Apoptosis-specific protein (ASP 45 kDa) is distinct from human Apg5, the homologue of the yeast autophagic gene apg5.
We have examined whether the apoptosis-specific protein p45ASP and human Apg5 are identical proteins. Like p45ASP, myc-hApg5 cross-reacted with a c-Jun antibody and approximately 50% of myc-hApg5 was bound to a Triton X-100-insoluble fraction in HeLa cells. However, soluble myc-hApg5 was degraded du...
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Format: | Journal article |
Language: | English |
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2002
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author | Yung, H Xue, L Tolkovsky, A |
author_facet | Yung, H Xue, L Tolkovsky, A |
author_sort | Yung, H |
collection | OXFORD |
description | We have examined whether the apoptosis-specific protein p45ASP and human Apg5 are identical proteins. Like p45ASP, myc-hApg5 cross-reacted with a c-Jun antibody and approximately 50% of myc-hApg5 was bound to a Triton X-100-insoluble fraction in HeLa cells. However, soluble myc-hApg5 was degraded during apoptosis induced by staurosporine or TNFalpha/cycloheximide whilst expression of soluble p45ASP was stabilised. Furthermore, myc-hApg5 degradation was blocked by the caspase inhibitor Boc-Asp(OMe)FMK whilst p45ASP expression was eliminated. Moreover, myc-hApg5 ( approximately 32 kDa) never assumed the size of p45ASP (45 kDa). It is therefore likely that p45ASP and human Apg5 are distinct proteins although they do share some common characteristics. |
first_indexed | 2024-03-07T03:37:59Z |
format | Journal article |
id | oxford-uuid:bcece0d1-9926-4a61-85e7-0ebf4e7df55d |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T03:37:59Z |
publishDate | 2002 |
record_format | dspace |
spelling | oxford-uuid:bcece0d1-9926-4a61-85e7-0ebf4e7df55d2022-03-27T05:28:00ZApoptosis-specific protein (ASP 45 kDa) is distinct from human Apg5, the homologue of the yeast autophagic gene apg5.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:bcece0d1-9926-4a61-85e7-0ebf4e7df55dEnglishSymplectic Elements at Oxford2002Yung, HXue, LTolkovsky, AWe have examined whether the apoptosis-specific protein p45ASP and human Apg5 are identical proteins. Like p45ASP, myc-hApg5 cross-reacted with a c-Jun antibody and approximately 50% of myc-hApg5 was bound to a Triton X-100-insoluble fraction in HeLa cells. However, soluble myc-hApg5 was degraded during apoptosis induced by staurosporine or TNFalpha/cycloheximide whilst expression of soluble p45ASP was stabilised. Furthermore, myc-hApg5 degradation was blocked by the caspase inhibitor Boc-Asp(OMe)FMK whilst p45ASP expression was eliminated. Moreover, myc-hApg5 ( approximately 32 kDa) never assumed the size of p45ASP (45 kDa). It is therefore likely that p45ASP and human Apg5 are distinct proteins although they do share some common characteristics. |
spellingShingle | Yung, H Xue, L Tolkovsky, A Apoptosis-specific protein (ASP 45 kDa) is distinct from human Apg5, the homologue of the yeast autophagic gene apg5. |
title | Apoptosis-specific protein (ASP 45 kDa) is distinct from human Apg5, the homologue of the yeast autophagic gene apg5. |
title_full | Apoptosis-specific protein (ASP 45 kDa) is distinct from human Apg5, the homologue of the yeast autophagic gene apg5. |
title_fullStr | Apoptosis-specific protein (ASP 45 kDa) is distinct from human Apg5, the homologue of the yeast autophagic gene apg5. |
title_full_unstemmed | Apoptosis-specific protein (ASP 45 kDa) is distinct from human Apg5, the homologue of the yeast autophagic gene apg5. |
title_short | Apoptosis-specific protein (ASP 45 kDa) is distinct from human Apg5, the homologue of the yeast autophagic gene apg5. |
title_sort | apoptosis specific protein asp 45 kda is distinct from human apg5 the homologue of the yeast autophagic gene apg5 |
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