Prevention of Vertebrate Neuronal Death by the crmA Gene

Abstract

Interleukin-1 beta converting enzyme (ICE) is a mammalian homolog of CED-3, a protein required for programmed cell death in the nematode Caenorhabditis elegans. The activity of ICE can be specifically inhibited by the product of crmA, a cytokine response modifier gene encoded by cowpox virus. Microinjection of the crmA gene into chicken dorsal root ganglion neurons was found to prevent cell death induced by deprivation of nerve growth factor. Thus, ICE is likely to participate in neuronal death in vertebrates.

Survivin initiates cell cycle entry by the competitive interaction with Cdk4/p16INK4a and Cdk2/Cyclin E complex activation

“…Compared with other IAP family members, such as crmA, p35, iap and ILP (Clem and Miller, 1994;Gagliardini et al, 1994;Miura et al, 1995;Xue and Horvitz, 1995;Duckett et al, 1996;Deveraux et al, 1997), Survivin contains a single baculovirus IAP repeat, lacks a carboxyl-terminal RING ®nger and is unique in that its expression is observed only in proliferating cells. Thus, possible involvement of Survivin in cell proliferation is suggested , however, the molecular details are not understood.…”

Bcl-2, Bcl-xL and adenovirus protein E1B19kD are functionally equivalent in their ability to inhibit cell death

“…No mammalian ced-4 homologue has been discovered thus far, but ced-3 encodes a cysteine protease related to the interleukin-1b converting enzyme (ICE) (Yuan et al, 1993) and ced-9 is a functional and structural homologue of bcl-2 (Vaux et al, 1992a;Hengartner and Horvitz, 1994b). Since apoptosis can be induced by overexpression of cysteine proteases (reviewed by Kumar, 1995) and blocked by pseudo-substrate inhibitors encoded by viruses (Gagliardini et al, 1994;Bump et al, 1995), it appears that cell death is initiated by proteolytic cleavage of one or several critical substrates. Thus, Bcl-2 and Ced-9 may function by blocking a step that leads to the activation or activity of cysteine proteases (Hengartner and Horvitz, 1994a;Cory, 1995;White, 1996).…”

Differential expression and translocation of protein tyrosine phosphatase 1B-related proteins in ME-180 tumor cells expressing apoptotic sensitivity and resistance to tumor necrosis factor: potential interaction with epidermal growth factor receptor

“…Several biological, physical and chemical mediators have been shown to contribute to the apoptotic signal. These include environmental stress induced through DNA damaging drugs (Dubrez et al, 1996;Lumelsky and Schwartz, 1996), radiation (Chen et al, 1996a;Santana et al, 1996), oxidation (Goossens et al, 1995;Wong et al, 1989) and growth factor withdrawal (Stefanis et al, 1996;Gagliardini et al, 1994). In addition, cytokines, such as TNF and Fas ligand, bind speci®c cell surface receptors and activate a cell death program (Nagata and Golstein, 1995;Cleveland and Ihle, 1995).…”