By N. M. Hooper
A panel of hugely expert investigators describe intimately their cutting-edge biochemical, phone organic, and molecular organic thoughts for learning the molecular foundation of Alzheimer's illness. those simply reproducible, step by step equipment specialize in paintings with the amyloid precursor protein and the amyloidogenic peptide A?, but additionally include-with the hot id of presenilin proteins-techniques for identifying the constitution and organic functionality of those proteins. furthermore, there are chapters protecting the tau protein and its function in Alzheimer's sickness, in addition to an introductory dialogue of the heritage of the disorder, its genetic foundation, and the presently on hand and attainable destiny healing brokers. state of the art and huge ranging, Alzheimer's ailment: tools and Protocols presents prepared entry to confirmed, reproducible equipment for elucidating the molecular foundation of this most typical senile dementia.
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Additional resources for Alzheimer's Disease: Methods and Protocols (Methods in Molecular Medicine)
J. Neurochem. 63,495-500. 84. Goodman,Y. and Mattson, M. P. (1994) Secreted forms of P-amyloid precursor protein protect hippocampal neurons against amyloid P-peptide-induced oxidative injury. Exp. Neurol. 128,l-12. , Culwell, A. , Esch, F. , and Rydel, R. E. 85. Mattson, M. , Cheng, (1993) Evidence for excitoprotective and intraneuronal calcium-regulating roles Neuron (1993) 10,243-254. for secreted forms of the P-amyloid precursor protein. 86. Smith-Swintosky, V. , Pettigrew, L. , Craddock, S .
Therefore, it remains uncertain as to whether AP deposition is causally related to the disease process or represents a surrogate marker for some other more fundamental disturbance in neuronal metabolism. 6. 1. Molecular Genetics of the Presenilins Following the discoveryof mutations in APP and the fact that they were a rare causeof FAD, several groups undertook a survey of the remaining nonsex chromosomes excluding chromosomes 19 and 21. 3 (51-53). The gene was found to be highly conserved in evolution encoding what appears to be an integral membrane protein(seefollowing).
Rostagno, J. , Liem, P. , Gorevic, P. , and Frangione, B. (1992) A 109-amino-acid C-terminal fragment of Alzheimer’sdisease amyloid precursor protein contains a sequence, -RHDS-, that promotes cell adhesion. Biochem. J. 288,1053-1059. 80. Breen, K. , andAnderton, B. H. (1991) Beta amyloid precursor protein mediates neuronal cell-cell and cell-surface adhesion. J. Neurosci. Res. 28,90-100. 81. , Roch, J. , Sundsmo, M. , Otero, D. , and Saitoh, T,(1993) Amino acid sequence R E M S represents the active domain of amyloid PIA4 protein J.
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