Advances in Research on Neurodegeneration: Volume 7 by C. L. Wellington, B. R. Leavitt (auth.), Prof. Y. Mizuno,

By C. L. Wellington, B. R. Leavitt (auth.), Prof. Y. Mizuno, Prof. D. B. Calne, Dr. R. Horowski, Prof. W. Poewe, Prof. P. Riederer, Prof. M. B. H. Youdim (eds.)

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Brain Res 799: 301-306 Autosomal-dominantly inherited forms of Parkinson's disease 39 Holthoff VA, Vieregge P, Kessler J, Pietrzyk U, Herholz K, Bonner J, Wagner R, Wienhard K, Pawlik G, Heiss WD (1994) Discordant twins with Parkinson's disease: positron emission tomography and early signs of impaired cognitive circuits. Ann Neurol36: 176-182 Ishikawa A , Takahashi H (1998) Clinical and neuropathological aspects of autosomal recessive juvenile parkinsonism. J Neurol 245: P4-9 Jensen PH, Nielsen MS, Jakes R, Dotti CG, Goedert M (1998) Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson 's disease mutation.

This model is very similar to one proposed for C. elegans, in which Ced-9 (Bel-2 homolog) binds to pro-Ced-3 (c. elegans caspase) through Ced-4 (Hengartner, 1997) (Fig. 1). Prevention of the release of mitochondrial apoptogenic factors by Bcl-2IBcl-x L Bel-2 and Bel-XL are localized in the mitochondiral membrane as well as in the endolasmic reticulum membrane and the nuelear envelope. Bel-2 and Bel-XL in the mitochondria have been attracting much attention and have been shown to prevent the apoptosis-associated mitochondrial changes such as loss of membrane potential, permeability transition (PT) and release of apoptogenic factor cytochrome c (Adams and Cory, 1998).

1997; reviewed by Adams and Cory, 1998). However, it still remains to be determined whether Bel-2 family proteins actually form ion channels in vivo and whether these proteins regulate apoptosis via the creation of ion channels. Thus, the life or death of a cell may be determined by Bel-2 family proteins in two ways, either through heterodimerization between anti-apoptotic and pro-apoptotic members, or through the independent functions of these proteins. , 1994). , 1995). , 1996), suggesting the improtant role of Bax in neuronal death.

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