A hallmark feature of Alzheimer’s disease (AD) and other tauopathies is the misfolding, aggregation and cerebral accumulation of tau deposits. Compelling evidence indicates that misfolded tau aggregates are neurotoxic, producing synaptic loss and neuronal damage.
https://www.nature.com/articles/s41598-020-59364-x
I have a blog where I post links to all the latest on AD, dementia, sleep, aging, etc... I don't want to bombard this wonderful forum with a bazillion links. There are SO many studies & a lot of great info out there. Shows that the world is concerned, rightfully so.
Bacterial DNA promotes Tau aggregation
Re: Bacterial DNA promotes Tau aggregation
Great article! Maybe this ties into the observation of Alzheimer’s care givers and nurses that UTIs (Urinary Tract Infections) cause an increase of dementia/Alzheimer’s symptoms.
One of the current theories is that when ApoE4 breaks down it’s degradation products are “toxic” in the sense that they straighten out the Tau protein that usually has a bend in it. This misfolded Tau protein now combines with Amyloid oligomers instead of monomers due to our ApoE4 high REL A vs SIRT1 expression when cutting APP up. This Tau-amyloid body is what is responsible for the tangles we see in AD pathology. Tau-Amyloid expression is highly correlated with AD. Amyloid without Tau or Tau without Amyloid is much less correlated.
Perhaps during bacterial infection we express REL A (North Korea/military defense as Bredesen calls it) at a higher level increasing the amyloid oligomer to monomer ratio further or perhaps the bacteria itself mis folds the Tau ? It is really Interesting stuff, I know UCSF is really pursuing this prion/mis folded protein pathway. I guess a lot of the mouse ApoE4 research is being re-evaluated and parsed as mouse ApoE 4 and human ApoE4 are different in these process (human more toxic/mouse-less toxic).
Thanks for the great article. Do you have a link to your blog?
One of the current theories is that when ApoE4 breaks down it’s degradation products are “toxic” in the sense that they straighten out the Tau protein that usually has a bend in it. This misfolded Tau protein now combines with Amyloid oligomers instead of monomers due to our ApoE4 high REL A vs SIRT1 expression when cutting APP up. This Tau-amyloid body is what is responsible for the tangles we see in AD pathology. Tau-Amyloid expression is highly correlated with AD. Amyloid without Tau or Tau without Amyloid is much less correlated.
Perhaps during bacterial infection we express REL A (North Korea/military defense as Bredesen calls it) at a higher level increasing the amyloid oligomer to monomer ratio further or perhaps the bacteria itself mis folds the Tau ? It is really Interesting stuff, I know UCSF is really pursuing this prion/mis folded protein pathway. I guess a lot of the mouse ApoE4 research is being re-evaluated and parsed as mouse ApoE 4 and human ApoE4 are different in these process (human more toxic/mouse-less toxic).
Thanks for the great article. Do you have a link to your blog?
