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Heparin nanoparticles for ? amyloid binding and mitigation of ? amyloid associated cytotoxicity.

ABSTRACT: Accumulation of ? amyloid (A?) in the brain is believed to play a key role in the pathology of Alzheimer's disease. Glycosaminoglycans on surface of neuronal cells can serve as nucleation sites to promote plaque formation on cell surface. To mimic this process, magnetic nanoparticles coated with heparin have been synthesized. The heparin nanoparticles were demonstrated to bind with A? through a variety of techniques including enzyme-linked immunosorbent assay, gel electrophoresis, and thioflavin T assay. The nanoparticle exhibited little toxicity to neuronal cells and at the same time can effectively protect them from A? induced cytotoxicity. These results suggest that heparin nanoparticles can be a very useful tool for A? studies.

SUBMITTER: Wang P

PROVIDER: S-EPMC4314519 | biostudies-other | 2015 Mar

REPOSITORIES: biostudies-other

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Heparin nanoparticles for β amyloid binding and mitigation of β amyloid associated cytotoxicity.

Wang Peng P Kouyoumdjian Hovig H Zhu David C DC Huang Xuefei X

Carbohydrate research 20140802

Accumulation of β amyloid (Aβ) in the brain is believed to play a key role in the pathology of Alzheimer's disease. Glycosaminoglycans on surface of neuronal cells can serve as nucleation sites to promote plaque formation on cell surface. To mimic this process, magnetic nanoparticles coated with heparin have been synthesized. The heparin nanoparticles were demonstrated to bind with Aβ through a variety of techniques including enzyme-linked immunosorbent assay, gel electrophoresis, and thioflavin ...[more]

PMID: 25498198

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Project description:Complement inhibitor C4b-binding protein (C4BP) is synthesized in liver and pancreas and composed of 7 identical alpha chains and one unique beta chain. We showed previously that C4BP binds islet amyloid polypeptide (IAPP) and affects fibril formation in vitro. Now we found that polymeric C4BP inhibited lysis of human erythrocytes incubated with monomeric IAPP while no erythrocyte lysis was observed after incubation with preformed IAPP fibrils. In contrast, monomeric alpha chain of C4BP had significantly reduced activity. Further, addition of monomeric IAPP to a rat insulinoma cell line (INS-1) resulted in decreased cell viability, which was restored in the presence of physiological concentrations of C4BP. Accordingly, addition of C4BP rescued the ability of INS-1 cells and isolated rat islets to respond to glucose stimulation with insulin secretion, which was impaired in the presence of IAPP alone. C4BP was internalized together with IAPP into INS-1 cells and therefore we aimed to study its effect on gene expression. Pathway analyses of mRNA expression microarray data indicated that cells exposed to C4BP and IAPP in comparison to IAPP alone increased expression of genes involved in cholesterol synthesis. Depletion of cholesterol through methyl-Î²-cyclodextrin or cholesterol oxidase abolished the protective effect of C4BP on IAPP cytotoxicity of INS-1 cells. Also, inhibition of phosphoinositide 3-kinase but not NF-ÎºB had a similar effect. Taken together, one of the mechanisms by which C4BP protects beta-cells from IAPP cytotoxicity is by enhancing cholesterol synthesis. The INS-1 cells were grown as 5 separate clones for 10 passages before plating in a 12-well plate (Nunc) at 100.000 cells per well and grown in complete RPMI 1640 medium to 70% confluency for approximately 48 h. The cells were then challenged by adding 77 Î¼M monomeric IAPP alone or together with C4BP (0.6 Î¼M). DMSO (1%) used as solvent for IAPP as well as C4BP (0.6 Î¼M) alone were used as controls. RNA was extracted after 10h incubation and analysis carried out using Rat Gene 2.0 array chip (Affymetrix).

Dataset Information

Heparin nanoparticles for ? amyloid binding and mitigation of ? amyloid associated cytotoxicity.

Publications

Heparin nanoparticles for β amyloid binding and mitigation of β amyloid associated cytotoxicity.

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