Abstract
Commercially available medicinal plant extracts such as Ginkgo biloba leaf extract show no consistent pattern of clinical benefit for people with dementia or cognitive impairment, and have been suggested to be toxic to cells at higher doses. However, medicinal plants may contain other more efficient bioactive molecules apart from the well-known flavonoids and terpenoids. Therapeutic recombinant proteins, plant-made copper chaperone for superoxide dismutase (CCS) derived from Ginkgo biloba leaves, may establish and maintain physiologic Cu levels through restoration and modulation of biometal metabolism in organ systems of younger Alzheimer patients (> 50 years). Medications developed from plant-made copper chaperone proteins may delay progression during early disease stages or even be a basis for a possible causal treatment of preclinical stages of Alzheimer’s disease by preventing formation of A β plaques in the brain, a major putative factor involved in Alzheimer’s disease pathogenesis.
Highlights
The dysregulation of biometal (Cu, Zn, Fe) homeostasis and oxidative stress in brain cells have been found to impact on accumulation of amyloid β (Aβ), a major putative factor involved in early Alzheimer’s disease (AD) pathogenesis [1]
For the restoration and modulation of metal ion homeostasis in the treatment of AD, we have proposed a novel class of pharmacologically active plant ingredients as antioxidants: copper chaperone for superoxide dismutase derived from medicinal plants (e.g., Ginkgo biloba)
For the restoration and modulation of metal ion homeostasis and for balancing intracellular pro-oxidative and antioxidative processes in the treatment of Alzheimer’s disease, plant-made copper chaperone for superoxide dismutase (CCS) proteins potentially have greater efficacy and fewer side-effects compared to small organic molecules from medicinal plant extracts or therapeutic recombinant proteins produced in bacteria, fungi or mammals
Summary
The dysregulation of biometal (Cu, Zn, Fe) homeostasis and oxidative stress in brain cells have been found to impact on accumulation of amyloid β (Aβ), a major putative factor involved in early Alzheimer’s disease (AD) pathogenesis [1]. The dynamic interplay of properly folded CCS and SOD-1 guarantees that free Cu and Zn ions are being complexed by these metal proteins and do not catalyze oxidation processes of proteins, lipids, DNA, and other molecules in the cells [2]. When these physiological complexation mechanisms do not function properly, oxidative stress and dys-homeostasis of Cu and Zn metabolism may give rise to misfolding, accumulation and aggregation of amyloid β peptides [2]. AD patients (> 50 years old) with preclinical stages of disease
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