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Growing evidence is showing that diabetes and AD are concurrent entities
Adaugat pe 17/05/2018 10:35:47 de lilyeven12
Plaques containing fibrillar Aβ deposits associated with dying cells and
inflammatory processes are hallmark pathological features in AD and
diabetes15,16. The accumulation of Aβ within islet β-cells is a major
pathological feature of the pancreas in patients with chronic diabetes. Viruses
also may be involved Creutzfeldt–Jakob disease (CJD) despite its earlier
connection with prion accumulation. CJD is more commonly known as the human form
of “mad cow disease” [bovine spongiform encephalopathy (BSE)]. This devastating
degenerative neurological disorder is untreatable and inevitably fatal Dental
. CJD is characterized by the presence of a deformed protein called a
prion. There is controversy as to how the disease progresses. The explanation
most commonly accepted is that a defective prion replicates by converting its
properly folded counterparts in the host to the same misfolded structure it
possesses, or “prion only theory”17. However, Laura Manuelidis, MD,18 proposed
that virus particles cause CJD.19 Manuelidis claimed that although much work
remains to be done, there is a reasonable explanation that viral particles cause
the transformation of the prion that is the hallmark of CJD. It is likely that
all the various versions of an abnormal prion are the result of infection by an
exogenous and stable viral particle and are a consequence of the
neurodegenerative disease process rather than its cause. Abnormal prions are
present in extremely small amounts in accessible tissues or body fluids such as
blood, urine, saliva, and cerebrospinal fluid20,21. CJD causes tissue to
degenerate rapidly. As the disease destroys the brain, holes in the neural
structures develop that resemble a sponge in appearance. Viruses incorporating
their DNA elements into the host DNA can reprogram the prion protein synthesis
mechanism to produce “mutant” prions. Prion disease epidemics, which have
demonstrated unpredictable recurrence, are of significant concern for animal and
human health. Furthermore, chronic wasting disease (CWD) is a relatively new and
burgeoning prion epidemic in deer, elk, and moose (members of the cervid family)
and may be related to the human prion versions22,23 turbine
air compressor
. This perspective on possible links between CJD and viral
pathogens causes us to question if other neurologic diseases causing similar
brain damage also may by caused by viruses. AD, multiple sclerosis, autism,
Parkinson’s disease, amyotrophic lateral sclerosis, and other neurological
entities display similar brain damage. AD24 is the most common of many
neurodegenerative disorders primarily affecting aging humans. Frank Dohler and
his colleagues25 reported an investigation that showed an amyloid’s abnormal
ability to attract and bind to prions, the same type of molecules that become
erratic in BSE and CJD. A normal amyloid is a stacking of normal prions26
(Figure 4). The main problem in AD is that Aβ formation becomes so prevalent
that this material interferes with normal electrical connections in the brain11.
Aβ are peptides of 36 to 43 amino acids that are fatefully involved in AD as the
main component of the Aβ plaques11. These peptides result from an amyloid
precursor protein (APP) that is altered by certain enzymes to yield Aβ. These
molecules can accumulate to form flexible, soluble Aβ fibrils. Abnormal Aβ is a
variant binding of a deformed amyloid with folded-over prions, the same
malformed, problematic process that exists in BSE and CJD. It is now believed
that certain misfolded abnormal oligomers known as seeds can induce other
amyloid molecules to also take on an aberrant, misfolded oligomeric form,
leading to a chain reaction akin to an abnormal prion infection.27 The seeds, or
the resulting Aβ plaques, interfere with function and are toxic to nerve cells
. The other protein implicated in AD, tau protein, also forms prion-like
misfolded oligomers, and there is some evidence that misfolded Aβ can induce tau
to misfold 32, 28. In BSE and CJD, as discussed earlier, there is a growing
consensus that a virus is encoding prions that are misfolded. If this hypothesis
proves to be true, then what is the possibility that the final step of the AD
process is also caused by the same virus?  

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