| Heat-shock protein 72 cell-surface expression on human lung carcinoma cells in associated with an increased sensitivity to lysis mediated by adherent natural killer cells. | |
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MedLine Citation:
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PMID: 9003468 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The cell-surface expression patterns of major histocompatibility complex (MHC) class I, class II and heat-shock protein 72 (HSP72) molecules were measured on human lung (LX-1) and mammary (MX-1) carcinoma cells. No major differences were found in the MHC cell-surface expression pattern of both cell lines. However, they differ significantly in their capacity to express HSP72 on their cell surface. Under physiological conditions LX-1 cells express HSP72 molecules on more than 90% of the cells, whereas MX-1 cells exhibit no significant HSP72 cell-surface expression (less than 5%). These expression patterns remained stable in all further cell passages tested. The sensitivity to lysis mediated by an interleukin-2 (IL-2)-stimulated, adherent natural killer (NK) cell population could be correlated with the amount of cell-surface-expressed HSP72 molecules. By antibody-blocking studies, using HSP72-specific monoclonal antibody (mAb), a strong inhibition of lysis was only found with LX-1 cells but not with MX-1 cells. In contrast to the cell-surface expression, the cytoplasmic amount of HSP72 in MX-1 cells was twice as high compared to LX-1 cells under physiological conditions. After nonlethal heat-shock the rate of induction and the total cytoplasmic amounts of HSP72 were comparable in both cell lines. The clonogenic cell viability of LX-1 cells after incubation at temperatures ranging from 41 degrees C to 44 degrees C was significantly elevated compared to that of MX-1 cells. In conclusion we state the following: (i) HSP72 cell-surface expression on human carcinoma cells is independent of the cytoplasmic amount of HSP72; (ii) the cell-surface expression of HSP72 is associated with an increased sensitivity of tumor cells to lysis mediated by an IL-2-stimulated, adherent NK cell population; (iii) thermoresistance is not related to the cytoplasmic HSP72 level but might be related to the amount of HSP72 expressed on the cell surface. |
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Authors:
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C Botzler; R Issels; G Multhoff |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Cancer immunology, immunotherapy : CII Volume: 43 ISSN: 0340-7004 ISO Abbreviation: Cancer Immunol. Immunother. Publication Date: 1996 Dec |
Date Detail:
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Created Date: 1997-02-19 Completed Date: 1997-02-19 Revised Date: 2005-11-17 |
Medline Journal Info:
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Nlm Unique ID: 8605732 Medline TA: Cancer Immunol Immunother Country: GERMANY |
Other Details:
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Languages: eng Pagination: 226-30 Citation Subset: IM |
Affiliation:
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GSF-National Research Centre for Environment and Health, Institute of Clinical Hematology, Munich, Germany. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Cell Adhesion
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physiology Cell Count Cytotoxicity, Immunologic Flow Cytometry HSP72 Heat-Shock Proteins Heat-Shock Proteins / metabolism* Histocompatibility Antigens Class I / metabolism Histocompatibility Antigens Class II / metabolism Humans Killer Cells, Natural / cytology, immunology* Lung Neoplasms / immunology*, metabolism* Sensitivity and Specificity |
| Chemical | |
Reg. No./Substance:
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0/HSP72 Heat-Shock Proteins; 0/Heat-Shock Proteins; 0/Histocompatibility Antigens Class I; 0/Histocompatibility Antigens Class II |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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