Alzheimer: Could there be a connection: RF-EMF and Alzheimer’s?

Bron: betweenrockandhardplace.wordpress.com/2016/06/16/could-there-be-a-connection-rf-emf-and-alzheimers/
16 juni 2016

Just published study by Kumar et al. “Amyloid-β peptide protects against microbial infection in mouse and worm models of Alzheimer’s disease.” in the Science Translational Medicine proposes a new explanation for the Alzheimer’s disease.
stm.sciencemag.org/content/8/340/340ra72
The authors suggest that the disease would be a defensive mechanism against the bacteria and viruses invading the brain. Of course, as every scientific study, also this one has its critics.

However, the hypothesis of brain defending itself against bacteria and viruses by generating plaques that “imprison” the invaders sounds interesting and should be explored in more detail.

This hypothesis, on brain defense, is possible to extend into… cell phone radiation. This is not yet another crazy idea suggesting that anything what is wrong with human health is caused by RF-EMF. It is hypothesis that has potential scientific basis and should be also examined in detail.

There have been published studies suggesting a link between exposures to cell phone radiation and Alzheimer’s disease and cognition. The EMF Portal lists 8 experimental studies. Especially these from research group of Gary Arendash are worth examining. His work, on Alzheimer’s and cognition, is under a replication attempt by John Finnie in Australia.

The link between Alzheimer’s and RF-EMF exposure might be indirect one.

The RF-EMF has been shown, in some animal studies, to increase permeability of the blood-brain barrier but others did not find such effect. One possible mechanism of the RF-EMF effect of increasing permeability of the BBB could be the activation of cellular stress response in endothelial cells being part of the blood-brain barrier.

My research group, when it still existed, has published some 14 years ago a study showing activation of the Hsp27/p38MAPK pathway in endothelial cells, shown in subsequent studies to cause relocation of F-actin stress fibers and shrinkage and detachment of endothelium from the substratum.

https://betweenrockandhardplace.files.wordpress.com/2016/06/leszczynski-et-al-hypothesis-rf-and-bbb.jpg

Considering altogether, the RF-EMF-induced stress response in endothelium, the RF-EMF-induced blood-brain barrier permeability and the potential defensive role of the Alzheimer’s in brain infections, it is possible to put forward a hypothesis, shown below (click to enlarge), suggesting that cell phone radiation by activation of stress response causes increased leakage of the blood-brain barrier allowing easier traffic of pathogens into the brain tissue where the defensive mechanisms cause formation of plaques to imprison the infecting pathogens.

https://betweenrockandhardplace.files.wordpress.com/2016/06/leszczynski-hypothesis-alzheimer.jpg


Uit: stm.sciencemag.org/content/8/340/340ra72 :

Rehabilitation of a β-amyloid bad boy

A protein called Aβ is thought to cause neuronal death in Alzheimer’s disease (AD). Aβ forms insoluble aggregates in the brains of patients with AD, which are a hallmark of the disease. Aβ and its propensity for aggregation are widely viewed as intrinsically abnormal. However, in new work, Kumar et al. show that Aβ is a natural antibiotic that protects the brain from infection. Most surprisingly, Aβ aggregates trap and imprison bacterial pathogens. It remains unclear whether Aβ is fighting a real or falsely perceived infection in AD. However, in any case, these findings identify inflammatory pathways as potential new drug targets for treating AD.

Abstract

The amyloid-β peptide (Aβ) is a key protein in Alzheimer’s disease (AD) pathology. We previously reported in vitro evidence suggesting that Aβ is an antimicrobial peptide. We present in vivo data showing that Aβ expression protects against fungal and bacterial infections in mouse, nematode, and cell culture models of AD. We show that Aβ oligomerization, a behavior traditionally viewed as intrinsically pathological, may be necessary for the antimicrobial activities of the peptide. Collectively, our data are consistent with a model in which soluble Aβ oligomers first bind to microbial cell wall carbohydrates via a heparin-binding domain. Developing protofibrils inhibited pathogen adhesion to host cells. Propagating β-amyloid fibrils mediate agglutination and eventual entrapment of unatttached microbes. Consistent with our model, Salmonella Typhimurium bacterial infection of the brains of transgenic 5XFAD mice resulted in rapid seeding and accelerated β-amyloid deposition, which closely colocalized with the invading bacteria. Our findings raise the intriguing possibility that β-amyloid may play a protective role in innate immunity and infectious or sterile inflammatory stimuli may drive amyloidosis. These data suggest a dual protective/damaging role for Aβ, as has been described for other antimicrobial peptides.



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