By C. L. Masters, K. Beyreuther (auth.), C. L. Masters M.D., K. Beyreuther Ph.D., M. Trillet Prof., Y. Christen Ph.D. (eds.)

This publication summarizes the final ten years' examine on Alzheimer's ailment. Genetic mutations within the gene which codes for amyloid precursor protein (APP) have now been proven to reason Alzheimer's ailment in a few households. different genetic loci are actually being found which relate to Alzheimer's affliction in a few households. knowing the traditional constitution and serve as of the APP gene product will ultimately supply avenues for constructing particular healing techniques specified on the amyloid deposition within the Alzheimer's affliction mind. medications that can inhibit or dissolve the amyloid, impact the synthesis and proteolysis of APP, or which control the job of the APP gene all carry the promise of finally yielding an efficient therapy for Alzheimer's sickness.

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Identified the ligand for the sevenless receptor (Kramer et al. 1991), but also downstream elements such as Ras, guanine nucleotide exchange factor Sos, and SH2/SH3 domain containing factor drk (Simon et al. 1991, 1993; Oliver et al. 1993). , see Egan et al. 1993; Rozakis-Adcock et al. 1993; Li et al. 1993; Simon et al. 1993; Olivier et al. 1993). Examples like this make it reasonable for us to suggest that in future it should be possible to unearth molecules that interact with APPL in Drosophila, and also to use the Drosophila system to test physiological roles of interacting molecules implicated in APP function.

See Egan et al. 1993; Rozakis-Adcock et al. 1993; Li et al. 1993; Simon et al. 1993; Olivier et al. 1993). Examples like this make it reasonable for us to suggest that in future it should be possible to unearth molecules that interact with APPL in Drosophila, and also to use the Drosophila system to test physiological roles of interacting molecules implicated in APP function. Acknowledgments. W. We thank Patricia Parmenter for help in manuscript preparation. References Benzer S (1967) Behavioral mutants of Drosophila isolated by countercurrent distribution.

Miinch Med Wochenschr 69: 1537 Carter DA, Desmarais E, Bellis M, Campion D, Clerget-Darpoux F, Brice A, Agid Y, JaillardSerradt A, Mallet J (1992) More missense in amyloid gene: Nature Genet. 2: 255-256 Castano EM, Frangione B (1988). Biology of disease: human amyloidosis, Alzheimer disease and related disorders. Lab Invest. 58: 122-132 Castano, EM, Ghiso J, Prelli F, Gorevic PD, Migheli A, Frangione B (1986) In vitro formation of amyloid fibrils from two synthetic peptides of different lengths homologous to Alzheimer's disease fJ-protein.

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