Direct targeting of cancer cells: A multiparameter approach
Lectins have been widely used in cell surface studies and in the development of potential anticancer drugs. Many past studies that have examined lectin toxicity have only evaluated the effects on cancer cells, not their non-cancer counterparts. In addition, few past studies have evaluated the relati...
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description | Lectins have been widely used in cell surface studies and in the development of potential anticancer drugs. Many past studies that have examined lectin toxicity have only evaluated the effects on cancer cells, not their non-cancer counterparts. In addition, few past studies have evaluated the relationship between lectin-cell binding and lectin toxicity on both cell types. Here we examine these parameters in one study: lectin-cell binding and lectin toxicity with both cancer cells and their normal counterparts. We found that the human colon cancer cell line CCL-220/Colo320DM bound to agarose beads derivatized with
Phaseolus vulgaris agglutinin (PHA-L) and wheat germ agglutinin (WGA), while the non-cancer human colon cell line CRL-1459/CCD-18Co did not. When these lectins were tested for their effects on cell viability in culture, both cell lines were affected by the lectins but at 6, 48 and 72
h incubation times, PHA-L was most toxic to the cancer cell line in a concentration dependent manner. At 48
h incubation, WGA was more toxic to the cancer cell line. The results suggest that it may be possible to develop lectin protocols that selectively target cancer cells for death. In any case, examination of both malignant cells and their non-malignant counterparts, analysis of their binding characteristics to immobilized lectins, and examination of the toxicity of free lectins in culture, provides a multiparameter model for obtaining more comprehensive information than from more limited approaches. |
doi_str_mv | 10.1016/j.acthis.2005.06.013 |
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Phaseolus vulgaris agglutinin (PHA-L) and wheat germ agglutinin (WGA), while the non-cancer human colon cell line CRL-1459/CCD-18Co did not. When these lectins were tested for their effects on cell viability in culture, both cell lines were affected by the lectins but at 6, 48 and 72
h incubation times, PHA-L was most toxic to the cancer cell line in a concentration dependent manner. At 48
h incubation, WGA was more toxic to the cancer cell line. The results suggest that it may be possible to develop lectin protocols that selectively target cancer cells for death. In any case, examination of both malignant cells and their non-malignant counterparts, analysis of their binding characteristics to immobilized lectins, and examination of the toxicity of free lectins in culture, provides a multiparameter model for obtaining more comprehensive information than from more limited approaches.</description><identifier>ISSN: 0065-1281</identifier><identifier>EISSN: 1618-0372</identifier><identifier>DOI: 10.1016/j.acthis.2005.06.013</identifier><identifier>PMID: 16181664</identifier><language>eng</language><publisher>Germany: Elsevier GmbH</publisher><subject>Animals ; Cell Count ; Cell Line ; Cell Line, Tumor ; Cell Survival ; Colon - cytology ; Colon - metabolism ; Colonic Neoplasms - metabolism ; Colonic Neoplasms - pathology ; Histocytochemistry - methods ; Human colon cancer and non-cancer colon cells ; Humans ; Immobilized lectin binding ; Lectin toxicity in culture ; Lectins - metabolism ; Lectins - toxicity ; Mice ; Mice, Nude ; PHA-L ; Phytohemagglutinins - metabolism ; Phytohemagglutinins - toxicity ; Plant Proteins - metabolism ; Plant Proteins - toxicity ; WGA ; Wheat Germ Agglutinins - metabolism ; Wheat Germ Agglutinins - toxicity</subject><ispartof>Acta histochemica, 2005-01, Vol.107 (5), p.335-344</ispartof><rights>2005 Elsevier GmbH</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c492t-528834d55e00ec0d59d81056821b43b14f575486e857c098180b25a84d8aab9b3</citedby><cites>FETCH-LOGICAL-c492t-528834d55e00ec0d59d81056821b43b14f575486e857c098180b25a84d8aab9b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.acthis.2005.06.013$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,780,784,885,3548,27922,27923,45993,64385</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16181664$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Heinrich, Eileen L.</creatorcontrib><creatorcontrib>Welty, Lily Anne Y.</creatorcontrib><creatorcontrib>Banner, Lisa R.</creatorcontrib><creatorcontrib>Oppenheimer, Steven B.</creatorcontrib><title>Direct targeting of cancer cells: A multiparameter approach</title><title>Acta histochemica</title><addtitle>Acta Histochem</addtitle><description>Lectins have been widely used in cell surface studies and in the development of potential anticancer drugs. Many past studies that have examined lectin toxicity have only evaluated the effects on cancer cells, not their non-cancer counterparts. In addition, few past studies have evaluated the relationship between lectin-cell binding and lectin toxicity on both cell types. Here we examine these parameters in one study: lectin-cell binding and lectin toxicity with both cancer cells and their normal counterparts. We found that the human colon cancer cell line CCL-220/Colo320DM bound to agarose beads derivatized with
Phaseolus vulgaris agglutinin (PHA-L) and wheat germ agglutinin (WGA), while the non-cancer human colon cell line CRL-1459/CCD-18Co did not. When these lectins were tested for their effects on cell viability in culture, both cell lines were affected by the lectins but at 6, 48 and 72
h incubation times, PHA-L was most toxic to the cancer cell line in a concentration dependent manner. At 48
h incubation, WGA was more toxic to the cancer cell line. The results suggest that it may be possible to develop lectin protocols that selectively target cancer cells for death. In any case, examination of both malignant cells and their non-malignant counterparts, analysis of their binding characteristics to immobilized lectins, and examination of the toxicity of free lectins in culture, provides a multiparameter model for obtaining more comprehensive information than from more limited approaches.</description><subject>Animals</subject><subject>Cell Count</subject><subject>Cell Line</subject><subject>Cell Line, Tumor</subject><subject>Cell Survival</subject><subject>Colon - cytology</subject><subject>Colon - metabolism</subject><subject>Colonic Neoplasms - metabolism</subject><subject>Colonic Neoplasms - pathology</subject><subject>Histocytochemistry - methods</subject><subject>Human colon cancer and non-cancer colon cells</subject><subject>Humans</subject><subject>Immobilized lectin binding</subject><subject>Lectin toxicity in culture</subject><subject>Lectins - metabolism</subject><subject>Lectins - toxicity</subject><subject>Mice</subject><subject>Mice, Nude</subject><subject>PHA-L</subject><subject>Phytohemagglutinins - metabolism</subject><subject>Phytohemagglutinins - toxicity</subject><subject>Plant Proteins - metabolism</subject><subject>Plant Proteins - toxicity</subject><subject>WGA</subject><subject>Wheat Germ Agglutinins - metabolism</subject><subject>Wheat Germ Agglutinins - toxicity</subject><issn>0065-1281</issn><issn>1618-0372</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kFtLI0EQhRtx2UTdfyAyT77NWH1Nj4Ig3nZB2Jf1uenpqSQd5mZ3R_DfOzHB6Ms-FVSdOlXnI-SUQkGBqotVYV1a-lgwAFmAKoDyAzKliuoc-IwdkimAkjllmk7IUYwrACiBs59kshFRpcSUXN35gC5lyYYFJt8tsn6eOds5DJnDpomX2U3WrpvkBxtsi2ns22EIvXXLE_JjbpuIv3b1mDw_3P-7_Z0__X38c3vzlDtRspRLpjUXtZQIgA5qWdaaglSa0Urwioq5nEmhFWo5c1BqqqFi0mpRa2ursuLH5HrrO6yrFmuHXQq2MUPwrQ1vprfefJ90fmkW_auhoyPnYjQ43xmE_mWNMZnWx00622G_joYzzhSTfBSKrdCFPsaA888jFMyGulmZLXWzoW5AmZH6uHb29cH90g7zPgGOmF49BhOdxxFy_UHf1L3__4V3MoaU0w</recordid><startdate>20050101</startdate><enddate>20050101</enddate><creator>Heinrich, Eileen L.</creator><creator>Welty, Lily Anne Y.</creator><creator>Banner, Lisa R.</creator><creator>Oppenheimer, Steven B.</creator><general>Elsevier GmbH</general><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>7U5</scope><scope>8FD</scope><scope>L7M</scope><scope>5PM</scope></search><sort><creationdate>20050101</creationdate><title>Direct targeting of cancer cells: A multiparameter approach</title><author>Heinrich, Eileen L. ; Welty, Lily Anne Y. ; Banner, Lisa R. ; Oppenheimer, Steven B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c492t-528834d55e00ec0d59d81056821b43b14f575486e857c098180b25a84d8aab9b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Animals</topic><topic>Cell Count</topic><topic>Cell Line</topic><topic>Cell Line, Tumor</topic><topic>Cell Survival</topic><topic>Colon - cytology</topic><topic>Colon - metabolism</topic><topic>Colonic Neoplasms - metabolism</topic><topic>Colonic Neoplasms - pathology</topic><topic>Histocytochemistry - methods</topic><topic>Human colon cancer and non-cancer colon cells</topic><topic>Humans</topic><topic>Immobilized lectin binding</topic><topic>Lectin toxicity in culture</topic><topic>Lectins - metabolism</topic><topic>Lectins - toxicity</topic><topic>Mice</topic><topic>Mice, Nude</topic><topic>PHA-L</topic><topic>Phytohemagglutinins - metabolism</topic><topic>Phytohemagglutinins - toxicity</topic><topic>Plant Proteins - metabolism</topic><topic>Plant Proteins - toxicity</topic><topic>WGA</topic><topic>Wheat Germ Agglutinins - metabolism</topic><topic>Wheat Germ Agglutinins - toxicity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Heinrich, Eileen L.</creatorcontrib><creatorcontrib>Welty, Lily Anne Y.</creatorcontrib><creatorcontrib>Banner, Lisa R.</creatorcontrib><creatorcontrib>Oppenheimer, Steven B.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Acta histochemica</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Heinrich, Eileen L.</au><au>Welty, Lily Anne Y.</au><au>Banner, Lisa R.</au><au>Oppenheimer, Steven B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Direct targeting of cancer cells: A multiparameter approach</atitle><jtitle>Acta histochemica</jtitle><addtitle>Acta Histochem</addtitle><date>2005-01-01</date><risdate>2005</risdate><volume>107</volume><issue>5</issue><spage>335</spage><epage>344</epage><pages>335-344</pages><issn>0065-1281</issn><eissn>1618-0372</eissn><abstract>Lectins have been widely used in cell surface studies and in the development of potential anticancer drugs. Many past studies that have examined lectin toxicity have only evaluated the effects on cancer cells, not their non-cancer counterparts. In addition, few past studies have evaluated the relationship between lectin-cell binding and lectin toxicity on both cell types. Here we examine these parameters in one study: lectin-cell binding and lectin toxicity with both cancer cells and their normal counterparts. We found that the human colon cancer cell line CCL-220/Colo320DM bound to agarose beads derivatized with
Phaseolus vulgaris agglutinin (PHA-L) and wheat germ agglutinin (WGA), while the non-cancer human colon cell line CRL-1459/CCD-18Co did not. When these lectins were tested for their effects on cell viability in culture, both cell lines were affected by the lectins but at 6, 48 and 72
h incubation times, PHA-L was most toxic to the cancer cell line in a concentration dependent manner. At 48
h incubation, WGA was more toxic to the cancer cell line. The results suggest that it may be possible to develop lectin protocols that selectively target cancer cells for death. In any case, examination of both malignant cells and their non-malignant counterparts, analysis of their binding characteristics to immobilized lectins, and examination of the toxicity of free lectins in culture, provides a multiparameter model for obtaining more comprehensive information than from more limited approaches.</abstract><cop>Germany</cop><pub>Elsevier GmbH</pub><pmid>16181664</pmid><doi>10.1016/j.acthis.2005.06.013</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals Cell Count Cell Line Cell Line, Tumor Cell Survival Colon - cytology Colon - metabolism Colonic Neoplasms - metabolism Colonic Neoplasms - pathology Histocytochemistry - methods Human colon cancer and non-cancer colon cells Humans Immobilized lectin binding Lectin toxicity in culture Lectins - metabolism Lectins - toxicity Mice Mice, Nude PHA-L Phytohemagglutinins - metabolism Phytohemagglutinins - toxicity Plant Proteins - metabolism Plant Proteins - toxicity WGA Wheat Germ Agglutinins - metabolism Wheat Germ Agglutinins - toxicity |
title | Direct targeting of cancer cells: A multiparameter approach |
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