Gastpar, Robert and Gross, Catharina and Rossbacher, Lydia and Ellwart, Joachim and Riegger, Julia and Multhoff, Gabriele (2004) The cell surface-localized heat shock protein 70 epitope TKD induces migration and cytolytic activity selectively in human NK cells. JOURNAL OF IMMUNOLOGY, 172 (2). pp. 972-980. ISSN 0022-1767, 1550-6606
Full text not available from this repository. (Request a copy)Abstract
Profiling of surface-bound proteins uncovers a tumor-selective heat shock protein 70 (Hsp70) membrane expression that provides a target structure for human NK cells. Hsp70 peptide TKD (TKDNNLLGRFELSG; aa 450-463) was found to enhance the cytolytic activity of NK cells. In this study, we demonstrate that TKD-activated CD3(-)CD56(+)CD94(+) NK cells are selectively attracted by Hsp70 membrane-positive tumor cells, and supernatants derived thereof. Hsp70 membrane-negative tumors failed to attract these NK cells. The capacity to migrate was associated with a substantial lytic activity against Hsp70-positive tumor cells. Because NK cell migration was independent of cell-to-cell contact, the involvement of a soluble factor was assumed. Interestingly, synthetic Hsp70 protein and Hsp70 peptide TKD, mimicking surface-bound Hsp70, initiates migration of NK cells in a concentration-dependent (1-5 mug/ml), highly selective, and chemokine-independent manner. In summary, our results indicate that Hsp70 peptide TKD not only stimulates cytolysis but also chemotaxis in CD3(-)CD56(+)CD94(+) NK cells. The Journal of Immunology, 2004,172:972-980.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | NATURAL-KILLER-CELLS; SEVERE COMBINED IMMUNODEFICIENCY; HEAT-SHOCK-PROTEIN; TUMOR-NECROSIS-FACTOR; RECEPTORS; HSP70; LIVER; EXPRESSION; MICE; RECOGNITION; |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Innere Medizin III (Hämatologie und Internistische Onkologie) |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 02 Aug 2021 11:20 |
| Last Modified: | 02 Aug 2021 11:20 |
| URI: | https://pred.uni-regensburg.de/id/eprint/38077 |
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