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Bid truncation mediated by caspases-3 and -9 in vinorelbine-induced apoptosis
Vinorelbine is a chemotherapeutic vinca alkaloid clinically prescribed for non-small cell lung cancer and breast cancer. Here we studied the mechanism for vinorelbine-induced apoptosis in a human T-cell lymphoma. Although vinorelbine induces DNA fragmentation that is inhibited by specific peptide in...
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| Published in: | Apoptosis (London) 2008-04, Vol.13 (4), p.523-530 |
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| cites | cdi_FETCH-LOGICAL-c490t-4fea7b8aeab77a807e7808837000079df41f5a09147ebeefdbc2eb76e0ea32e23 |
| container_end_page | 530 |
| container_issue | 4 |
| container_start_page | 523 |
| container_title | Apoptosis (London) |
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| creator | Hayakawa, Akemi Kawamoto, Yoshiyuki Nakajima, Hiroo Sakai, Jun-ichi Takasawa, Ryoko Nakashima, Izumi Magae, Junji Tanuma, Sei-ichi |
| description | Vinorelbine is a chemotherapeutic vinca alkaloid clinically prescribed for non-small cell lung cancer and breast cancer. Here we studied the mechanism for vinorelbine-induced apoptosis in a human T-cell lymphoma. Although vinorelbine induces DNA fragmentation that is inhibited by specific peptide inhibitors for caspases-9 and -3 in Jurkat cells, caspase-8 deficiency retards vinorelbine-induced apoptosis. Activation of caspase-8 is also observed in vinorelbine-treated cells, and the activity is diminished when the caspase-3 activity is blocked by a specific peptide inhibitor, Ac-DNLC-CHO. Blocking of the Fas receptor with an antagonistic anti-Fas antibody does not affect vinorelbine-induced DNA fragmentation. These results suggest that vinorelbine-induced apoptosis is enhanced by the activation of caspase-8 via caspase-9-mediated activation of caspase-3, but not through a Fas-triggered signal. Western blotting suggests that vinorelbine cleaves caspase-3, -9 and -8 and reduces the amount of mitochondrial cytochrome c. Caspase-8 deficiency suppresses all of these events. A downstream substrate for caspase-8, Bid, is also cleaved in vinorelbine-treated cells, but the Bid truncation is also observed in caspase-8-deficient Jurkat cells. Importantly, recombinant caspases-3 and -9, as well as caspase-8, directly cleaves recombinant Bid in vitro. These results suggest that caspases-3 and -9 participate in Bid truncation, indicating a new mechanism for vinorelbine-induces apoptosis. |
| doi_str_mv | 10.1007/s10495-008-0184-y |
| format | article |
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Here we studied the mechanism for vinorelbine-induced apoptosis in a human T-cell lymphoma. Although vinorelbine induces DNA fragmentation that is inhibited by specific peptide inhibitors for caspases-9 and -3 in Jurkat cells, caspase-8 deficiency retards vinorelbine-induced apoptosis. Activation of caspase-8 is also observed in vinorelbine-treated cells, and the activity is diminished when the caspase-3 activity is blocked by a specific peptide inhibitor, Ac-DNLC-CHO. Blocking of the Fas receptor with an antagonistic anti-Fas antibody does not affect vinorelbine-induced DNA fragmentation. These results suggest that vinorelbine-induced apoptosis is enhanced by the activation of caspase-8 via caspase-9-mediated activation of caspase-3, but not through a Fas-triggered signal. Western blotting suggests that vinorelbine cleaves caspase-3, -9 and -8 and reduces the amount of mitochondrial cytochrome c. Caspase-8 deficiency suppresses all of these events. A downstream substrate for caspase-8, Bid, is also cleaved in vinorelbine-treated cells, but the Bid truncation is also observed in caspase-8-deficient Jurkat cells. Importantly, recombinant caspases-3 and -9, as well as caspase-8, directly cleaves recombinant Bid in vitro. These results suggest that caspases-3 and -9 participate in Bid truncation, indicating a new mechanism for vinorelbine-induces apoptosis.</description><identifier>ISSN: 1360-8185</identifier><identifier>EISSN: 1573-675X</identifier><identifier>DOI: 10.1007/s10495-008-0184-y</identifier><identifier>PMID: 18297401</identifier><language>eng</language><publisher>Boston: Boston : Springer US</publisher><subject>Apoptosis - drug effects ; BH3 Interacting Domain Death Agonist Protein - metabolism ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Cancer Research ; Caspase 3 - physiology ; Caspase 8 - physiology ; Caspase 9 - physiology ; Cell Biology ; Cell Line, Tumor ; Cytochromes c - metabolism ; Deoxyribonucleic acid ; DNA ; Humans ; Jurkat Cells ; Lung cancer ; Lymphoma ; Lymphoma, T-Cell - drug therapy ; Lymphoma, T-Cell - pathology ; Oncology ; Original Paper ; Vinblastine - analogs & derivatives ; Vinblastine - pharmacology ; Vinblastine - therapeutic use ; Vinca ; Virology</subject><ispartof>Apoptosis (London), 2008-04, Vol.13 (4), p.523-530</ispartof><rights>Springer Science+Business Media, LLC 2008</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c490t-4fea7b8aeab77a807e7808837000079df41f5a09147ebeefdbc2eb76e0ea32e23</citedby><cites>FETCH-LOGICAL-c490t-4fea7b8aeab77a807e7808837000079df41f5a09147ebeefdbc2eb76e0ea32e23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,783,787,27938,27939</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18297401$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hayakawa, Akemi</creatorcontrib><creatorcontrib>Kawamoto, Yoshiyuki</creatorcontrib><creatorcontrib>Nakajima, Hiroo</creatorcontrib><creatorcontrib>Sakai, Jun-ichi</creatorcontrib><creatorcontrib>Takasawa, Ryoko</creatorcontrib><creatorcontrib>Nakashima, Izumi</creatorcontrib><creatorcontrib>Magae, Junji</creatorcontrib><creatorcontrib>Tanuma, Sei-ichi</creatorcontrib><title>Bid truncation mediated by caspases-3 and -9 in vinorelbine-induced apoptosis</title><title>Apoptosis (London)</title><addtitle>Apoptosis</addtitle><addtitle>Apoptosis</addtitle><description>Vinorelbine is a chemotherapeutic vinca alkaloid clinically prescribed for non-small cell lung cancer and breast cancer. Here we studied the mechanism for vinorelbine-induced apoptosis in a human T-cell lymphoma. Although vinorelbine induces DNA fragmentation that is inhibited by specific peptide inhibitors for caspases-9 and -3 in Jurkat cells, caspase-8 deficiency retards vinorelbine-induced apoptosis. Activation of caspase-8 is also observed in vinorelbine-treated cells, and the activity is diminished when the caspase-3 activity is blocked by a specific peptide inhibitor, Ac-DNLC-CHO. Blocking of the Fas receptor with an antagonistic anti-Fas antibody does not affect vinorelbine-induced DNA fragmentation. These results suggest that vinorelbine-induced apoptosis is enhanced by the activation of caspase-8 via caspase-9-mediated activation of caspase-3, but not through a Fas-triggered signal. Western blotting suggests that vinorelbine cleaves caspase-3, -9 and -8 and reduces the amount of mitochondrial cytochrome c. Caspase-8 deficiency suppresses all of these events. A downstream substrate for caspase-8, Bid, is also cleaved in vinorelbine-treated cells, but the Bid truncation is also observed in caspase-8-deficient Jurkat cells. Importantly, recombinant caspases-3 and -9, as well as caspase-8, directly cleaves recombinant Bid in vitro. These results suggest that caspases-3 and -9 participate in Bid truncation, indicating a new mechanism for vinorelbine-induces apoptosis.</description><subject>Apoptosis - drug effects</subject><subject>BH3 Interacting Domain Death Agonist Protein - metabolism</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cancer Research</subject><subject>Caspase 3 - physiology</subject><subject>Caspase 8 - physiology</subject><subject>Caspase 9 - physiology</subject><subject>Cell Biology</subject><subject>Cell Line, Tumor</subject><subject>Cytochromes c - metabolism</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>Humans</subject><subject>Jurkat Cells</subject><subject>Lung cancer</subject><subject>Lymphoma</subject><subject>Lymphoma, T-Cell - drug therapy</subject><subject>Lymphoma, T-Cell - pathology</subject><subject>Oncology</subject><subject>Original Paper</subject><subject>Vinblastine - 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Academic</collection><jtitle>Apoptosis (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hayakawa, Akemi</au><au>Kawamoto, Yoshiyuki</au><au>Nakajima, Hiroo</au><au>Sakai, Jun-ichi</au><au>Takasawa, Ryoko</au><au>Nakashima, Izumi</au><au>Magae, Junji</au><au>Tanuma, Sei-ichi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bid truncation mediated by caspases-3 and -9 in vinorelbine-induced apoptosis</atitle><jtitle>Apoptosis (London)</jtitle><stitle>Apoptosis</stitle><addtitle>Apoptosis</addtitle><date>2008-04-01</date><risdate>2008</risdate><volume>13</volume><issue>4</issue><spage>523</spage><epage>530</epage><pages>523-530</pages><issn>1360-8185</issn><eissn>1573-675X</eissn><notes>http://dx.doi.org/10.1007/s10495-008-0184-y</notes><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>Vinorelbine is a chemotherapeutic vinca alkaloid clinically prescribed for non-small cell lung cancer and breast cancer. Here we studied the mechanism for vinorelbine-induced apoptosis in a human T-cell lymphoma. Although vinorelbine induces DNA fragmentation that is inhibited by specific peptide inhibitors for caspases-9 and -3 in Jurkat cells, caspase-8 deficiency retards vinorelbine-induced apoptosis. Activation of caspase-8 is also observed in vinorelbine-treated cells, and the activity is diminished when the caspase-3 activity is blocked by a specific peptide inhibitor, Ac-DNLC-CHO. Blocking of the Fas receptor with an antagonistic anti-Fas antibody does not affect vinorelbine-induced DNA fragmentation. These results suggest that vinorelbine-induced apoptosis is enhanced by the activation of caspase-8 via caspase-9-mediated activation of caspase-3, but not through a Fas-triggered signal. Western blotting suggests that vinorelbine cleaves caspase-3, -9 and -8 and reduces the amount of mitochondrial cytochrome c. Caspase-8 deficiency suppresses all of these events. A downstream substrate for caspase-8, Bid, is also cleaved in vinorelbine-treated cells, but the Bid truncation is also observed in caspase-8-deficient Jurkat cells. Importantly, recombinant caspases-3 and -9, as well as caspase-8, directly cleaves recombinant Bid in vitro. These results suggest that caspases-3 and -9 participate in Bid truncation, indicating a new mechanism for vinorelbine-induces apoptosis.</abstract><cop>Boston</cop><pub>Boston : Springer US</pub><pmid>18297401</pmid><doi>10.1007/s10495-008-0184-y</doi><tpages>8</tpages></addata></record> |
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| subjects | Apoptosis - drug effects BH3 Interacting Domain Death Agonist Protein - metabolism Biochemistry Biomedical and Life Sciences Biomedicine Cancer Research Caspase 3 - physiology Caspase 8 - physiology Caspase 9 - physiology Cell Biology Cell Line, Tumor Cytochromes c - metabolism Deoxyribonucleic acid DNA Humans Jurkat Cells Lung cancer Lymphoma Lymphoma, T-Cell - drug therapy Lymphoma, T-Cell - pathology Oncology Original Paper Vinblastine - analogs & derivatives Vinblastine - pharmacology Vinblastine - therapeutic use Vinca Virology |
| title | Bid truncation mediated by caspases-3 and -9 in vinorelbine-induced apoptosis |
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