Apoptosis-specific protein (ASP 45 kDa) is distinct from human Apg5, the homologue of the yeast autophagic gene apg5.

Journal article

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.

Authors: Yung, H; Xue, L; Tolkovsky, A

• Journal: FEBS letters
• Volume: 531
• Issue: 2
• Pages: 168-172
• Publication date: 2002-11-01
• DOI: 10.1016/s0014-5793(02)03497-x
• EISSN: 1873-3468
• ISSN: 0014-5793
• Language: English
• Keywords: Hela Cells; Recombinant Fusion Proteins; Caspases; Cytoskeletal Proteins; Caspase 3; Apoptosis; Proto-Oncogene Proteins c-jun; Humans; Genes, Fungal; Proteins; Saccharomyces cerevisiae Proteins; Cross Reactions