Localization and quantitation of hsp84 in mammalian cells
In order to investigate the function of heat shock protein 84 (hsp84) we have isolated the protein from mouse neuroblastoma cells and raised a polyclonal antiserum which was affinity-purified. The specificity of the antibody was established by immunoprecipitation and immunoblotting. Immunofluorescen...
Ausführliche Beschreibung
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1988 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Experimental Cell Research - Amsterdam : Elsevier, 177(1988), 2, Seite 257-271 |
| Übergeordnetes Werk: |
volume:177 ; year:1988 ; number:2 ; pages:257-271 |
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| 520 | |a In order to investigate the function of heat shock protein 84 (hsp84) we have isolated the protein from mouse neuroblastoma cells and raised a polyclonal antiserum which was affinity-purified. The specificity of the antibody was established by immunoprecipitation and immunoblotting. Immunofluorescence studies revealed both a cytoplasmic and a nuclear localization of hsp84 in five different mammalian cell lines (mouse neuroblastoma cells and fibroblasts, rat hepatoma cells, and HeLa cells). In none of the five cell lines were found significant differences in the total cellular levels of hsp84 before and immediately after a heat shock (4 h, 42 ^oC) by immunoblot quantification. Furthermore after heat shock the fluorescence of anti-hsp84-labeled nuclei was increased relative to that of the surrounding cytopiasm. The increased fluorescence disappeared upon reincubation at 37 ^oC. The heat-induced increase in contrast between cytoplasmic and nuclear fluorescence could be explained by a combination of three factors: (a) decrease in nuclear projection area, (b) increase in cytoplasmic projection area, and (c) translocation of hsp84. The contribution of these factors to the increase after heat treatment was different for the cell lines. | ||
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(DE-627)NLEJ184352991 (DE-599)GBVNLZ184352991 DE-627 ger DE-627 rakwb eng Localization and quantitation of hsp84 in mammalian cells 1988 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In order to investigate the function of heat shock protein 84 (hsp84) we have isolated the protein from mouse neuroblastoma cells and raised a polyclonal antiserum which was affinity-purified. The specificity of the antibody was established by immunoprecipitation and immunoblotting. Immunofluorescence studies revealed both a cytoplasmic and a nuclear localization of hsp84 in five different mammalian cell lines (mouse neuroblastoma cells and fibroblasts, rat hepatoma cells, and HeLa cells). In none of the five cell lines were found significant differences in the total cellular levels of hsp84 before and immediately after a heat shock (4 h, 42 ^oC) by immunoblot quantification. Furthermore after heat shock the fluorescence of anti-hsp84-labeled nuclei was increased relative to that of the surrounding cytopiasm. The increased fluorescence disappeared upon reincubation at 37 ^oC. The heat-induced increase in contrast between cytoplasmic and nuclear fluorescence could be explained by a combination of three factors: (a) decrease in nuclear projection area, (b) increase in cytoplasmic projection area, and (c) translocation of hsp84. The contribution of these factors to the increase after heat treatment was different for the cell lines. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Berbers, G.A.M. oth Kunnen, R. oth van Bergen en Henegouwen, P.M.P. oth Wijk, R.v. oth in Experimental Cell Research Amsterdam : Elsevier 177(1988), 2, Seite 257-271 (DE-627)NLEJ177031808 (DE-600)1466780-0 0014-4827 nnns volume:177 year:1988 number:2 pages:257-271 http://dx.doi.org/10.1016/0014-4827(88)90460-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 177 1988 2 257-271 |
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(DE-627)NLEJ184352991 (DE-599)GBVNLZ184352991 DE-627 ger DE-627 rakwb eng Localization and quantitation of hsp84 in mammalian cells 1988 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In order to investigate the function of heat shock protein 84 (hsp84) we have isolated the protein from mouse neuroblastoma cells and raised a polyclonal antiserum which was affinity-purified. The specificity of the antibody was established by immunoprecipitation and immunoblotting. Immunofluorescence studies revealed both a cytoplasmic and a nuclear localization of hsp84 in five different mammalian cell lines (mouse neuroblastoma cells and fibroblasts, rat hepatoma cells, and HeLa cells). In none of the five cell lines were found significant differences in the total cellular levels of hsp84 before and immediately after a heat shock (4 h, 42 ^oC) by immunoblot quantification. Furthermore after heat shock the fluorescence of anti-hsp84-labeled nuclei was increased relative to that of the surrounding cytopiasm. The increased fluorescence disappeared upon reincubation at 37 ^oC. The heat-induced increase in contrast between cytoplasmic and nuclear fluorescence could be explained by a combination of three factors: (a) decrease in nuclear projection area, (b) increase in cytoplasmic projection area, and (c) translocation of hsp84. The contribution of these factors to the increase after heat treatment was different for the cell lines. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Berbers, G.A.M. oth Kunnen, R. oth van Bergen en Henegouwen, P.M.P. oth Wijk, R.v. oth in Experimental Cell Research Amsterdam : Elsevier 177(1988), 2, Seite 257-271 (DE-627)NLEJ177031808 (DE-600)1466780-0 0014-4827 nnns volume:177 year:1988 number:2 pages:257-271 http://dx.doi.org/10.1016/0014-4827(88)90460-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 177 1988 2 257-271 |
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(DE-627)NLEJ184352991 (DE-599)GBVNLZ184352991 DE-627 ger DE-627 rakwb eng Localization and quantitation of hsp84 in mammalian cells 1988 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In order to investigate the function of heat shock protein 84 (hsp84) we have isolated the protein from mouse neuroblastoma cells and raised a polyclonal antiserum which was affinity-purified. The specificity of the antibody was established by immunoprecipitation and immunoblotting. Immunofluorescence studies revealed both a cytoplasmic and a nuclear localization of hsp84 in five different mammalian cell lines (mouse neuroblastoma cells and fibroblasts, rat hepatoma cells, and HeLa cells). In none of the five cell lines were found significant differences in the total cellular levels of hsp84 before and immediately after a heat shock (4 h, 42 ^oC) by immunoblot quantification. Furthermore after heat shock the fluorescence of anti-hsp84-labeled nuclei was increased relative to that of the surrounding cytopiasm. The increased fluorescence disappeared upon reincubation at 37 ^oC. The heat-induced increase in contrast between cytoplasmic and nuclear fluorescence could be explained by a combination of three factors: (a) decrease in nuclear projection area, (b) increase in cytoplasmic projection area, and (c) translocation of hsp84. The contribution of these factors to the increase after heat treatment was different for the cell lines. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Berbers, G.A.M. oth Kunnen, R. oth van Bergen en Henegouwen, P.M.P. oth Wijk, R.v. oth in Experimental Cell Research Amsterdam : Elsevier 177(1988), 2, Seite 257-271 (DE-627)NLEJ177031808 (DE-600)1466780-0 0014-4827 nnns volume:177 year:1988 number:2 pages:257-271 http://dx.doi.org/10.1016/0014-4827(88)90460-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 177 1988 2 257-271 |
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(DE-627)NLEJ184352991 (DE-599)GBVNLZ184352991 DE-627 ger DE-627 rakwb eng Localization and quantitation of hsp84 in mammalian cells 1988 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In order to investigate the function of heat shock protein 84 (hsp84) we have isolated the protein from mouse neuroblastoma cells and raised a polyclonal antiserum which was affinity-purified. The specificity of the antibody was established by immunoprecipitation and immunoblotting. Immunofluorescence studies revealed both a cytoplasmic and a nuclear localization of hsp84 in five different mammalian cell lines (mouse neuroblastoma cells and fibroblasts, rat hepatoma cells, and HeLa cells). In none of the five cell lines were found significant differences in the total cellular levels of hsp84 before and immediately after a heat shock (4 h, 42 ^oC) by immunoblot quantification. Furthermore after heat shock the fluorescence of anti-hsp84-labeled nuclei was increased relative to that of the surrounding cytopiasm. The increased fluorescence disappeared upon reincubation at 37 ^oC. The heat-induced increase in contrast between cytoplasmic and nuclear fluorescence could be explained by a combination of three factors: (a) decrease in nuclear projection area, (b) increase in cytoplasmic projection area, and (c) translocation of hsp84. The contribution of these factors to the increase after heat treatment was different for the cell lines. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Berbers, G.A.M. oth Kunnen, R. oth van Bergen en Henegouwen, P.M.P. oth Wijk, R.v. oth in Experimental Cell Research Amsterdam : Elsevier 177(1988), 2, Seite 257-271 (DE-627)NLEJ177031808 (DE-600)1466780-0 0014-4827 nnns volume:177 year:1988 number:2 pages:257-271 http://dx.doi.org/10.1016/0014-4827(88)90460-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 177 1988 2 257-271 |
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(DE-627)NLEJ184352991 (DE-599)GBVNLZ184352991 DE-627 ger DE-627 rakwb eng Localization and quantitation of hsp84 in mammalian cells 1988 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In order to investigate the function of heat shock protein 84 (hsp84) we have isolated the protein from mouse neuroblastoma cells and raised a polyclonal antiserum which was affinity-purified. The specificity of the antibody was established by immunoprecipitation and immunoblotting. Immunofluorescence studies revealed both a cytoplasmic and a nuclear localization of hsp84 in five different mammalian cell lines (mouse neuroblastoma cells and fibroblasts, rat hepatoma cells, and HeLa cells). In none of the five cell lines were found significant differences in the total cellular levels of hsp84 before and immediately after a heat shock (4 h, 42 ^oC) by immunoblot quantification. Furthermore after heat shock the fluorescence of anti-hsp84-labeled nuclei was increased relative to that of the surrounding cytopiasm. The increased fluorescence disappeared upon reincubation at 37 ^oC. The heat-induced increase in contrast between cytoplasmic and nuclear fluorescence could be explained by a combination of three factors: (a) decrease in nuclear projection area, (b) increase in cytoplasmic projection area, and (c) translocation of hsp84. The contribution of these factors to the increase after heat treatment was different for the cell lines. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Berbers, G.A.M. oth Kunnen, R. oth van Bergen en Henegouwen, P.M.P. oth Wijk, R.v. oth in Experimental Cell Research Amsterdam : Elsevier 177(1988), 2, Seite 257-271 (DE-627)NLEJ177031808 (DE-600)1466780-0 0014-4827 nnns volume:177 year:1988 number:2 pages:257-271 http://dx.doi.org/10.1016/0014-4827(88)90460-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 177 1988 2 257-271 |
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Localization and quantitation of hsp84 in mammalian cells |
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In order to investigate the function of heat shock protein 84 (hsp84) we have isolated the protein from mouse neuroblastoma cells and raised a polyclonal antiserum which was affinity-purified. The specificity of the antibody was established by immunoprecipitation and immunoblotting. Immunofluorescence studies revealed both a cytoplasmic and a nuclear localization of hsp84 in five different mammalian cell lines (mouse neuroblastoma cells and fibroblasts, rat hepatoma cells, and HeLa cells). In none of the five cell lines were found significant differences in the total cellular levels of hsp84 before and immediately after a heat shock (4 h, 42 ^oC) by immunoblot quantification. Furthermore after heat shock the fluorescence of anti-hsp84-labeled nuclei was increased relative to that of the surrounding cytopiasm. The increased fluorescence disappeared upon reincubation at 37 ^oC. The heat-induced increase in contrast between cytoplasmic and nuclear fluorescence could be explained by a combination of three factors: (a) decrease in nuclear projection area, (b) increase in cytoplasmic projection area, and (c) translocation of hsp84. The contribution of these factors to the increase after heat treatment was different for the cell lines. |
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In order to investigate the function of heat shock protein 84 (hsp84) we have isolated the protein from mouse neuroblastoma cells and raised a polyclonal antiserum which was affinity-purified. The specificity of the antibody was established by immunoprecipitation and immunoblotting. Immunofluorescence studies revealed both a cytoplasmic and a nuclear localization of hsp84 in five different mammalian cell lines (mouse neuroblastoma cells and fibroblasts, rat hepatoma cells, and HeLa cells). In none of the five cell lines were found significant differences in the total cellular levels of hsp84 before and immediately after a heat shock (4 h, 42 ^oC) by immunoblot quantification. Furthermore after heat shock the fluorescence of anti-hsp84-labeled nuclei was increased relative to that of the surrounding cytopiasm. The increased fluorescence disappeared upon reincubation at 37 ^oC. The heat-induced increase in contrast between cytoplasmic and nuclear fluorescence could be explained by a combination of three factors: (a) decrease in nuclear projection area, (b) increase in cytoplasmic projection area, and (c) translocation of hsp84. The contribution of these factors to the increase after heat treatment was different for the cell lines. |
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In order to investigate the function of heat shock protein 84 (hsp84) we have isolated the protein from mouse neuroblastoma cells and raised a polyclonal antiserum which was affinity-purified. The specificity of the antibody was established by immunoprecipitation and immunoblotting. Immunofluorescence studies revealed both a cytoplasmic and a nuclear localization of hsp84 in five different mammalian cell lines (mouse neuroblastoma cells and fibroblasts, rat hepatoma cells, and HeLa cells). In none of the five cell lines were found significant differences in the total cellular levels of hsp84 before and immediately after a heat shock (4 h, 42 ^oC) by immunoblot quantification. Furthermore after heat shock the fluorescence of anti-hsp84-labeled nuclei was increased relative to that of the surrounding cytopiasm. The increased fluorescence disappeared upon reincubation at 37 ^oC. The heat-induced increase in contrast between cytoplasmic and nuclear fluorescence could be explained by a combination of three factors: (a) decrease in nuclear projection area, (b) increase in cytoplasmic projection area, and (c) translocation of hsp84. The contribution of these factors to the increase after heat treatment was different for the cell lines. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ184352991</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706230057.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1988 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ184352991</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ184352991</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Localization and quantitation of hsp84 in mammalian cells</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1988</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">In order to investigate the function of heat shock protein 84 (hsp84) we have isolated the protein from mouse neuroblastoma cells and raised a polyclonal antiserum which was affinity-purified. The specificity of the antibody was established by immunoprecipitation and immunoblotting. Immunofluorescence studies revealed both a cytoplasmic and a nuclear localization of hsp84 in five different mammalian cell lines (mouse neuroblastoma cells and fibroblasts, rat hepatoma cells, and HeLa cells). In none of the five cell lines were found significant differences in the total cellular levels of hsp84 before and immediately after a heat shock (4 h, 42 ^oC) by immunoblot quantification. Furthermore after heat shock the fluorescence of anti-hsp84-labeled nuclei was increased relative to that of the surrounding cytopiasm. The increased fluorescence disappeared upon reincubation at 37 ^oC. The heat-induced increase in contrast between cytoplasmic and nuclear fluorescence could be explained by a combination of three factors: (a) decrease in nuclear projection area, (b) increase in cytoplasmic projection area, and (c) translocation of hsp84. The contribution of these factors to the increase after heat treatment was different for the cell lines.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Berbers, G.A.M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kunnen, R.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">van Bergen en Henegouwen, P.M.P.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wijk, R.v.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Experimental Cell Research</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">177(1988), 2, Seite 257-271</subfield><subfield code="w">(DE-627)NLEJ177031808</subfield><subfield code="w">(DE-600)1466780-0</subfield><subfield code="x">0014-4827</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:177</subfield><subfield code="g">year:1988</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:257-271</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/0014-4827(88)90460-0</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">177</subfield><subfield code="j">1988</subfield><subfield code="e">2</subfield><subfield code="h">257-271</subfield></datafield></record></collection>
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