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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:International journal of cancer 2002-04, Vol.98 (5), p.682-689
Hauptverfasser: Reiher, Frank K., Volpert, Olga V., Jimenez, Benilde, Crawford, Susan E., Dinney, Colin P., Henkin, Jack, Haviv, Fortuna, Bouck, Noel P., Campbell, Steven C.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 689
container_issue 5
container_start_page 682
container_title International journal of cancer
container_volume 98
creator Reiher, Frank K.
Volpert, Olga V.
Jimenez, Benilde
Crawford, Susan E.
Dinney, Colin P.
Henkin, Jack
Haviv, Fortuna
Bouck, Noel P.
Campbell, Steven C.
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
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_71559318</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>71559318</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3517-feb117a7f59f3c2caff385b5a7b67c2f2c5390e474957c6320cc8e909058ef463</originalsourceid><addsrcrecordid>eNp10L1OwzAQB3ALgaB8DLwA8gISQ8CO4zgZUcVHERILDEyR456pqzgOtquqG4_AM_IkGFqpE9OddD_d6f4InVJyRQnJr81cpSYvxA4aUVKLjOSU76JRmpFMUFYeoMMQ5oRQykmxjw4orXNSsnKE3ib9zLQmGtdjp3FcWOfxu3fLOMPtCodViGCNwtGDjBb6iJcmjeLMO9u6MLh-avrvzy-KBxiimQK2xkI0KhyjPS27ACebeoRe725fxg_Z0_P9ZHzzlCnGqcg0tJQKKTSvNVO5klqzirdcirYUKte54qwmUIii5kKVLCdKVVCTmvAKdFGyI3Sx3jt497GAEBtrgoKukz24RWgE5bxmtErwcg2VdyF40M3gjZV-1VDS_ObYpBybvxyTPdssXbQWplu5CS6B8w2QQclOe9krE7aO8Uqk_5K7Xrul6WD1_8Vm8jhen_4BsCyLJA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>71559318</pqid></control><display><type>article</type><title>Inhibition of tumor growth by systemic treatment with thrombospondin‐1 peptide mimetics</title><source>MEDLINE</source><source>Access via Wiley Online Library</source><source>EZB-FREE-00999 freely available EZB journals</source><creator>Reiher, Frank K. ; Volpert, Olga V. ; Jimenez, Benilde ; Crawford, Susan E. ; Dinney, Colin P. ; Henkin, Jack ; Haviv, Fortuna ; Bouck, Noel P. ; Campbell, Steven C.</creator><creatorcontrib>Reiher, Frank K. ; Volpert, Olga V. ; Jimenez, Benilde ; Crawford, Susan E. ; Dinney, Colin P. ; Henkin, Jack ; Haviv, Fortuna ; Bouck, Noel P. ; Campbell, Steven C.</creatorcontrib><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><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 &amp; 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 &amp; 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&amp;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 &amp; 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 &amp; 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 &amp; 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 &amp; 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>
fulltext fulltext
identifier ISSN: 0020-7136
ispartof International journal of cancer, 2002-04, Vol.98 (5), p.682-689
issn 0020-7136
1097-0215
language eng
recordid cdi_proquest_miscellaneous_71559318
source MEDLINE; Access via Wiley Online Library; EZB-FREE-00999 freely available EZB journals
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
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-09T13%3A39%3A00IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Inhibition%20of%20tumor%20growth%20by%20systemic%20treatment%20with%20thrombospondin%E2%80%901%20peptide%20mimetics&rft.jtitle=International%20journal%20of%20cancer&rft.au=Reiher,%20Frank%20K.&rft.date=2002-04-10&rft.volume=98&rft.issue=5&rft.spage=682&rft.epage=689&rft.pages=682-689&rft.issn=0020-7136&rft.eissn=1097-0215&rft.coden=IJCNAW&rft_id=info:doi/10.1002/ijc.10247&rft_dat=%3Cproquest_cross%3E71559318%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=71559318&rft_id=info:pmid/11920636&rfr_iscdi=true