Amyloid Protein Precursor in Development, Aging and by C. L. Masters, K. Beyreuther (auth.), C. L. Masters M.D., K.

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 e-book 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 illness in a few households. different genetic loci at the moment are being came upon which relate to Alzheimer's disorder in a few households. realizing the conventional constitution and serve as of the APP gene product will finally offer avenues for constructing particular healing techniques unique on the amyloid deposition within the Alzheimer's sickness mind. medicinal drugs that may inhibit or dissolve the amyloid, impact the synthesis and proteolysis of APP, or which keep an eye on the job of the APP gene all carry the promise of ultimately yielding an efficient remedy for Alzheimer's illness.

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Additional info for Amyloid Protein Precursor in Development, Aging and Alzheimer's Disease (Research and Perspectives in Alzheimer's Disease)

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1962; Cooper 1974). This property is correlated to the existence of extended f3-pleated sheet structure within insoluble peptide aggregates: it is also detected in poly-L-Iysine when it adopts a f3-sheet structure after heating (Glenner et al. 1972). These results further corroborate the assumption that a f3-pleated sheet conformation (leading to the formation of filamentous aggregates) is the ultrastructural commonality behind all types of amyloid (for reviews see Glenner 1980; Castafio and Frangione 1988).

However, as this hydrophobic region is of high importance for the structure of f3A4, substitutions might also result in variants with increased amyloidogenicity. In a family suffering from Alzheimer's disease and cerebral hemorrhage, Hendrick et al. (1992) identified an APP mutation that leads to a substitution of alanine 21 by glycine. It might well be that this substitution results in a stabilization of the hydrophobic core and, consequently, of f3A4 aggregates. The synthesis of f3A4 analogue pep tides FF -+ GI and FF -+ TT which can inhibit filament formation in vitro opens a possibility for therapeutic approaches.

Grund and S. Pinto are gratefully acknowledged. This work was supported by the Federal Ministry of Science and Technology and the "Fonds der Chemischen Industrie". References Bennhold H (1992) Eine spezifische Amyloidfarbung mit Kongorot. 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.

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