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Caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides
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| Zeitschriftentitel: | FEBS Letters |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | FEBS Letters, 555, 2003, 2, S. 380-384 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Giri, Kalyan Ghosh, Utpal Bhattacharyya, Nitai P Basak, Soumen Giri, Kalyan Ghosh, Utpal Bhattacharyya, Nitai P Basak, Soumen |
|---|---|
| author |
Giri, Kalyan Ghosh, Utpal Bhattacharyya, Nitai P Basak, Soumen |
| spellingShingle |
Giri, Kalyan Ghosh, Utpal Bhattacharyya, Nitai P Basak, Soumen FEBS Letters Caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| author_sort |
giri, kalyan |
| spelling |
Giri, Kalyan Ghosh, Utpal Bhattacharyya, Nitai P Basak, Soumen 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/s0014-5793(03)01294-8 <jats:p>Expansion of a polyalanine stretch from 10 to 12–17 residues in the N‐terminus of the protein PABP2 has been implicated in the genetically acquired disease oculopharyngeal muscular dystrophy, characterized by nuclear protein deposits. Here we report a correlation between the structural properties and cell toxicity of two peptides mimicking the N‐terminal domain of PABP2: one containing seven and the other 11 uninterrupted alanine residues. Consistent with earlier observations, the longer peptide (11‐ala) was found to adopt β‐sheet structure while the shorter one (7‐ala) formed α‐helix over a wide range of concentrations (∼20–500 μM). We observed that treatment with 11‐ala resulted in significantly enhanced death of Chinese hamster V79 cells, compared to the effect of treatment with 7‐ala, via the cytochrome <jats:italic>c</jats:italic> mediated apoptotic pathway. Increases in caspase 8 and caspase 3 activity were also observed in human cells (K562) treated with 11‐ala. These results indicate that the toxicity of pathogenic peptides is directly linked to their β‐sheet structure and also support recent observations that small oligomeric species of peptides and proteins are the key toxic elements in causing protein aggregation diseases.</jats:p> Caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides FEBS Letters |
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Wiley, 2003 |
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FEBS Letters |
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| title |
Caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides |
| title_unstemmed |
Caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides |
| title_full |
Caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides |
| title_fullStr |
Caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides |
| title_full_unstemmed |
Caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides |
| title_short |
Caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides |
| title_sort |
caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides |
| topic |
Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| url |
http://dx.doi.org/10.1016/s0014-5793(03)01294-8 |
| publishDate |
2003 |
| physical |
380-384 |
| description |
<jats:p>Expansion of a polyalanine stretch from 10 to 12–17 residues in the N‐terminus of the protein PABP2 has been implicated in the genetically acquired disease oculopharyngeal muscular dystrophy, characterized by nuclear protein deposits. Here we report a correlation between the structural properties and cell toxicity of two peptides mimicking the N‐terminal domain of PABP2: one containing seven and the other 11 uninterrupted alanine residues. Consistent with earlier observations, the longer peptide (11‐ala) was found to adopt β‐sheet structure while the shorter one (7‐ala) formed α‐helix over a wide range of concentrations (∼20–500 μM). We observed that treatment with 11‐ala resulted in significantly enhanced death of Chinese hamster V79 cells, compared to the effect of treatment with 7‐ala, via the cytochrome <jats:italic>c</jats:italic> mediated apoptotic pathway. Increases in caspase 8 and caspase 3 activity were also observed in human cells (K562) treated with 11‐ala. These results indicate that the toxicity of pathogenic peptides is directly linked to their β‐sheet structure and also support recent observations that small oligomeric species of peptides and proteins are the key toxic elements in causing protein aggregation diseases.</jats:p> |
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| author | Giri, Kalyan, Ghosh, Utpal, Bhattacharyya, Nitai P, Basak, Soumen |
| author_facet | Giri, Kalyan, Ghosh, Utpal, Bhattacharyya, Nitai P, Basak, Soumen, Giri, Kalyan, Ghosh, Utpal, Bhattacharyya, Nitai P, Basak, Soumen |
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| description | <jats:p>Expansion of a polyalanine stretch from 10 to 12–17 residues in the N‐terminus of the protein PABP2 has been implicated in the genetically acquired disease oculopharyngeal muscular dystrophy, characterized by nuclear protein deposits. Here we report a correlation between the structural properties and cell toxicity of two peptides mimicking the N‐terminal domain of PABP2: one containing seven and the other 11 uninterrupted alanine residues. Consistent with earlier observations, the longer peptide (11‐ala) was found to adopt β‐sheet structure while the shorter one (7‐ala) formed α‐helix over a wide range of concentrations (∼20–500 μM). We observed that treatment with 11‐ala resulted in significantly enhanced death of Chinese hamster V79 cells, compared to the effect of treatment with 7‐ala, via the cytochrome <jats:italic>c</jats:italic> mediated apoptotic pathway. Increases in caspase 8 and caspase 3 activity were also observed in human cells (K562) treated with 11‐ala. These results indicate that the toxicity of pathogenic peptides is directly linked to their β‐sheet structure and also support recent observations that small oligomeric species of peptides and proteins are the key toxic elements in causing protein aggregation diseases.</jats:p> |
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| imprint | Wiley, 2003 |
| imprint_str_mv | Wiley, 2003 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Rs1, DE-Pl11, DE-105, DE-14, DE-Ch1, DE-L229 |
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| physical | 380-384 |
| publishDate | 2003 |
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| series | FEBS Letters |
| source_id | 49 |
| spelling | Giri, Kalyan Ghosh, Utpal Bhattacharyya, Nitai P Basak, Soumen 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/s0014-5793(03)01294-8 <jats:p>Expansion of a polyalanine stretch from 10 to 12–17 residues in the N‐terminus of the protein PABP2 has been implicated in the genetically acquired disease oculopharyngeal muscular dystrophy, characterized by nuclear protein deposits. Here we report a correlation between the structural properties and cell toxicity of two peptides mimicking the N‐terminal domain of PABP2: one containing seven and the other 11 uninterrupted alanine residues. Consistent with earlier observations, the longer peptide (11‐ala) was found to adopt β‐sheet structure while the shorter one (7‐ala) formed α‐helix over a wide range of concentrations (∼20–500 μM). We observed that treatment with 11‐ala resulted in significantly enhanced death of Chinese hamster V79 cells, compared to the effect of treatment with 7‐ala, via the cytochrome <jats:italic>c</jats:italic> mediated apoptotic pathway. Increases in caspase 8 and caspase 3 activity were also observed in human cells (K562) treated with 11‐ala. These results indicate that the toxicity of pathogenic peptides is directly linked to their β‐sheet structure and also support recent observations that small oligomeric species of peptides and proteins are the key toxic elements in causing protein aggregation diseases.</jats:p> Caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides FEBS Letters |
| spellingShingle | Giri, Kalyan, Ghosh, Utpal, Bhattacharyya, Nitai P, Basak, Soumen, FEBS Letters, Caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides, Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| title | Caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides |
| title_full | Caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides |
| title_fullStr | Caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides |
| title_full_unstemmed | Caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides |
| title_short | Caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides |
| title_sort | caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides |
| title_unstemmed | Caspase 8 mediated apoptotic cell death induced by β‐sheet forming polyalanine peptides |
| topic | Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| url | http://dx.doi.org/10.1016/s0014-5793(03)01294-8 |