung Neoplasms - metabolism</subject><subject>Lung Neoplasms - prevention & control</subject><subject>Male</subject><subject>Medical sciences</subject><subject>melanoma</subject><subject>Melanoma, Experimental - drug therapy</subject><subject>Melanoma, Experimental - pathology</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Mice, Nude</subject><subject>Molecular Mimicry</subject><subject>Neovascularization, Pathologic - drug therapy</subject><subject>Neovascularization, Pathologic - metabolism</subject><subject>Peptide Fragments - therapeutic use</subject><subject>peptide mimetics</subject><subject>Pharmacology. Drug treatments</subject><subject>Platelet Endothelial Cell Adhesion Molecule-1 - metabolism</subject><subject>Proliferating Cell Nuclear Antigen - metabolism</subject><subject>Thrombospondin 1 - therapeutic use</subject><subject>thrombospondin‐1</subject><subject>tumor angiogenesis</subject><subject>Urinary Bladder Neoplasms - blood supply</subject><subject>Urinary Bladder Neoplasms - metabolism</subject><subject>Urinary Bladder Neoplasms - prevention & control</subject><issn>0020-7136</issn><issn>1097-0215</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp10L1OwzAQB3ALgaB8DLwA8gISQ8CO4zgZUcVHERILDEyR456pqzgOtquqG4_AM_IkGFqpE9OddD_d6f4InVJyRQnJr81cpSYvxA4aUVKLjOSU76JRmpFMUFYeoMMQ5oRQykmxjw4orXNSsnKE3ib9zLQmGtdjp3FcWOfxu3fLOMPtCodViGCNwtGDjBb6iJcmjeLMO9u6MLh-avrvzy-KBxiimQK2xkI0KhyjPS27ACebeoRe725fxg_Z0_P9ZHzzlCnGqcg0tJQKKTSvNVO5klqzirdcirYUKte54qwmUIii5kKVLCdKVVCTmvAKdFGyI3Sx3jt497GAEBtrgoKukz24RWgE5bxmtErwcg2VdyF40M3gjZV-1VDS_ObYpBybvxyTPdssXbQWplu5CS6B8w2QQclOe9krE7aO8Uqk_5K7Xrul6WD1_8Vm8jhen_4BsCyLJA</recordid><startdate>20020410</startdate><enddate>20020410</enddate><creator>Reiher, Frank K.</creator><creator>Volpert, Olga V.</creator><creator>Jimenez, Benilde</creator><creator>Crawford, Susan E.</creator><creator>Dinney, Colin P.</creator><creator>Henkin, Jack</creator><creator>Haviv, Fortuna</creator><creator>Bouck, Noel P.</creator><creator>Campbell, Steven C.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley-Liss</general><scope>IQODW</scope><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></search><sort><creationdate>20020410</creationdate><title>Inhibition of tumor growth by systemic treatment with thrombospondin‐1 peptide mimetics</title><author>Reiher, Frank K. ; Volpert, Olga V. ; Jimenez, Benilde ; Crawford, Susan E. ; Dinney, Colin P. ; Henkin, Jack ; Haviv, Fortuna ; Bouck, Noel P. ; Campbell, Steven C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3517-feb117a7f59f3c2caff385b5a7b67c2f2c5390e474957c6320cc8e909058ef463</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animals</topic><topic>Antineoplastic agents</topic><topic>Apoptosis - drug effects</topic><topic>Biological and medical sciences</topic><topic>bladder cancer</topic><topic>CD36 Antigens - metabolism</topic><topic>Cell Division - drug effects</topic><topic>Cell Division - physiology</topic><topic>Chemotherapy</topic><topic>Dose-Response Relationship, Drug</topic><topic>Endothelium, Vascular - drug effects</topic><topic>Endothelium, Vascular - pathology</topic><topic>Humans</topic><topic>In Situ Nick-End Labeling</topic><topic>Lung Neoplasms - blood supply</topic><topic>Lung Neoplasms - metabolism</topic><topic>Lung Neoplasms - prevention & control</topic><topic>Male</topic><topic>Medical sciences</topic><topic>melanoma</topic><topic>Melanoma, Experimental - drug therapy</topic><topic>Melanoma, Experimental - pathology</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Mice, Nude</topic><topic>Molecular Mimicry</topic><topic>Neovascularization, Pathologic - drug therapy</topic><topic>Neovascularization, Pathologic - metabolism</topic><topic>Peptide Fragments - therapeutic use</topic><topic>peptide mimetics</topic><topic>Pharmacology. Drug treatments</topic><topic>Platelet Endothelial Cell Adhesion Molecule-1 - metabolism</topic><topic>Proliferating Cell Nuclear Antigen - metabolism</topic><topic>Thrombospondin 1 - therapeutic use</topic><topic>thrombospondin‐1</topic><topic>tumor angiogenesis</topic><topic>Urinary Bladder Neoplasms - blood supply</topic><topic>Urinary Bladder Neoplasms - metabolism</topic><topic>Urinary Bladder Neoplasms - prevention & control</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Reiher, Frank K.</creatorcontrib><creatorcontrib>Volpert, Olga V.</creatorcontrib><creatorcontrib>Jimenez, Benilde</creatorcontrib><creatorcontrib>Crawford, Susan E.</creatorcontrib><creatorcontrib>Dinney, Colin P.</creatorcontrib><creatorcontrib>Henkin, Jack</creatorcontrib><creatorcontrib>Haviv, Fortuna</creatorcontrib><creatorcontrib>Bouck, Noel P.</creatorcontrib><creatorcontrib>Campbell, Steven C.</creatorcontrib><collection>Pascal-Francis</collection><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>International journal of cancer</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Reiher, Frank K.</au><au>Volpert, Olga V.</au><au>Jimenez, Benilde</au><au>Crawford, Susan E.</au><au>Dinney, Colin P.</au><au>Henkin, Jack</au><au>Haviv, Fortuna</au><au>Bouck, Noel P.</au><au>Campbell, Steven C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inhibition of tumor growth by systemic treatment with thrombospondin‐1 peptide mimetics</atitle><jtitle>International journal of cancer</jtitle><addtitle>Int J Cancer</addtitle><date>2002-04-10</date><risdate>2002</risdate><volume>98</volume><issue>5</issue><spage>682</spage><epage>689</epage><pages>682-689</pages><issn>0020-7136</issn><eissn>1097-0215</eissn><coden>IJCNAW</coden><abstract>Many normal human cells produce thrombospondin‐1 (TSP‐1), a potent antiangiogenic protein that promotes vascular quiescence. In various organ systems, including the brain, breast and bladder and in fibroblasts, TSP‐1 secretion is reduced during tumorigenesis, thereby allowing induction of the vigorous neovascularization required for tumor growth and metastasis. Full‐length and short TSP‐1–derived peptides inhibit angiogenesis by inducing endothelial cell apoptosis and thus disrupting the vasculature of the growing tumor. CD36 expressed on the surface of endothelial cells functions as the primary antiangiogenic receptor for TSP‐1. A D‐isoleucyl enantiomer of a TSP‐1 heptapeptide specifically inhibits the proliferation and migration of capillary endothelial cells. DI‐TSP, an approximately 1 kDa capped version of this peptide, is also antiangiogenic in vitro, with a specific activity approaching that of the 450 kDa parental molecule. Here, we show that DI‐TSP delivered systemically dose‐dependently inhibits the growth of murine melanoma metastases in syngeneic animals and that its more soluble isomer, DI‐TSPa, similarly blocks the progression of primary human bladder tumors in an orthotopic model in immune‐deficient mice. Like intact TSP‐1, these peptide mimetics had no effect on cancer cells growing in vitro but markedly suppressed the growth of endothelial cells by inducing receptor‐dependent apoptosis. Antibodies raised against CD36 blocked the ability of peptides to induce apoptosis in endothelial cells but had no effect on tumor necrosis factor‐α–induced apoptosis. In vivo, the peptide mimetics were associated with a significantly reduced microvessel density and increased apoptotic indices in both the endothelial and tumor cell compartments. Such short peptides targeted to a specific antiangiogenic receptor, potent and easy to synthesize, show great promise as lead compounds in clinical antiangiogenic strategies. © 2002 Wiley‐Liss, Inc.</abstract><cop>New York</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>11920636</pmid><doi>10.1002/ijc.10247</doi><tpages>8</tpages></addata></record> |
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subjects | Animals Antineoplastic agents Apoptosis - drug effects Biological and medical sciences bladder cancer CD36 Antigens - metabolism Cell Division - drug effects Cell Division - physiology Chemotherapy Dose-Response Relationship, Drug Endothelium, Vascular - drug effects Endothelium, Vascular - pathology Humans In Situ Nick-End Labeling Lung Neoplasms - blood supply Lung Neoplasms - metabolism Lung Neoplasms - prevention & control Male Medical sciences melanoma Melanoma, Experimental - drug therapy Melanoma, Experimental - pathology Mice Mice, Inbred C57BL Mice, Nude Molecular Mimicry Neovascularization, Pathologic - drug therapy Neovascularization, Pathologic - metabolism Peptide Fragments - therapeutic use peptide mimetics Pharmacology. Drug treatments Platelet Endothelial Cell Adhesion Molecule-1 - metabolism Proliferating Cell Nuclear Antigen - metabolism Thrombospondin 1 - therapeutic use thrombospondin‐1 tumor angiogenesis Urinary Bladder Neoplasms - blood supply Urinary Bladder Neoplasms - metabolism Urinary Bladder Neoplasms - prevention & control |
title | Inhibition of tumor growth by systemic treatment with thrombospondin‐1 peptide mimetics |
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