Loading…
Sialic acid content of tissue-specific gp96 and its potential role in modulating gp96-macrophage interactions
Cancer-derived heat shock protein gp96 induces a tumor-specific protective immune response primarily mediated by cytotoxic T lymphocytes (CTL) directed toward cancer-associated peptides associated with gp96. Both innate and adaptive immune responses have been demonstrated using a cell culture-based...
Saved in:
Published in: | Glycobiology (Oxford) 2009-12, Vol.19 (12), p.1427-1435 |
---|---|
Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c457t-e9b757f8042b8fe0dfdeaa2570b50f4681cbab1c3c53464f5bd5ea19899f5b173 |
---|---|
cites | cdi_FETCH-LOGICAL-c457t-e9b757f8042b8fe0dfdeaa2570b50f4681cbab1c3c53464f5bd5ea19899f5b173 |
container_end_page | 1435 |
container_issue | 12 |
container_start_page | 1427 |
container_title | Glycobiology (Oxford) |
container_volume | 19 |
creator | Suriano, Robert Ghosh, Salil K Chaudhuri, Devyani Mittelman, Abraham Banerjee, Asesh Tiwari, Raj K |
description | Cancer-derived heat shock protein gp96 induces a tumor-specific protective immune response primarily mediated by cytotoxic T lymphocytes (CTL) directed toward cancer-associated peptides associated with gp96. Both innate and adaptive immune responses have been demonstrated using a cell culture-based signaling mechanism. When used as an extraneous vaccine, one critical interaction which must occur for an immune response to be generated is the interaction between gp96 and the antigen presenting cell (APC) surface receptors (CD91, SR-A, TLR-2, and TLR-4). Our previous study concluded that gp96 purified from various rat and human prostate cancers is differentially glycosylated based on the amino and neutral monosaccharide content, and it was postulated that the monosaccharides may play a role in its biological activity. In this report, we report differences in the cancer-specific sialic acid content of gp96 purified from normal rat prostate compared to two rat prostate cancers, MAT-LyLu and Dunning G, as well as between two human prostate cancer cells, LnCaP and DU145. We also examined the modulatory effect of sialic acid residues on the binding of gp96 to APCs and its subsequent activation. Our results supported the contention that significant differences in the sialic acid content exist between Dunning G, MAT-LyLu, and normal rat prostate gp96, which affected its binding and biochemical activity to APCs. We therefore postulate that varied glycans of HPS96, a hitherto neglected structural component, may play a pivotal role in its anticancer activity. We suggest that construction of the glycan tree is a key to identification of the necessary and sufficient elements in the structure-function activity of HSP96. |
doi_str_mv | 10.1093/glycob/cwp096 |
format | article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_733681888</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><oup_id>10.1093/glycob/cwp096</oup_id><sourcerecordid>733681888</sourcerecordid><originalsourceid>FETCH-LOGICAL-c457t-e9b757f8042b8fe0dfdeaa2570b50f4681cbab1c3c53464f5bd5ea19899f5b173</originalsourceid><addsrcrecordid>eNqF0s9v1iAYB3BiXNzr9OhVOamXOijl13Euzi6Z0WQuMV4IpVDRtlSgmfvv5bVv3E1PkDwfvoTnAYBnGL3BSJLTYbwzoTs1twuS7AHY4Yahqm5q8hDskKSyYoyKY_A4pe8IYYYFfQSOsaRcYIZ2YLr2evQGauN7aMKc7ZxhcDD7lFZbpcUa70p9WCSDeu6hzwkuYc_KQRjDaKGf4RT6ddTZz8MfWU3axLB808O-mm3UJvswpyfgyOkx2aeH9QTcXLz7fN5WVx_fX56fXVWmoTxXVnaccidQU3fCWdS73mpdU446ilzDBDad7rAhhpKGNY52PbUaSyFl2WNOTsCrLXeJ4edqU1aTT8aOo55tWJPihJQQIUSRL_8pa4yFFAgVWG2wPCylaJ1aop90vFMYqf0k1DYJtU2i-OeH4LWbbH-vD60v4PUGwrr8N-twt0_Z_vqLdfyhGCecqvbLV3XxSX7gbduqt8W_2LzTQekh-qRurmuESfkApUlEkt8NIq4c</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>21189800</pqid></control><display><type>article</type><title>Sialic acid content of tissue-specific gp96 and its potential role in modulating gp96-macrophage interactions</title><source>Oxford Journals Online</source><creator>Suriano, Robert ; Ghosh, Salil K ; Chaudhuri, Devyani ; Mittelman, Abraham ; Banerjee, Asesh ; Tiwari, Raj K</creator><creatorcontrib>Suriano, Robert ; Ghosh, Salil K ; Chaudhuri, Devyani ; Mittelman, Abraham ; Banerjee, Asesh ; Tiwari, Raj K</creatorcontrib><description>Cancer-derived heat shock protein gp96 induces a tumor-specific protective immune response primarily mediated by cytotoxic T lymphocytes (CTL) directed toward cancer-associated peptides associated with gp96. Both innate and adaptive immune responses have been demonstrated using a cell culture-based signaling mechanism. When used as an extraneous vaccine, one critical interaction which must occur for an immune response to be generated is the interaction between gp96 and the antigen presenting cell (APC) surface receptors (CD91, SR-A, TLR-2, and TLR-4). Our previous study concluded that gp96 purified from various rat and human prostate cancers is differentially glycosylated based on the amino and neutral monosaccharide content, and it was postulated that the monosaccharides may play a role in its biological activity. In this report, we report differences in the cancer-specific sialic acid content of gp96 purified from normal rat prostate compared to two rat prostate cancers, MAT-LyLu and Dunning G, as well as between two human prostate cancer cells, LnCaP and DU145. We also examined the modulatory effect of sialic acid residues on the binding of gp96 to APCs and its subsequent activation. Our results supported the contention that significant differences in the sialic acid content exist between Dunning G, MAT-LyLu, and normal rat prostate gp96, which affected its binding and biochemical activity to APCs. We therefore postulate that varied glycans of HPS96, a hitherto neglected structural component, may play a pivotal role in its anticancer activity. We suggest that construction of the glycan tree is a key to identification of the necessary and sufficient elements in the structure-function activity of HSP96.</description><identifier>ISSN: 0959-6658</identifier><identifier>EISSN: 1460-2423</identifier><identifier>DOI: 10.1093/glycob/cwp096</identifier><identifier>PMID: 19578160</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Animals ; cancer ; Cell Communication - immunology ; Cells, Cultured ; Cytokines - secretion ; Glycosylation ; gp96 ; heat shock proteins ; HPAE-PAD ; Humans ; Macrophages - immunology ; Macrophages - metabolism ; Macrophages - physiology ; Membrane Glycoproteins - chemistry ; Membrane Glycoproteins - isolation & purification ; Membrane Glycoproteins - metabolism ; Membrane Glycoproteins - physiology ; N-Acetylneuraminic Acid - analysis ; N-Acetylneuraminic Acid - chemistry ; N-Acetylneuraminic Acid - isolation & purification ; N-Acetylneuraminic Acid - physiology ; Neoplasms - immunology ; Polysaccharides - analysis ; Polysaccharides - metabolism ; Protein Binding ; Protein Processing, Post-Translational ; Rats ; sialic acid ; Structure-Activity Relationship</subject><ispartof>Glycobiology (Oxford), 2009-12, Vol.19 (12), p.1427-1435</ispartof><rights>Oxford University Press © The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c457t-e9b757f8042b8fe0dfdeaa2570b50f4681cbab1c3c53464f5bd5ea19899f5b173</citedby><cites>FETCH-LOGICAL-c457t-e9b757f8042b8fe0dfdeaa2570b50f4681cbab1c3c53464f5bd5ea19899f5b173</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19578160$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Suriano, Robert</creatorcontrib><creatorcontrib>Ghosh, Salil K</creatorcontrib><creatorcontrib>Chaudhuri, Devyani</creatorcontrib><creatorcontrib>Mittelman, Abraham</creatorcontrib><creatorcontrib>Banerjee, Asesh</creatorcontrib><creatorcontrib>Tiwari, Raj K</creatorcontrib><title>Sialic acid content of tissue-specific gp96 and its potential role in modulating gp96-macrophage interactions</title><title>Glycobiology (Oxford)</title><addtitle>Glycobiology</addtitle><addtitle>Glycobiology</addtitle><description>Cancer-derived heat shock protein gp96 induces a tumor-specific protective immune response primarily mediated by cytotoxic T lymphocytes (CTL) directed toward cancer-associated peptides associated with gp96. Both innate and adaptive immune responses have been demonstrated using a cell culture-based signaling mechanism. When used as an extraneous vaccine, one critical interaction which must occur for an immune response to be generated is the interaction between gp96 and the antigen presenting cell (APC) surface receptors (CD91, SR-A, TLR-2, and TLR-4). Our previous study concluded that gp96 purified from various rat and human prostate cancers is differentially glycosylated based on the amino and neutral monosaccharide content, and it was postulated that the monosaccharides may play a role in its biological activity. In this report, we report differences in the cancer-specific sialic acid content of gp96 purified from normal rat prostate compared to two rat prostate cancers, MAT-LyLu and Dunning G, as well as between two human prostate cancer cells, LnCaP and DU145. We also examined the modulatory effect of sialic acid residues on the binding of gp96 to APCs and its subsequent activation. Our results supported the contention that significant differences in the sialic acid content exist between Dunning G, MAT-LyLu, and normal rat prostate gp96, which affected its binding and biochemical activity to APCs. We therefore postulate that varied glycans of HPS96, a hitherto neglected structural component, may play a pivotal role in its anticancer activity. We suggest that construction of the glycan tree is a key to identification of the necessary and sufficient elements in the structure-function activity of HSP96.</description><subject>Animals</subject><subject>cancer</subject><subject>Cell Communication - immunology</subject><subject>Cells, Cultured</subject><subject>Cytokines - secretion</subject><subject>Glycosylation</subject><subject>gp96</subject><subject>heat shock proteins</subject><subject>HPAE-PAD</subject><subject>Humans</subject><subject>Macrophages - immunology</subject><subject>Macrophages - metabolism</subject><subject>Macrophages - physiology</subject><subject>Membrane Glycoproteins - chemistry</subject><subject>Membrane Glycoproteins - isolation & purification</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Membrane Glycoproteins - physiology</subject><subject>N-Acetylneuraminic Acid - analysis</subject><subject>N-Acetylneuraminic Acid - chemistry</subject><subject>N-Acetylneuraminic Acid - isolation & purification</subject><subject>N-Acetylneuraminic Acid - physiology</subject><subject>Neoplasms - immunology</subject><subject>Polysaccharides - analysis</subject><subject>Polysaccharides - metabolism</subject><subject>Protein Binding</subject><subject>Protein Processing, Post-Translational</subject><subject>Rats</subject><subject>sialic acid</subject><subject>Structure-Activity Relationship</subject><issn>0959-6658</issn><issn>1460-2423</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><recordid>eNqF0s9v1iAYB3BiXNzr9OhVOamXOijl13Euzi6Z0WQuMV4IpVDRtlSgmfvv5bVv3E1PkDwfvoTnAYBnGL3BSJLTYbwzoTs1twuS7AHY4Yahqm5q8hDskKSyYoyKY_A4pe8IYYYFfQSOsaRcYIZ2YLr2evQGauN7aMKc7ZxhcDD7lFZbpcUa70p9WCSDeu6hzwkuYc_KQRjDaKGf4RT6ddTZz8MfWU3axLB808O-mm3UJvswpyfgyOkx2aeH9QTcXLz7fN5WVx_fX56fXVWmoTxXVnaccidQU3fCWdS73mpdU446ilzDBDad7rAhhpKGNY52PbUaSyFl2WNOTsCrLXeJ4edqU1aTT8aOo55tWJPihJQQIUSRL_8pa4yFFAgVWG2wPCylaJ1aop90vFMYqf0k1DYJtU2i-OeH4LWbbH-vD60v4PUGwrr8N-twt0_Z_vqLdfyhGCecqvbLV3XxSX7gbduqt8W_2LzTQekh-qRurmuESfkApUlEkt8NIq4c</recordid><startdate>20091201</startdate><enddate>20091201</enddate><creator>Suriano, Robert</creator><creator>Ghosh, Salil K</creator><creator>Chaudhuri, Devyani</creator><creator>Mittelman, Abraham</creator><creator>Banerjee, Asesh</creator><creator>Tiwari, Raj K</creator><general>Oxford University Press</general><scope>FBQ</scope><scope>BSCLL</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>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20091201</creationdate><title>Sialic acid content of tissue-specific gp96 and its potential role in modulating gp96-macrophage interactions</title><author>Suriano, Robert ; Ghosh, Salil K ; Chaudhuri, Devyani ; Mittelman, Abraham ; Banerjee, Asesh ; Tiwari, Raj K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c457t-e9b757f8042b8fe0dfdeaa2570b50f4681cbab1c3c53464f5bd5ea19899f5b173</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Animals</topic><topic>cancer</topic><topic>Cell Communication - immunology</topic><topic>Cells, Cultured</topic><topic>Cytokines - secretion</topic><topic>Glycosylation</topic><topic>gp96</topic><topic>heat shock proteins</topic><topic>HPAE-PAD</topic><topic>Humans</topic><topic>Macrophages - immunology</topic><topic>Macrophages - metabolism</topic><topic>Macrophages - physiology</topic><topic>Membrane Glycoproteins - chemistry</topic><topic>Membrane Glycoproteins - isolation & purification</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Membrane Glycoproteins - physiology</topic><topic>N-Acetylneuraminic Acid - analysis</topic><topic>N-Acetylneuraminic Acid - chemistry</topic><topic>N-Acetylneuraminic Acid - isolation & purification</topic><topic>N-Acetylneuraminic Acid - physiology</topic><topic>Neoplasms - immunology</topic><topic>Polysaccharides - analysis</topic><topic>Polysaccharides - metabolism</topic><topic>Protein Binding</topic><topic>Protein Processing, Post-Translational</topic><topic>Rats</topic><topic>sialic acid</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Suriano, Robert</creatorcontrib><creatorcontrib>Ghosh, Salil K</creatorcontrib><creatorcontrib>Chaudhuri, Devyani</creatorcontrib><creatorcontrib>Mittelman, Abraham</creatorcontrib><creatorcontrib>Banerjee, Asesh</creatorcontrib><creatorcontrib>Tiwari, Raj K</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Glycobiology (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Suriano, Robert</au><au>Ghosh, Salil K</au><au>Chaudhuri, Devyani</au><au>Mittelman, Abraham</au><au>Banerjee, Asesh</au><au>Tiwari, Raj K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sialic acid content of tissue-specific gp96 and its potential role in modulating gp96-macrophage interactions</atitle><jtitle>Glycobiology (Oxford)</jtitle><stitle>Glycobiology</stitle><addtitle>Glycobiology</addtitle><date>2009-12-01</date><risdate>2009</risdate><volume>19</volume><issue>12</issue><spage>1427</spage><epage>1435</epage><pages>1427-1435</pages><issn>0959-6658</issn><eissn>1460-2423</eissn><abstract>Cancer-derived heat shock protein gp96 induces a tumor-specific protective immune response primarily mediated by cytotoxic T lymphocytes (CTL) directed toward cancer-associated peptides associated with gp96. Both innate and adaptive immune responses have been demonstrated using a cell culture-based signaling mechanism. When used as an extraneous vaccine, one critical interaction which must occur for an immune response to be generated is the interaction between gp96 and the antigen presenting cell (APC) surface receptors (CD91, SR-A, TLR-2, and TLR-4). Our previous study concluded that gp96 purified from various rat and human prostate cancers is differentially glycosylated based on the amino and neutral monosaccharide content, and it was postulated that the monosaccharides may play a role in its biological activity. In this report, we report differences in the cancer-specific sialic acid content of gp96 purified from normal rat prostate compared to two rat prostate cancers, MAT-LyLu and Dunning G, as well as between two human prostate cancer cells, LnCaP and DU145. We also examined the modulatory effect of sialic acid residues on the binding of gp96 to APCs and its subsequent activation. Our results supported the contention that significant differences in the sialic acid content exist between Dunning G, MAT-LyLu, and normal rat prostate gp96, which affected its binding and biochemical activity to APCs. We therefore postulate that varied glycans of HPS96, a hitherto neglected structural component, may play a pivotal role in its anticancer activity. We suggest that construction of the glycan tree is a key to identification of the necessary and sufficient elements in the structure-function activity of HSP96.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>19578160</pmid><doi>10.1093/glycob/cwp096</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0959-6658 |
ispartof | Glycobiology (Oxford), 2009-12, Vol.19 (12), p.1427-1435 |
issn | 0959-6658 1460-2423 |
language | eng |
recordid | cdi_proquest_miscellaneous_733681888 |
source | Oxford Journals Online |
subjects | Animals cancer Cell Communication - immunology Cells, Cultured Cytokines - secretion Glycosylation gp96 heat shock proteins HPAE-PAD Humans Macrophages - immunology Macrophages - metabolism Macrophages - physiology Membrane Glycoproteins - chemistry Membrane Glycoproteins - isolation & purification Membrane Glycoproteins - metabolism Membrane Glycoproteins - physiology N-Acetylneuraminic Acid - analysis N-Acetylneuraminic Acid - chemistry N-Acetylneuraminic Acid - isolation & purification N-Acetylneuraminic Acid - physiology Neoplasms - immunology Polysaccharides - analysis Polysaccharides - metabolism Protein Binding Protein Processing, Post-Translational Rats sialic acid Structure-Activity Relationship |
title | Sialic acid content of tissue-specific gp96 and its potential role in modulating gp96-macrophage interactions |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T04%3A49%3A45IST&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=Sialic%20acid%20content%20of%20tissue-specific%20gp96%20and%20its%20potential%20role%20in%20modulating%20gp96-macrophage%20interactions&rft.jtitle=Glycobiology%20(Oxford)&rft.au=Suriano,%20Robert&rft.date=2009-12-01&rft.volume=19&rft.issue=12&rft.spage=1427&rft.epage=1435&rft.pages=1427-1435&rft.issn=0959-6658&rft.eissn=1460-2423&rft_id=info:doi/10.1093/glycob/cwp096&rft_dat=%3Cproquest_cross%3E733681888%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c457t-e9b757f8042b8fe0dfdeaa2570b50f4681cbab1c3c53464f5bd5ea19899f5b173%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=21189800&rft_id=info:pmid/19578160&rft_oup_id=10.1093/glycob/cwp096&rfr_iscdi=true |