Interaction of Heat Shock Protein 70 Peptidewith NK Cells Involves the NK Receptor CD94
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| 024 | 7 | 0 | |a 10.1515/BC.2003.030 |2 doi |
| 035 | |a (NATIONALLICENCE)gruyter-10.1515/BC.2003.030 | ||
| 245 | 0 | 0 | |a Interaction of Heat Shock Protein 70 Peptidewith NK Cells Involves the NK Receptor CD94 |h [Elektronische Daten] |c [C. Gross, D. Hansch, R. Gastpar, G. Multhoff] |
| 520 | 3 | |a Full-length Hsp70 protein (Hsp70) and the C-terminal domain of Hsp70 (Hsp70C) both stimulate the cytolytic activity of naive natural killer (NK) cells against Hsp70-positive tumor target cells. Here, we describe the characterization of Hsp70-NK cell interaction with binding studies using the human NK cell line YT. Binding of recombinant Hsp70 protein (Hsp70) and the C-terminal domain of Hsp70 (Hsp70C) to YT cells is demonstrated by immunofluorescence studies. A phenotypic characterization revealed that none of the recently described HSP-receptors (α 2-macroglobulin receptor CD91, Toll-like receptors 2, 4, 9, CD14) are expressed on YT cells. Only the C-type lectin receptor CD94 is commonly expressed by YT cells and Hsp70 reactive NK cells. A correlation of the cell density-dependent, variable CD94 expression and the binding capacity of Hsp70 was detected. Furthermore, Hsp70 binding could be completely abrogated by preincubation of YT cells with a CD94-specific antibody. Competition assays using either unlabeled Hsp70 protein or an unrelated protein (GST) in 20-fold excess and binding studies with escalating doses of Hsp70 protein provide evidence for a specific and concentration-dependent interaction of Hsp70 with YT cells. In addition to Hsp70 and Hsp70C, a 14-mer Hsp70 peptide termed TKD is known to exhibit comparable stimulatory properties on NK cells. Similar to fulllength Hsp70 protein (10 ug/ml-50 ug/ml), a specific binding of this peptide to YT cells was observed at 4C, at equivalent concentrations (2.0 ug/ml-8.0 ug/ml). Following a 30 min incubation period at 37C, membrane-bound Hsp70 protein and Hsp70 peptide TKD were completely taken up into the cytoplasm. | |
| 540 | |a Copyright © 2003 by Walter de Gruyter GmbH & Co. KG | ||
| 690 | 7 | |a Biochemistry |2 nationallicence | |
| 690 | 7 | |a Molecular biology |2 nationallicence | |
| 690 | 7 | |a Cellular biology |2 nationallicence | |
| 700 | 1 | |a Gross |D C. |4 aut | |
| 700 | 1 | |a Hansch |D D. |4 aut | |
| 700 | 1 | |a Gastpar |D R. |4 aut | |
| 700 | 1 | |a Multhoff |D G. |4 aut | |
| 773 | 0 | |t Biological Chemistry |d Walter de Gruyter |g 384/2(2003-02-20), 267-279 |x 1431-6730 |q 384:2<267 |1 2003 |2 384 |o bchm | |
| 856 | 4 | 0 | |u https://doi.org/10.1515/BC.2003.030 |q text/html |z Onlinezugriff via DOI |
| 908 | |D 1 |a research article |2 jats | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1515/BC.2003.030 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Gross |D C. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Hansch |D D. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Gastpar |D R. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Multhoff |D G. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Biological Chemistry |d Walter de Gruyter |g 384/2(2003-02-20), 267-279 |x 1431-6730 |q 384:2<267 |1 2003 |2 384 |o bchm | ||
| 900 | 7 | |b CC0 |u http://creativecommons.org/publicdomain/zero/1.0 |2 nationallicence | |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-gruyter | ||