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Thiamin and Alzheimer's disease.

J P Blass¹, K F Sheu, A J Cooper

¹Altshul Laboratory for Dementia Research, Cornell University Medical College, Burke Medical Research Institute, White Plains, NY 10605.

Journal of Nutritional Science and Vitaminology

|January 1, 1992

Summary

Alzheimer's disease (DAT) shows reduced activity in key thiamin pyrophosphate (TPP) dependent enzymes, particularly alpha-ketoglutarate dehydrogenase complex (KGDHC). This suggests a potential link between thiamin metabolism and DAT pathogenesis.

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Area of Science:

Neuroscience
Biochemistry
Metabolic Disorders

Background:

Clinical and neuropathological similarities exist between Alzheimer's disease (DAT) and Wernicke-Korsakoff syndrome (thiamin deficiency).
Thiamin pyrophosphate (TPP) is a crucial cofactor for several metabolic enzymes.

Purpose of the Study:

To investigate the role of TPP-dependent enzymes in the pathogenesis of DAT.
To compare enzyme activities in DAT brain tissue and cultured fibroblasts with controls.

Main Methods:

Assay of TPP-dependent enzyme activities (transketolase, pyruvate dehydrogenase complex, alpha-ketoglutarate dehydrogenase complex) in DAT brain and fibroblasts.
Structural and molecular studies of enzymes are ongoing.

Main Results:

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Reduced activities of transketolase (TK), pyruvate dehydrogenase complex (PDHC), and alpha-ketoglutarate dehydrogenase complex (KGDHC) were observed in DAT brain.
KGDHC activity was most significantly reduced (to <20% of normal) in DAT brain.
In fibroblasts, KGDHC activity was 50-60% of normal, TK activity 80-90%, and PDHC was normal.

Conclusions:

A lesion in KGDHC may contribute to the pathogenesis of DAT.
While thiamin treatment has not been definitively beneficial, further investigation into thiamin-dependent mechanisms in DAT is warranted.