Laminin-111-derived peptides and cancer
Laminin-111 is a large trimeric basement membrane glycoprotein with many active sites. In particular, four peptides active in tumor malignancy studies have been identified in laminin-111 using a systematic peptide screening method followed by various assays. Two of the peptides (IKVAV and AG73) are...
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| Veröffentlicht in: | Cell adhesion & migration 2013-01, Vol.7 (1), p.150-159 |
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| creator | Kikkawa, Yamato Hozumi, Kentaro Katagiri, Fumihiko Nomizu, Motoyoshi Kleinman, Hynda K. Koblinski, Jennifer E. |
| description | Laminin-111 is a large trimeric basement membrane glycoprotein with many active sites. In particular, four peptides active in tumor malignancy studies have been identified in laminin-111 using a systematic peptide screening method followed by various assays. Two of the peptides (IKVAV and AG73) are found on the α1 chain, one (YIGSR) of the β1 chain and one (C16) on the γ1 chain. The four peptides have distinct activities and receptors. Since three of the peptides (IKVAV, AG73 and C16) strongly promote tumor growth, this may explain the potent effects laminin-111 has on malignant cells. The peptide, YIGSR, decreases tumor growth and experimental metastasis via a 32/67 kD receptor while IKVAV increases tumor growth, angiogenesis and protease activity via integrin receptors. AG73 increases tumor growth and metastases via syndecan receptors. C16 increases tumor growth and angiogenesis via integrins. Identification of such sites on laminin-111 will have use in defining strategies to develop therapeutics for cancer. |
| doi_str_mv | 10.4161/cam.22827 |
| format | Article |
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In particular, four peptides active in tumor malignancy studies have been identified in laminin-111 using a systematic peptide screening method followed by various assays. Two of the peptides (IKVAV and AG73) are found on the α1 chain, one (YIGSR) of the β1 chain and one (C16) on the γ1 chain. The four peptides have distinct activities and receptors. Since three of the peptides (IKVAV, AG73 and C16) strongly promote tumor growth, this may explain the potent effects laminin-111 has on malignant cells. The peptide, YIGSR, decreases tumor growth and experimental metastasis via a 32/67 kD receptor while IKVAV increases tumor growth, angiogenesis and protease activity via integrin receptors. AG73 increases tumor growth and metastases via syndecan receptors. C16 increases tumor growth and angiogenesis via integrins. Identification of such sites on laminin-111 will have use in defining strategies to develop therapeutics for cancer.</description><identifier>ISSN: 1933-6918</identifier><identifier>EISSN: 1933-6926</identifier><identifier>DOI: 10.4161/cam.22827</identifier><identifier>PMID: 23263633</identifier><language>eng</language><publisher>United States: Taylor & Francis</publisher><subject>adhesion ; Amino Acid Sequence ; angiogenesis ; Animals ; Antineoplastic Agents - pharmacology ; basement membrane ; Basement Membrane - metabolism ; Catalytic Domain ; Cell Adhesion ; Cell Line, Tumor ; Cell Movement ; Enzyme Activation ; Extracellular Matrix - metabolism ; Humans ; Laminin - metabolism ; Laminin - pharmacology ; laminin-111 ; Melanoma - drug therapy ; Melanoma - metabolism ; Melanoma - pathology ; metastasis ; migration ; Neoplasm Metastasis - drug therapy ; Neoplasm Metastasis - pathology ; Oligopeptides - metabolism ; Oligopeptides - pharmacology ; Peptide Fragments - metabolism ; Peptide Fragments - pharmacology ; proteases ; Protein Binding ; Review ; synthetic peptide ; tumor growth</subject><ispartof>Cell adhesion & migration, 2013-01, Vol.7 (1), p.150-159</ispartof><rights>Copyright © 2013 Landes Bioscience 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c420t-4858857a8769595e8251bfcd0251ed2669f748dda6d7a55cc9154be6f3109cc23</citedby><cites>FETCH-LOGICAL-c420t-4858857a8769595e8251bfcd0251ed2669f748dda6d7a55cc9154be6f3109cc23</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/PMC3544779/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3544779/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23263633$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kikkawa, Yamato</creatorcontrib><creatorcontrib>Hozumi, Kentaro</creatorcontrib><creatorcontrib>Katagiri, Fumihiko</creatorcontrib><creatorcontrib>Nomizu, Motoyoshi</creatorcontrib><creatorcontrib>Kleinman, Hynda K.</creatorcontrib><creatorcontrib>Koblinski, Jennifer E.</creatorcontrib><title>Laminin-111-derived peptides and cancer</title><title>Cell adhesion & migration</title><addtitle>Cell Adh Migr</addtitle><description>Laminin-111 is a large trimeric basement membrane glycoprotein with many active sites. In particular, four peptides active in tumor malignancy studies have been identified in laminin-111 using a systematic peptide screening method followed by various assays. Two of the peptides (IKVAV and AG73) are found on the α1 chain, one (YIGSR) of the β1 chain and one (C16) on the γ1 chain. The four peptides have distinct activities and receptors. Since three of the peptides (IKVAV, AG73 and C16) strongly promote tumor growth, this may explain the potent effects laminin-111 has on malignant cells. The peptide, YIGSR, decreases tumor growth and experimental metastasis via a 32/67 kD receptor while IKVAV increases tumor growth, angiogenesis and protease activity via integrin receptors. AG73 increases tumor growth and metastases via syndecan receptors. C16 increases tumor growth and angiogenesis via integrins. Identification of such sites on laminin-111 will have use in defining strategies to develop therapeutics for cancer.</description><subject>adhesion</subject><subject>Amino Acid Sequence</subject><subject>angiogenesis</subject><subject>Animals</subject><subject>Antineoplastic Agents - pharmacology</subject><subject>basement membrane</subject><subject>Basement Membrane - metabolism</subject><subject>Catalytic Domain</subject><subject>Cell Adhesion</subject><subject>Cell Line, Tumor</subject><subject>Cell Movement</subject><subject>Enzyme Activation</subject><subject>Extracellular Matrix - metabolism</subject><subject>Humans</subject><subject>Laminin - metabolism</subject><subject>Laminin - pharmacology</subject><subject>laminin-111</subject><subject>Melanoma - drug therapy</subject><subject>Melanoma - metabolism</subject><subject>Melanoma - pathology</subject><subject>metastasis</subject><subject>migration</subject><subject>Neoplasm Metastasis - drug therapy</subject><subject>Neoplasm Metastasis - pathology</subject><subject>Oligopeptides - metabolism</subject><subject>Oligopeptides - pharmacology</subject><subject>Peptide Fragments - metabolism</subject><subject>Peptide Fragments - pharmacology</subject><subject>proteases</subject><subject>Protein Binding</subject><subject>Review</subject><subject>synthetic peptide</subject><subject>tumor growth</subject><issn>1933-6918</issn><issn>1933-6926</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>0YH</sourceid><sourceid>EIF</sourceid><recordid>eNplkMtKAzEUhoMoVqsLX0C6UxdTc79sBCneoOBG1yFNMhqZSWoyrfTtHW0tiqv_wPn4z-ED4ATBMUUcXVrTjjGWWOyAA6QIqbjCfHc7IzkAh6W8Qcgk4nwfDDDBnHBCDsDZ1LQhhlghhCrnc1h6N5r7eRecLyMT3ciaaH0-Anu1aYo_3uQQPN_ePE3uq-nj3cPkelpZimFXUcmkZMJIwRVTzEvM0Ky2DvbpHeZc1YJK5wx3wjBmrUKMzjyvCYLKWkyG4GrdO1_MWu-sj102jZ7n0Jq80skE_XcTw6t-SUtNGKVCqL7gfFOQ0_vCl063oVjfNCb6tCgaYUEI5JKQHr1YozanUrKvt2cQ1F9idS9Wf4vt2dPff23JH5M9QNdAiHXKrflIuXG6M6sm5Tr3DkPR5H_vJwe2hC4</recordid><startdate>20130101</startdate><enddate>20130101</enddate><creator>Kikkawa, Yamato</creator><creator>Hozumi, Kentaro</creator><creator>Katagiri, Fumihiko</creator><creator>Nomizu, Motoyoshi</creator><creator>Kleinman, Hynda K.</creator><creator>Koblinski, Jennifer E.</creator><general>Taylor & Francis</general><general>Landes Bioscience</general><scope>0YH</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><scope>5PM</scope></search><sort><creationdate>20130101</creationdate><title>Laminin-111-derived peptides and cancer</title><author>Kikkawa, Yamato ; Hozumi, Kentaro ; Katagiri, Fumihiko ; Nomizu, Motoyoshi ; Kleinman, Hynda K. ; Koblinski, Jennifer E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c420t-4858857a8769595e8251bfcd0251ed2669f748dda6d7a55cc9154be6f3109cc23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>adhesion</topic><topic>Amino Acid Sequence</topic><topic>angiogenesis</topic><topic>Animals</topic><topic>Antineoplastic Agents - pharmacology</topic><topic>basement membrane</topic><topic>Basement Membrane - metabolism</topic><topic>Catalytic Domain</topic><topic>Cell Adhesion</topic><topic>Cell Line, Tumor</topic><topic>Cell Movement</topic><topic>Enzyme Activation</topic><topic>Extracellular Matrix - metabolism</topic><topic>Humans</topic><topic>Laminin - metabolism</topic><topic>Laminin - pharmacology</topic><topic>laminin-111</topic><topic>Melanoma - drug therapy</topic><topic>Melanoma - metabolism</topic><topic>Melanoma - pathology</topic><topic>metastasis</topic><topic>migration</topic><topic>Neoplasm Metastasis - drug therapy</topic><topic>Neoplasm Metastasis - pathology</topic><topic>Oligopeptides - metabolism</topic><topic>Oligopeptides - pharmacology</topic><topic>Peptide Fragments - metabolism</topic><topic>Peptide Fragments - pharmacology</topic><topic>proteases</topic><topic>Protein Binding</topic><topic>Review</topic><topic>synthetic peptide</topic><topic>tumor growth</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kikkawa, Yamato</creatorcontrib><creatorcontrib>Hozumi, Kentaro</creatorcontrib><creatorcontrib>Katagiri, Fumihiko</creatorcontrib><creatorcontrib>Nomizu, Motoyoshi</creatorcontrib><creatorcontrib>Kleinman, Hynda K.</creatorcontrib><creatorcontrib>Koblinski, Jennifer E.</creatorcontrib><collection>Taylor & Francis Open Access</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell adhesion & migration</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kikkawa, Yamato</au><au>Hozumi, Kentaro</au><au>Katagiri, Fumihiko</au><au>Nomizu, Motoyoshi</au><au>Kleinman, Hynda K.</au><au>Koblinski, Jennifer E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Laminin-111-derived peptides and cancer</atitle><jtitle>Cell adhesion & migration</jtitle><addtitle>Cell Adh Migr</addtitle><date>2013-01-01</date><risdate>2013</risdate><volume>7</volume><issue>1</issue><spage>150</spage><epage>159</epage><pages>150-159</pages><issn>1933-6918</issn><eissn>1933-6926</eissn><abstract>Laminin-111 is a large trimeric basement membrane glycoprotein with many active sites. In particular, four peptides active in tumor malignancy studies have been identified in laminin-111 using a systematic peptide screening method followed by various assays. Two of the peptides (IKVAV and AG73) are found on the α1 chain, one (YIGSR) of the β1 chain and one (C16) on the γ1 chain. The four peptides have distinct activities and receptors. Since three of the peptides (IKVAV, AG73 and C16) strongly promote tumor growth, this may explain the potent effects laminin-111 has on malignant cells. The peptide, YIGSR, decreases tumor growth and experimental metastasis via a 32/67 kD receptor while IKVAV increases tumor growth, angiogenesis and protease activity via integrin receptors. AG73 increases tumor growth and metastases via syndecan receptors. C16 increases tumor growth and angiogenesis via integrins. Identification of such sites on laminin-111 will have use in defining strategies to develop therapeutics for cancer.</abstract><cop>United States</cop><pub>Taylor & Francis</pub><pmid>23263633</pmid><doi>10.4161/cam.22827</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | adhesion Amino Acid Sequence angiogenesis Animals Antineoplastic Agents - pharmacology basement membrane Basement Membrane - metabolism Catalytic Domain Cell Adhesion Cell Line, Tumor Cell Movement Enzyme Activation Extracellular Matrix - metabolism Humans Laminin - metabolism Laminin - pharmacology laminin-111 Melanoma - drug therapy Melanoma - metabolism Melanoma - pathology metastasis migration Neoplasm Metastasis - drug therapy Neoplasm Metastasis - pathology Oligopeptides - metabolism Oligopeptides - pharmacology Peptide Fragments - metabolism Peptide Fragments - pharmacology proteases Protein Binding Review synthetic peptide tumor growth |
| title | Laminin-111-derived peptides and cancer |
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