Heartburn? Can we convert it into Alzheimer's disease (AD) instead. Yes, rot the brain out as a "cure."

[Nun Giver]

One more thing for the rat bastard drug rep to pooh pooh.



1. PLoS One. 2013;8(3):e58837. doi: 10.1371/journal.pone.0058837.
Epub 2013 Mar 8.

The proton-pump inhibitor lansoprazole enhances amyloid Beta production.

Badiola N, Alcalde V, Pujol A, Münter LM, Multhaup G,
Lleó A, Coma M, Soler-López M, Aloy P.

Institute for Research in Biomedicine.
Joint IRB-BSC Program in Computational Biology,
Barcelona, Spain.

A key event in the pathogenesis of Alzheimer's disease (AD) is the accumulation
of amyloid-β (Aβ) species in the brain, derived from the sequential cleavage of
the amyloid precursor protein (APP) by β- and γ-secretases. Based on a systems
biology study to repurpose drugs for AD, we explore the effect of lansoprazole,
and other proton-pump inhibitors (PPIs), on Aβ production in AD cellular and
animal models. We found that lansoprazole enhances Aβ37, Aβ40 and Aβ42 production
and lowers Aβ38 levels on amyloid cell models. Interestingly, acute lansoprazole
treatment in wild type and AD transgenic mice promoted higher Aβ40 levels in
brain, indicating that lansoprazole may also exacerbate Aβ production in vivo.
Overall, our data presents for the first time that PPIs can affect amyloid
metabolism, both in vitro and in vivo.

PMCID: PMC3592824
PMID: 23520537 [PubMed - in process]

[Nun Giver]

Never trust a Doctor or a Pharma rep. They formerly denied that
PPI meds altered the function of other proton pumps in the body
not in the stomach lining.

J Clin Pharm Ther. 2010 Apr;35(2):125-6. doi: 10.1111/j.1365-2710.2009.01100.x.

Proton pump inhibitors: predisposers to Alzheimer disease?

Fallahzadeh MK, Borhani Haghighi A, Namazi MR.

Autoimmune Diseases Research Center,
Shiraz University of Medical Sciences,
Shiraz, Iran.

The abnormal processing of amyloid-beta peptide (A beta) and
resultant formation of fibrillar A beta (fA beta) are major events
in the pathogenesis of Alzheimer disease (AD). Microglia as the
phagocytic cells of the brain can engulf and digest fA beta within
their acidic lysosomes. The lysosomes of AD patients are
less acidic and therefore less capable of clearance of fA beta.
Vacuolar proton pumps (V-ATPases) which are found abundantly
in microglia and macrophages, acidify lysosomes by pumping
protons into these structures. Proton pump
inhibitors (PPIs) can inhibit V-ATPases of the lysosomes.
These drugs are shown to penetrate the blood-brain barrier
in animals. PPIs are consumed for long
periods in conditions such as gastroesophageal
reflux disease, with the resultant exposure of the human brain
to the substantial amounts of PPIs. We hypothesize
that by blocking the V-ATPases on microglial lysosomes,
PPIs may basify lysosomes and hamper degradation of fA beta.
Chronic consumption of PPIs may thus be a risk
factor for AD.

PMID: 20456731 [PubMed - indexed for MEDLINE]