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      Lens Fibre Cell Differentiation – A Link with Apoptosis?

      Ophthalmic Research

      S. Karger AG

      Apoptosis, Programmed cell death, Lens fibre cell differentiation, Denucleation

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          During the process of terminal differentiation, the fibre cells in the eye lens undergo many changes that are reminiscent of apoptotic/necrotic changes. Mitochondria, for instance, undergo permeability transition and nuclear degradation is accompanied by chromatin condensation, disintegration of the nucleolus, dissolution of the nuclear lamina, nuclear pore clustering and fragmentation of the DNA into oligonucleosomal fragments. As during apoptosis, members of the caspase family of proteases were shown to be active during fibre cell differentiation and Bcl-2 overexpression was demonstrated to block normal differentiation of lens cells. In this review, the current knowledge of the sequence of events during cell death is summarised and contrasted with events during lens fibre cell differentiation. Due to the numerous similarities between these processes, lens fibre cell differentiation is suggested to represent an attenuated form of cell death.

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          Most cited references 38

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          Mice deficient for p53 are developmentally normal but susceptible to spontaneous tumours.

          Mutations in the p53 tumour-suppressor gene are the most frequently observed genetic lesions in human cancers. To investigate the role of the p53 gene in mammalian development and tumorigenesis, a null mutation was introduced into the gene by homologous recombination in murine embryonic stem cells. Mice homozygous for the null allele appear normal but are prone to the spontaneous development of a variety of neoplasms by 6 months of age. These observations indicate that a normal p53 gene is dispensable for embryonic development, that its absence predisposes the animal to neoplastic disease, and that an oncogenic mutant form of p53 is not obligatory for the genesis of many types of tumours.
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            Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis.

            The protease responsible for the cleavage of poly(ADP-ribose) polymerase and necessary for apoptosis has been purified and characterized. This enzyme, named apopain, is composed of two subunits of relative molecular mass (M(r)) 17K and 12K that are derived from a common proenzyme identified as CPP32. This proenzyme is related to interleukin-1 beta-converting enzyme (ICE) and CED-3, the product of a gene required for programmed cell death in Caenorhabditis elegans. A potent peptide aldehyde inhibitor has been developed and shown to prevent apoptotic events in vitro, suggesting that apopain/CPP32 is important for the initiation of apoptotic cell death.
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              Caspases: intracellular signaling by proteolysis.

               V M Dixit,  G Salvesen (1997)

                Author and article information

                Ophthalmic Res
                Ophthalmic Research
                S. Karger AG
                June 1999
                30 April 1999
                : 31
                : 3
                : 163-183
                Department of Biochemistry, Medical Sciences Institute, University of Dundee, UK
                55530 Ophthalmic Res 1999;31:163–183
                © 1999 S. Karger AG, Basel

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                Page count
                Figures: 2, Tables: 2, References: 149, Pages: 21


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