Targeting membrane heat-shock protein 70 (Hsp70) on tumors by cmHsp70.1 antibody
Immunization of mice with a 14-mer peptide TKDNNLLGRFELSG, termed "TKD," comprising amino acids 450–461 (aa 450–461 ) in the C terminus of inducible Hsp70, resulted in the generation of an IgG1 mouse mAb cmHsp70.1. The epitope recognized by cmHsp70.1 mAb, which has been confirmed to be loc...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2011-01, Vol.108 (2), p.733-738 |
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| creator | Stangl, Stefan Gehrmann, Mathias Riegger, Julia Kuhs, Kristin Riederer, Isabelle Sievert, Wolfgang Hube, Kathrin Mocikat, Ralph Dressel, Ralf Kremmer, Elisabeth Pockley, Alan G. Friedrich, Lars Vigh, Laszlo Skerra, Arne Multhoff, Gabriele Kondorosi, Eva |
| description | Immunization of mice with a 14-mer peptide TKDNNLLGRFELSG, termed "TKD," comprising amino acids 450–461 (aa 450–461 ) in the C terminus of inducible Hsp70, resulted in the generation of an IgG1 mouse mAb cmHsp70.1. The epitope recognized by cmHsp70.1 mAb, which has been confirmed to be located in the TKD sequence by SPOT analysis, is frequently detectable on the cell surface of human and mouse tumors, but not on isogenic cells and normal tissues, and membrane Hsp70 might thus serve as a tumor-specific target structure. As shown for human tumors, Hsp70 is associated with cholesterol-rich microdomains in the plasma membrane of mouse tumors. Herein, we show that the cmHsp70.1 mAb can selectively induce antibody-dependent cellular cytotoxicity (ADCC) of membrane Hsp70⁺ mouse tumor cells by unstimulated mouse spleen cells. Tumor killing could be further enhanced by activating the effector cells with TKD and IL-2. Three consecutive injections of the cmHsp70.1 mAb into mice bearing CT26 tumors significantly inhibited tumor growth and enhanced the overall survival. These effects were associated with infiltrations of NK cells, macrophages, and granulocytes. The Hsp70 specificity of the ADCC response was confirmed by preventing the antitumor response in tumor-bearing mice by coinjecting the cognate TKD peptide with the cmHsp70.1 mAb, and by blocking the binding of cmHsp70.1 mAb to CT26 tumor cells using either TKD peptide or the C-terminal substrate-binding domain of Hsp70. |
| doi_str_mv | 10.1073/pnas.1016065108 |
| format | Article |
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The epitope recognized by cmHsp70.1 mAb, which has been confirmed to be located in the TKD sequence by SPOT analysis, is frequently detectable on the cell surface of human and mouse tumors, but not on isogenic cells and normal tissues, and membrane Hsp70 might thus serve as a tumor-specific target structure. As shown for human tumors, Hsp70 is associated with cholesterol-rich microdomains in the plasma membrane of mouse tumors. Herein, we show that the cmHsp70.1 mAb can selectively induce antibody-dependent cellular cytotoxicity (ADCC) of membrane Hsp70⁺ mouse tumor cells by unstimulated mouse spleen cells. Tumor killing could be further enhanced by activating the effector cells with TKD and IL-2. Three consecutive injections of the cmHsp70.1 mAb into mice bearing CT26 tumors significantly inhibited tumor growth and enhanced the overall survival. These effects were associated with infiltrations of NK cells, macrophages, and granulocytes. The Hsp70 specificity of the ADCC response was confirmed by preventing the antitumor response in tumor-bearing mice by coinjecting the cognate TKD peptide with the cmHsp70.1 mAb, and by blocking the binding of cmHsp70.1 mAb to CT26 tumor cells using either TKD peptide or the C-terminal substrate-binding domain of Hsp70.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1016065108</identifier><identifier>PMID: 21187371</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Amino acids ; Animals ; Antibodies ; Antibodies, Monoclonal - chemistry ; Antibody dependent cell cytotoxicity ; Binding sites ; Biochemistry ; Biological Sciences ; Cell Line, Tumor ; Cell lines ; Cell membranes ; Cholesterol - chemistry ; Cytotoxicity ; Granulocytes - cytology ; Heat shock proteins ; HSP70 Heat-Shock Proteins - chemistry ; Human subjects ; Humans ; Immunization ; Interleukin-2 - metabolism ; Killer Cells, Natural - cytology ; Macrophages - cytology ; Macrophages - metabolism ; Membranes ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Natural killer cells ; Neoplasm Transplantation ; Peptides ; Protein Binding ; Protein Structure, Tertiary ; Rodents ; Spleen cells ; T lymphocytes ; Tumor cell line ; Tumors</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2011-01, Vol.108 (2), p.733-738</ispartof><rights>Copyright National Academy of Sciences Jan 11, 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c529t-46c695d209b9950e0b61baf69c9f723a0af648171832e37902259622117847fa3</citedby><cites>FETCH-LOGICAL-c529t-46c695d209b9950e0b61baf69c9f723a0af648171832e37902259622117847fa3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/108/2.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/25770850$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/25770850$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27923,27924,53790,53792,58016,58249</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21187371$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Stangl, Stefan</creatorcontrib><creatorcontrib>Gehrmann, Mathias</creatorcontrib><creatorcontrib>Riegger, Julia</creatorcontrib><creatorcontrib>Kuhs, Kristin</creatorcontrib><creatorcontrib>Riederer, Isabelle</creatorcontrib><creatorcontrib>Sievert, Wolfgang</creatorcontrib><creatorcontrib>Hube, Kathrin</creatorcontrib><creatorcontrib>Mocikat, Ralph</creatorcontrib><creatorcontrib>Dressel, Ralf</creatorcontrib><creatorcontrib>Kremmer, Elisabeth</creatorcontrib><creatorcontrib>Pockley, Alan G.</creatorcontrib><creatorcontrib>Friedrich, Lars</creatorcontrib><creatorcontrib>Vigh, Laszlo</creatorcontrib><creatorcontrib>Skerra, Arne</creatorcontrib><creatorcontrib>Multhoff, Gabriele</creatorcontrib><creatorcontrib>Kondorosi, Eva</creatorcontrib><title>Targeting membrane heat-shock protein 70 (Hsp70) on tumors by cmHsp70.1 antibody</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Immunization of mice with a 14-mer peptide TKDNNLLGRFELSG, termed "TKD," comprising amino acids 450–461 (aa 450–461 ) in the C terminus of inducible Hsp70, resulted in the generation of an IgG1 mouse mAb cmHsp70.1. The epitope recognized by cmHsp70.1 mAb, which has been confirmed to be located in the TKD sequence by SPOT analysis, is frequently detectable on the cell surface of human and mouse tumors, but not on isogenic cells and normal tissues, and membrane Hsp70 might thus serve as a tumor-specific target structure. As shown for human tumors, Hsp70 is associated with cholesterol-rich microdomains in the plasma membrane of mouse tumors. Herein, we show that the cmHsp70.1 mAb can selectively induce antibody-dependent cellular cytotoxicity (ADCC) of membrane Hsp70⁺ mouse tumor cells by unstimulated mouse spleen cells. Tumor killing could be further enhanced by activating the effector cells with TKD and IL-2. Three consecutive injections of the cmHsp70.1 mAb into mice bearing CT26 tumors significantly inhibited tumor growth and enhanced the overall survival. These effects were associated with infiltrations of NK cells, macrophages, and granulocytes. The Hsp70 specificity of the ADCC response was confirmed by preventing the antitumor response in tumor-bearing mice by coinjecting the cognate TKD peptide with the cmHsp70.1 mAb, and by blocking the binding of cmHsp70.1 mAb to CT26 tumor cells using either TKD peptide or the C-terminal substrate-binding domain of Hsp70.</description><subject>Amino acids</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Antibodies, Monoclonal - chemistry</subject><subject>Antibody dependent cell cytotoxicity</subject><subject>Binding sites</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>Cell Line, Tumor</subject><subject>Cell lines</subject><subject>Cell membranes</subject><subject>Cholesterol - chemistry</subject><subject>Cytotoxicity</subject><subject>Granulocytes - cytology</subject><subject>Heat shock proteins</subject><subject>HSP70 Heat-Shock Proteins - chemistry</subject><subject>Human subjects</subject><subject>Humans</subject><subject>Immunization</subject><subject>Interleukin-2 - metabolism</subject><subject>Killer Cells, Natural - cytology</subject><subject>Macrophages - cytology</subject><subject>Macrophages - metabolism</subject><subject>Membranes</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Mice, Inbred C57BL</subject><subject>Natural killer cells</subject><subject>Neoplasm Transplantation</subject><subject>Peptides</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Rodents</subject><subject>Spleen cells</subject><subject>T lymphocytes</subject><subject>Tumor cell line</subject><subject>Tumors</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkc1vEzEQxS0EoqFw5gSyuACHbcff9gUJVUArVSqHcra8G2-yIWsvthcp_z1OGxroySPPb55m3kPoNYEzAoqdT8HlWhEJUhDQT9CCgCGN5AaeogUAVY3mlJ-gFzlvAMAIDc_RCSVEK6bIAn2_dWnlyxBWePRjm1zweO1dafI6dj_xlGLxQ8AK8IfLPCn4iGPAZR5jyrjd4W68-z0j2IUytHG5e4me9W6b_avDe4p-fP1ye3HZXN98u7r4fN10gprScNlJI5YUTGuMAA-tJK3rpelMryhzUGuuiSKaUc-UAUqFkbQurjRXvWOn6NO97jS3o192PpTktnZKw-jSzkY32P87YVjbVfxtGdDqFK0C7w8CKf6afS52HHLnt9tqQZyz1cwowigRlXz3iNzEOYV6ndUcqpNc8gqd30Ndijkn3z-sQsDus7L7rOwxqzrx9t8LHvi_4VTgzQHYTx7ltKVWMXbsb3KJ6TgvlAItgP0BizSgZQ</recordid><startdate>20110111</startdate><enddate>20110111</enddate><creator>Stangl, Stefan</creator><creator>Gehrmann, Mathias</creator><creator>Riegger, Julia</creator><creator>Kuhs, Kristin</creator><creator>Riederer, Isabelle</creator><creator>Sievert, Wolfgang</creator><creator>Hube, Kathrin</creator><creator>Mocikat, Ralph</creator><creator>Dressel, Ralf</creator><creator>Kremmer, Elisabeth</creator><creator>Pockley, Alan G.</creator><creator>Friedrich, Lars</creator><creator>Vigh, Laszlo</creator><creator>Skerra, Arne</creator><creator>Multhoff, Gabriele</creator><creator>Kondorosi, Eva</creator><general>National Academy of Sciences</general><general>National Acad Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20110111</creationdate><title>Targeting membrane heat-shock protein 70 (Hsp70) on tumors by cmHsp70.1 antibody</title><author>Stangl, Stefan ; Gehrmann, Mathias ; Riegger, Julia ; Kuhs, Kristin ; Riederer, Isabelle ; Sievert, Wolfgang ; Hube, Kathrin ; Mocikat, Ralph ; Dressel, Ralf ; Kremmer, Elisabeth ; Pockley, Alan G. ; Friedrich, Lars ; Vigh, Laszlo ; Skerra, Arne ; Multhoff, Gabriele ; Kondorosi, Eva</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c529t-46c695d209b9950e0b61baf69c9f723a0af648171832e37902259622117847fa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Amino acids</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Antibodies, Monoclonal - 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The epitope recognized by cmHsp70.1 mAb, which has been confirmed to be located in the TKD sequence by SPOT analysis, is frequently detectable on the cell surface of human and mouse tumors, but not on isogenic cells and normal tissues, and membrane Hsp70 might thus serve as a tumor-specific target structure. As shown for human tumors, Hsp70 is associated with cholesterol-rich microdomains in the plasma membrane of mouse tumors. Herein, we show that the cmHsp70.1 mAb can selectively induce antibody-dependent cellular cytotoxicity (ADCC) of membrane Hsp70⁺ mouse tumor cells by unstimulated mouse spleen cells. Tumor killing could be further enhanced by activating the effector cells with TKD and IL-2. Three consecutive injections of the cmHsp70.1 mAb into mice bearing CT26 tumors significantly inhibited tumor growth and enhanced the overall survival. These effects were associated with infiltrations of NK cells, macrophages, and granulocytes. The Hsp70 specificity of the ADCC response was confirmed by preventing the antitumor response in tumor-bearing mice by coinjecting the cognate TKD peptide with the cmHsp70.1 mAb, and by blocking the binding of cmHsp70.1 mAb to CT26 tumor cells using either TKD peptide or the C-terminal substrate-binding domain of Hsp70.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>21187371</pmid><doi>10.1073/pnas.1016065108</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino acids Animals Antibodies Antibodies, Monoclonal - chemistry Antibody dependent cell cytotoxicity Binding sites Biochemistry Biological Sciences Cell Line, Tumor Cell lines Cell membranes Cholesterol - chemistry Cytotoxicity Granulocytes - cytology Heat shock proteins HSP70 Heat-Shock Proteins - chemistry Human subjects Humans Immunization Interleukin-2 - metabolism Killer Cells, Natural - cytology Macrophages - cytology Macrophages - metabolism Membranes Mice Mice, Inbred BALB C Mice, Inbred C57BL Natural killer cells Neoplasm Transplantation Peptides Protein Binding Protein Structure, Tertiary Rodents Spleen cells T lymphocytes Tumor cell line Tumors |
| title | Targeting membrane heat-shock protein 70 (Hsp70) on tumors by cmHsp70.1 antibody |
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