Dr. Weeks’ Comment: Copper in our water (think copper pipes and think turquoise stain on porcelain) can hurt. Search psychosis and copper or anger and copper at pubmed…. but now we see the benefits of copper on brain health (think copper as antibiotic). Also, did you know that within each amyloid plaque is typically a herpes virus and that the plaque us a therapeutic effort to contain the virus (see following abstracts).
Copper Can Protect Against Alzheimer’s Disease
Feb. 17, 2013 ”” Researchers in The Birchall Centre at Keele University, Staffordshire, UK, have provided unequivocal evidence that under conditions which are approximately similar to those found in the brain, copper can only protect against beta amyloid forming beta sheets and as such it is highly unlikely that copper is directly involved in the formation of senile plaques in Alzheimer’s disease.
The research, published by Nature’s online journal Scientific Reports, may also imply that lower levels of copper in the brain may promote the mechanisms whereby beta amyloid is deposited as senile plaques in Alzheimer’s disease.
This research addressed the on-going question as to whether copper in the brain contributes to the formation of the senile plaques in Alzheimer’s disease. While previous research at Keele’s Birchall Centre pointed towards copper being potentially protective in preventing the protein beta amyloid from aggregating as beta sheets and forming senile plaques it had remained a controversial issue for some.
- Matthew Mold, Larissa Ouro-Gnao, Beata M Wieckowski, Christopher Exley. Copper prevents amyloid-Î²1-42 from forming amyloid fibrils under near-physiological conditions in vitro. Scientific Reports, 2013; 3 DOI: 10.1038/srep01256
Intracerebral propagation of Alzheimer’s disease: strengthening evidence of a herpes simplex virus etiology.
Department of Pathology, Oregon Health & Science University, Portland, OR, USA. email@example.com
A faulty human protein, abnormally phosphorylated tau, was recently publicized to spread “like a virus” from neuron to neuron in Alzheimer’s patients’ brains. For several decades, we have been amassing arguments showing that herpes simplex virus type 1 (HSV-1), not p-tau, propagates this interneuronal, transsynaptic pathologic cascade.
We reiterate convincing data from our own (and other) laboratories, reviewing the first anatomic foothold neurofibrillary tangles gain in brainstem and/or entorhinal cortex; the chronic immunosurveillance cellularity of the trigeminal ganglia wherein HSV-1 awakens from latency to reactivate; the inabilities of p-tau protein’s physical properties to promote it to jump synapses; the amino acid homology between human p-tau and VP22, a key target for phosphorylation by HSV serine/threonine-protein kinase UL13; and the exosomic secretion of HSV-1-infected cells’ L-particles, attesting to the cell-to-cell passage of microRNAs of herpesviruses.
The now-maturing construct that reactivated HSV-1 best accounts for the intracerebral propagation of AD changes in the human brain should at last seem highly attractive. This hypothesis might even explain statins’ apparent mechanism in some studies for lowering AD incidence.
Provided that funding agencies will quickly ignite a new realm of investigation, the rejuvenated enthusiasm for testing this optimistic construct holds incalculable potential for rapid, efficacious clinical application, through already available and relatively safe antiviral therapeutics.’
The essential lesion of Alzheimer disease: a surprise in retrospect.
Department of Pathology L-113, Oregon Health & Science University, 3181 SW Sam Jackson Pk. Rd., Portland, OR 97239-3098, USA. firstname.lastname@example.org
In the absence of any naturally occurring animal model of Alzheimer’s disease (AD), the British conviction in the 1970’s that clinicopathological investigations of human cases offered the best approach to unraveling the pathogenesis of AD rapidly influenced clinical neuroscientists, neuropathologists and funding agencies in Canada and the USA. But as with my confreres, years of our quantifying AD lesions in autopsy brains have yet to yield definitive conclusions about what is the most important neuronal abnormality. However, during my elusive search, evidence has been slowly gathered that reactivation of latent Herpes simplex virus, traveling from trigeminal ganglia into neighbouring mesial temporal cortex, might best explain the limbic predilection for and earliest site of neurofibrillary tangle formation. This maturing hypothesis may serendipitously prove to have been a more essential byproduct of generating the voluminous data than all the publications from our laboratory that reflected endless hours of quantitative morphometry.
Herpes simplex virus type 1 DNA is located within Alzheimer’s disease amyloid plaques.
Faculty of Life Sciences, University of Manchester, UK.
The brains of Alzheimer’s disease sufferers are characterized by amyloid plaques and neurofibrillary tangles. However, the cause(s) of these features and those of the disease are unknown, in sporadic cases. We previously showed that herpes simplex virus type 1 is a strong risk factor for Alzheimer’s disease when in the brains of possessors of the type 4 allele of the apolipoprotein E gene (APOE-epsilon4), and that beta-amyloid, the main component of plaques, accumulates in herpes simplex virus type 1-infected cell cultures and mouse brain. The present study aimed to elucidate the relationship of the virus to plaques by determining their proximity in human brain sections. We used in situ polymerase chain reaction to detect herpes simplex virus type 1 DNA, and immunohistochemistry or thioflavin S staining to detect amyloid plaques. We discovered a striking localization of herpes simplex virus type 1 DNA within plaques: in Alzheimer’s disease brains, 90% of the plaques contained the viral DNA and 72% of the DNA was associated with plaques; in aged normal brains, which contain amyloid plaques at a lower frequency, 80% of plaques contained herpes simplex virus type 1 DNA but only 24% of the viral DNA was plaque-associated (p < 0.001). We suggest that this is because in aged normal individuals, there is a lesser production and/or greater removal of beta-amyloid (Abeta), so that less of the viral DNA is seen to be associated with Abeta in the brain. Our present data, together with our finding of Abeta accumulation in herpes simplex virus type 1-infected cells and mouse brain, suggest that this virus is a major cause of amyloid plaques and hence probably a significant aetiological factor in Alzheimer’s disease. They point to the usage of antiviral agents to treat the disease and possibly of vaccination to prevent it.