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 ebook summarizes the final ten years' study on Alzheimer's disorder. Genetic mutations within the gene which codes for amyloid precursor protein (APP) have now been proven to reason Alzheimer's sickness in a few households. different genetic loci are actually being came across which relate to Alzheimer's disorder in a few households. knowing the traditional constitution and serve as of the APP gene product will ultimately offer avenues for constructing particular healing ideas designated on the amyloid deposition within the Alzheimer's illness mind. medicines which could inhibit or dissolve the amyloid, have an effect on the synthesis and proteolysis of APP, or which keep watch over 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
Thus, the solubilized peptide fractions cannot be regarded as stable solutions. , APC or ACA, is present (Hilbich et aL 1991). This conclusion was confirmed by the detection of f3A4 in cell culture media, blood plasma and cerebrospinal fluid (Seubert et aL 1992). A characterization of f3A4 has thus to discriminate between its solubilized and precipitated (solid) states. , f3A4 in its precipitated form. Secondary structure in the solid state was examined by IR spectroscopy of pep tides dispersed in dry KBr.
Is there functional homology between APPL and APP proteins? 5 kb predicts an 886 amino acid protein. In situ RNA localization data show that the Appl transcripts are found exclusively in post-mitotic neurons in all stages of development. They are not observed in neuronal precursor cells or in at least some and perhaps all glia. Appl transcripts are first observed in differentiating neurons, concomitant with axonal outgrowth, and continue to be expressed in mature neurons (Martin-Morris and While 1990).
1992; Seubert et al. 1992, 1993). Cell biological experiments have presented clues to the neurotoxicity of f3A4 peptides (Yankner et al. 1990; Mattson et al. 1992). Moreover, mutants of the APP gene have been isolated from patients suffering from familial Alzheimer's disease. Several amino acid substitutions have been identified in different families. Common to them all is their location close to or even within the f3A4 region (Hardy 1992 (review); Citron et al. 1992; Carter et al. 1992). Together these results strongly support the hypothesis that Alzheimer's disease is due to a metabolic defect of APP which results in the formation of f3A4 aggregates which, in turn, cause damage to growing neurons.