AI Article Synopsis
- Caspase-3 is a crucial enzyme involved in the process of apoptosis (programmed cell death) in mammalian cells, with gelsolin identified as one of its substrates.
- Gelsolin is cleaved by caspase-3 when cells are activated by Fas, and this cleavage disrupts actin filaments, affecting cell shape and movement.
- Mice lacking gelsolin demonstrate delayed signs of apoptosis, indicating that cleaved gelsolin plays a significant role in the changes that occur in cells during apoptosis.
Article Abstract
The caspase-3 (CPP32, apopain, YAMA) family of cysteinyl proteases has been implicated as key mediators of apoptosis in mammalian cells. Gelsolin was identified as a substrate for caspase-3 by screening the translation products of small complementary DNA pools for sensitivity to cleavage by caspase-3. Gelsolin was cleaved in vivo in a caspase-dependent manner in cells stimulated by Fas. Caspase-cleaved gelsolin severed actin filaments in vitro in a Ca2+-independent manner. Expression of the gelsolin cleavage product in multiple cell types caused the cells to round up, detach from the plate, and undergo nuclear fragmentation. Neutrophils isolated from mice lacking gelsolin had delayed onset of both blebbing and DNA fragmentation, following apoptosis induction, compared with wild-type neutrophils. Thus, cleaved gelsolin may be one physiological effector of morphologic change during apoptosis.
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| http://dx.doi.org/10.1126/science.278.5336.294 | DOI Listing |
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