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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.

Type

Journal article

Journal

FEBS Lett

Publication Date

06/11/2002

Volume

531

Pages

168 - 172

Keywords

Apoptosis, Autophagy-Related Protein 5, Caspase 3, Caspases, Cross Reactions, Cytoskeletal Proteins, Genes, Fungal, HeLa Cells, Humans, Proteins, Proto-Oncogene Proteins c-jun, Recombinant Fusion Proteins, Saccharomyces cerevisiae Proteins, Ubiquitin-Protein Ligases