Jun 15, 1996

Molecular physiology, biochemistry, and pharmacology of Alzheimer's amyloid precursor protein (APP)

Annals of the New York Academy of Sciences
Y H SuhM B Djamgoz

Abstract

The function of APP is not yet known in detail but growing evidence exists that APP may mediate cell interactions with the cell surface or soluble glycoproteins and defense mechanisms in the CNS involving the immune system. We describe here the finding that almost all CD4+ lymphocytes and the majority of CD8+ lymphocytes were positive for A beta and the antibodies against A beta or APP did not inhibit the [3H]-thymidine uptake of mitogen-treated lymphocytes significantly. There were no differences in the A beta immunoreactivity on the cell surface of lymphocytes between Alzheimer's disease (AD) and control samples. Excessive amyloidogenic pathway of APP processing may be the final common pathway involved in the pathogenesis of AD. Thus, the identification of proteases or factors leading to aberrant proteolysis which process APP to yield a variety of potentially amyloidogenic fragments would promise pharmacological targets to develop anti-AD drugs. In attempts to define the proteases or factors which alter the balance between nonamyloidogenic and amyloidogenic processing pathways, our study indicates that thrombin or acetylcholinesterase(AChE)-associated protease may be involved in the amyloidogenic processing pathway of APP in ...Continue Reading

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Mentioned in this Paper

Familial Alzheimer Disease (FAD)
Cessation of Life
Lymphoid Cells
Plaque, Amyloid
Alzheimer's Disease
Gene Expression
Polypeptides
Amyloid beta-Protein Precursor
Neurotoxicity Syndromes
Molecular Genetics (Discipline)

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