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By J. R. Atack (auth.), Prof. François Boller, Prof. Robert Katzman, Prof. André Rascol, Prof. Jean-Louis Signoret, Dr. Yves Christen (eds.)

This quantity offers the lawsuits of the symposium held in Toulouse on April 24, 1989, at the subject "Biological Markers of Alzheimer's illness. " This sym­ posium was once the fourth of a continual and winning sequence of Colloques Medecine et Recherche geared up via the Fondation IPSEN pour l. a. Recherche Therapeutique, addressing a variety of features of up to date examine within the box of Alzheimer's disorder (AD). The sequence began in September 1987 with "Im­ munology and Alzheimer's Disease," 6 months later in Paris by way of "Gene­ tics and Alzheimer's ailment" and in September 1988 in Montpellier by means of "Neuronal Grafting and Alzheimer's ailment. " the current symposium was once geared up for the aim of amassing the most up-tp-date principles bearing on organic markers of advert. The papers offered at this symposium could be approximately subdivided into 3 teams. the 1st offers with the markers of advert on the point of the mind itself. those markers are studied both throughout the cerebrospinal fluid or via strategies similar to nuclear magnetic resonance (NMR) - techniques which respectively objective at demonstrating the cerebral adjustments indicated via the particles because of the ailment, or learning the prospective neurochemical abnormalities that ensue within the past phases of AD.

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While many examples of alternative splicing of mRNA precursors have been documented, clearly demonstrated examples of regulation entirely by splice site selection and, by implication, trans-acting factors, are less numerous. Tau Phosphorylation Two features appear to predominate in studies of the posttranslational modifications of tau. One is that phophorylation is the only known posttranslational modification of tau. A second feature is that conformational changes, perhaps linked to phosphorylation events, must be considered in the design of protein level tau probes, and these changes are likely to have both biological and pathological implications.

Ossez, L. Buee, B. Hernon, M. Parent, A. Furby, D. Leys, M. Goudemand, A. Destee, and H. Petit Summary Tau proteins are the major antigenic component of PHF that accumulate in degenerating neurons in the brains of patients with AD. An abnormal phosphorylation of tau proteins has been suggested, but this is still under discussion. However, the mechanisms of incorporation of these normal cytoskeletal proteins in the PHF structure remain unknown. To obtain clues about the means by which tau proteins are modified during AD, we compared the tau immunodetection profile on immunoblots of brain homogenates from numerous Alzheimer patients versus numerous controls, using well-characterized antisera against human tau and against PHF.

Evidence is accumulating that deposits of beta-peptide amyloid fibers may precede formation of neuronal perikarya localized neurofibrillary tangles. The abnormal form of tau, a microtubule-associated protein shown to be part of the PHF, has also been shown by recent immunohistological studies to exist in a nontangle form (Bancher et al. 1989). We have used this information to develop ourPHF-protein diagnostic test which is based on the existence (1) of a soluble PHF-protein present in the CSF, which is in a ubiquitinated, unpolymerized form, Cerebrospinal Fluid-Based Laboratory Test for Alszheimer's Disease 25 and (2) on the observation that there is also an antigen in the CSF which reacts with anti-beta-peptide antibody.

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