Document Type

Journal Article

Publisher

Omics Publishing Group

School

School of Medical Sciences/Centre of Excellence in Alzheimer's Disease Research and Care

RAS ID

23070

Comments

Originally published as: Martins, I. J. (2016). Bacterial lipopolysaccharides change membrane fluidity with relevance to phospholipid and amyloid beta dynamics in Alzheimer's disease. Journal of Microbial & Biochemical Technology, 8(4), 322-324. Original article available here

Abstract

Bacterial lipopolysaccharides (LPS) and their increase in plasma in individuals in the developing world has become of major concern. LPS can transform cells by their rapid insertion into cell membranes that partition into cholesterol/sphingomyelin domains. LPS alter cell phospholipid dynamics associated with the recruitment of the Alzheimer’s disease amyloid beta (Aβ) peptide with the promotion of toxic Aβ oligomer formation. The common pattern of naturally occurring phospholipids such as1-palmitoyl-2-oleolyl-phosphatidylcholine in cells confers cells with the rapid transfer of Aβ and phospholipids. Phospholipids such as dipalmitoylphosphatidylcholine (DPPC), dimyristoylphosphatidylcholine (DMPC) and dioleoylphosphatidylcholine (DOPC) are poorly transported with delayed metabolism of Aβ oligomers. LPS can alter cells with POPC cell membrane characteristics by insertion of itself and promotion of ganglioside GM1-cholesterol as the seed for Aβ oligomerization. LPS modification of cell membrane fluidity in neurons involves the phospholipid transfer protein that affects vitamin E, phospholipid and Aβ metabolism. Healthy diets that contain olive oil, canola oil and vegetable oil promote membrane fluidity and Aβ metabolism but in the developing world increased LPS levels interfere with healthy diets and their regulation of phospholipid and Aβ dynamics. Unhealthy diets that contain palmitic acid should be avoided that promote DPPC cell membrane contents with poor phospholipid and Aβ metabolism. Nutritional therapy may improve metabolic disease and Alzheimer’s disease by the delay of LPS toxic induced Aβ interactions that involve various proteins such as albumin (Aβ selfassociation) with reduced toxic effects of LPS to astrocyte-neuron crosstalk in the brain.

DOI

10.4172/1948-5948.1000304

Access Rights

Free_to_read

Creative Commons License

Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.

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Diseases Commons

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