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Apoptosis‐specific protein (ASP 45 kDa) is distinct from human Apg5, the homologue of the yeast autophagic gene apg5
Author(s) -
Yung Hong Wa,
Xue Luzheng,
Tolkovsky Aviva M
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03497-x
Subject(s) - staurosporine , cycloheximide , hela , apoptosis , microbiology and biotechnology , yeast , gene , biology , chemistry , biochemistry , protein biosynthesis , cell , enzyme , protein kinase a
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 ∼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 TNFα/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 (∼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.