Wheat germ/Spermidine the Staff of Life Indeed

Neurodegenerative disease is associated with oxidative damage.

Neurodegenerative disease is associated with abnormal protein aggregates and plaques.

Neurodegenerative disease and plaques result from abnormal cell quality control.

Neurodegenerative diseases is associated with abnormal proteostasis.

Proteostasis includes the action of anabolic heat shock proteins like HSP1 that properly fold proteins or chaperone them to lysozymes for recycling.

Proteostasis includes the production and action of endogenous antioxidants.

Exogenous antioxidants are weak 1/1 in effectiveness and are spent like dollars and depleted.

Endogenous antioxidants, SOD and glutathione, are strong 1000/1 in effectiveness like reloadable gift cards.

The rate limiting step that results in oxidative damage and protein aggregates is Nrf2 pathway down regulation due to reduced proteostasis.

Spermidine is essential for eukaryotic life.

Spermidine declines with age.

Spermidine is the key for efficient proteostasis.

Wheat germ is high in spermidine.

Eat 2 tbsp of wheat germ daily. Increase whole grain foods in diet.

Spermidine decreases neurodegenerative disease, plaques and increases cell quality control activities as in autophagy, heat shock proteins or chaperone and endogenous protein enzymes that produce endogenous antioxidants.

http://www.pnas.org/content/114/5/803.extract

Combating Parkinson’s disease-associated toxicity by modulating proteostasis

Yangshin Park^a,^b,^c and                                   

The first page of the PDF of this article appears below.

The incidence of age-associated neurodegenerative disease is growing rapidly, and it is expected to triple by 2050 (1). Currently, there are no cures or treatments that significantly modify disease progression. As researchers develop an in-depth understanding of the mechanisms of neurodegeneration, common features across different diseases are becoming apparent. Chief among them is the presence of protein aggregates, such as amyloid plaques and tau tangles in Alzheimer’s disease (2); α-synuclein–rich Lewy bodies and Lewy neurites in Parkinson’s disease (3); huntingtin aggregates in Huntington’s disease (4); and aggregates of superoxide dismutase 1 (SOD1), TDP43, and FUS in amyotrophic lateral sclerosis (5). Although the precise mechanisms of protein aggregation-associated toxicity remain unclear, the accumulation of aggregated proteins in the diseased neurons indicates imbalances in protein homeostasis (proteostasis) (proteostasis is reviewed in ref. 6). As such, researchers are studying the potential therapeutic strategy of restoring proteostasis to normal levels by boosting the activity of molecular chaperones. One way to do so is to activate HSF1 (heat shock factor protein 1) by inhibiting HSP90 (heat shock protein 90), thereby stimulating the expression of multiple chaperones. Indeed, this strategy has been shown to be effective in fly models of Parkinson’s disease and … 

[Full Text of this Article]

↵¹To whom correspondence should be addressed. Email: qqhoang@iu.edu.

Joseph Thomas (Tony) Liverman, Jr