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Striatin is cleaved during apoptosis in a caspase‐3 mediated manner: a step towards novel biomarkers for apoptosis.

Recent reports showed that striatin (STRN) is a substrate for calpain2 and caspase‐3 in a model of traumatic brain injury, but its role in apoptosis remains uncertain. We found that striatin (110 kDa) is cleaved under different apoptotic stimuli (Staurosporine, etoposide, and TRAIL) in Hela cells and this cleavage (~60kDa) appeared mainly in the cytosolic fraction when compared to non‐cytosolic extracts (including mitochondria). Interestingly, staurosporine challenge of Hela cells decreased STRN levels in the non‐cytosolic fraction compared to the cytosolic fraction implying a shuttling of STRN under during apoptosis. Pharmacological treatment with the general caspase inhibitor z‐VAD.fmk abolished the cleavage of striatin in total cell lysates and in the cytosolic fraction of apoptotic Hela cells. While staurosporine was unable to significantly cleave STRN in cells lacking caspase‐3 (MCF‐7), overexpression of active or mutant (inactive) form of caspase‐3 resulted in cleavage of STRN (Western blot). Interestingly, this cleavage was also abolished by the pretreatment of MCF‐7 cells with z‐VAD.fmk. Collectively, our data suggest that STRN is cleaved during apoptosis in a caspase‐3 related manner and emerges as a novel marker for apoptosis.