• Preventive Nutrition and Food Science
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• v.12 no.2
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• pp.74-78
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• 2007

Fucoidan, that is high-molecular-weight sulfated polysaccharides extracted from brown seaweeds has been shown to elicit various biological activities. Here, we investigated the effects of fucoidan on cell proliferation and nitric oxide (NO) production in neuronal blastoma cell (SH-SY5Y). In the present study, we demonstrated that fucoidan treatment resulted in increase of cell proliferation and NO production. When cells were treated with amyloid-${\beta}$ (A${\beta}$) in the absence or presence of fucoidan, fucoidan recovered the cell viability decreased by A${\beta}$ peptides. To further determine whether nitric oxide synthase (NOS) is involved in proliferative effect of fucoidan, cells were treated with NOS inhibitors in the absence or presence of fucoidan. Selective constitutive nitric oxide synthase (cNOS) inhibitor, diphenylene iodonium chloride (DPI), caused a decrease of cell viability, whereas cell viability was increased by specific inducible nitric oxide synthase (iNOS) inhibitor, S-methylisothiourea (SMT), in the fucoidan-untreated cells. Treatment with fucoidan inhibited the cell viability decreased in DPI-exposed cells. In contrast, fucoidan had no effect on cell growth in SMT-treated cells, indicating that cNOS may not play a role in the proliferation of fucoidan-treated cells. The present data suggest that fucoidan has proliferative and neuroprotective effects and these effects may be associated with iNOS.

• Journal of the Korean Society of Food Science and Nutrition
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• v.45 no.11
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• pp.1552-1563
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• 2016

To examine the cognitive function of onion (Allium cepa L.) beverages (odourless and fortified), we analyzed in vitro neuronal cell protection against $H_2O_2$-induced cytotoxicity and performed in vivo tests on amyloid beta ($A{\beta}$)-induced cognitive dysfunction. Cellular oxidative stress and cell viability were evaluated by DCF-DA assay and MTT assay. These results show that fortified beverage resulted in better neuronal cell protection than odourless beverage at lower concentration ($0{\sim}100{\mu}g/mL$). Fortified beverage also showed more excellent acetylcholinesterase (AChE) inhibitory activity ($IC_{50}$: 4.20 mg/mL) than odourless beverage. The cognitive functions of odourless beverage and fortified beverage in $A{\beta}$-induced neurotoxicity were assessed by Y-maze, passive avoidance, and Morris water maze tests. The results show improved cognitive function in both groups treated with beverages. After in vivo tests, cholinergic activities were determined based on AChE inhibition and acetylcholine levels, and antioxidant activities were measured as SOD, oxidized glutathione (GSH)/total GSH ratio, and MDA levels in mouse brain tissue. In a Q-TOF UPLC/MS system, main compounds were analyzed as follows: odourless beverage (five types of sugars and three types of phenolics) and fortified beverages (six types of phenolics and two types of steroidal saponins).

• Journal of Microbiology and Biotechnology
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• v.19 no.9
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• pp.960-965
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• 2009

${\beta}2$-Microglobulin (${\beta}2m$) is known to be a major factor for dialysis-related amyloidosis. We have studied ${\beta}2m$ removal through an aggregation process, which was initiated by a ligand that could catch the ${\beta}2m$ monomer and promote its aggregation into fibril. As a ligand, we have prepared ${\beta}2m$ fibril fragments and used them as a seed. The seed was coupled to PEGylated-PS beads to remove the monomeric ${\beta}2m$ from solution. The ${\beta}2m$ seed-conjugated resin effectively adsorbed the ${\beta}2m$ monomers with a capacity of 3.6 mg/ml via promoting their aggregation into fibrils on the resin at pH 7.4.

• Proceeding of EDISON Challenge
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• 2016.03a
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• pp.55-61
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• 2016

$A{\beta}_{40}$ peptides form oligomers that later aggregate into a plaque, which is deemed to be a leading cause of Alzheimer's Disease. Its non-crystalline morphology has limited an understanding of comprehensive structural study. In this research, computational biomolecular simulations were performed in the following order: solvent and ion addition in a box, energy minimization of protein, equilibration, and periodic boundary condition disaggregation of a monomer from fibril. The result founded the two-fold model is 25% more stable in the simulation environment, and the steric zippers held on most tightly until 220 ps of simulation. The study supports the previous findings that two-fold aggregate $A{\beta}_{40}$ is more stable at 310 K and discusses further how much contribution steric-zipper and hydrogen bonding are making.

• Proceedings of the PSK Conference
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• 2003.04a
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• pp.271.2-271.2
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• 2003

The ${\gamma}$- and ${\beta}$-secretase are one of the most important proteases, which cleave amyloid precursor protein (APP) into neurotoxic A${\beta}$ peptide in Azheimer's type dementia. In the course of screening for anti-dementia agents from natural products, the mycelial culture of mushroom Phellinus linteus showed potent inhibition againt ${\beta}$-secretase (BACE1). (omitted)

• Proceedings of the PSK Conference
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• 2003.10b
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• pp.124.1-124.1
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• 2003

We investigated whether the mushroom extracts can protect neuronal death and ameliorate memory deficits in Alzheimer"s disease induced by $\beta$-amyloid peptide[A$\beta$(25-35)]. Cellular model of Alzheimer"s disease was produced by using SK-N-SH human neuronal cells treated with $A\beta$. Treatment with 40uM $A\beta$ for 48hours caused a 46% loss of cell viability. First, we examined the effects of 22 mushroom extracts on neuronal death using MTT assay. We found that 3 mushroom extracts increased viability of the cells from 46% to 87%. (omitted)

• Journal of Life Science
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• v.21 no.11
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• pp.1636-1640
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• 2011

Alzheimer's disease (AD) is a progressive neurodegenerative disease, resulting in the loss of cognitive function. Mitochondrial aldehyde dehydrogenase (ALDH2) has been proposed to be a risk factor for the development of AD, but there is still controversy about that. In this study, we demonstrated the role of ALDH2 enzyme activity on amyloid-beta (A${\beta}$) and nuclear factor kappa B (NF-${\kappa}B$) expression in mice brain following ethanol exposure for 8 weeks. Five male Aldh2 (+/+) and Aldh2 (-/-) mice, 8 weeks-old of age (C57BL/6J strain), in each group were exposed to ethanol for 8 weeks (2 g/kg wt./day) using gavage. Those in the control groups received 0.9% saline alone. Results showed a difference in expression level of A${\beta}$ in the hippocampus after ethanol exposure according to the ALDH2 enzyme activity (p<0.05), but not in the level of NF-${\kappa}B$). Our results suggest a possibility that ALDH2 enzyme activity may be an important role in the development of AD.

• Bulletin of the Korean Chemical Society
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• v.30 no.12
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• pp.3006-3010
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• 2009

We have performed long time REMD simulation on 15-19 residues of human calcitonin hormone (DFNKF) which is known to form highly ordered amyloid fibril. The simulation started from randomly oriented multiple DFNKF strand. Using all-atom level simulations with the generalized Born solvation (GB) model (param99MOD3), we observed spontaneous formation of ${\beta}$-sheet for tetramer. Interestingly, the current simulation gives anti-parallel sheet as a major conformation, consistent with experiments. The major interaction stabilizing the anti-parallel sheet seems to be the inter-strand hydrogen bond.

• Journal of the Korean Magnetic Resonance Society
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• v.8 no.1
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• pp.19-27
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• 2004

C-terminal fragments of APP (APP-CTs), that contain complete Abeta sequence, are found in neuritic plaques, neurofibrillary tangles and the cytosol of lymphoblastoid cells obtained from AD patients. CT16, Lys649-Asp664 (KKQYTSIHHGVVEVD) has been known as the most toxic part in the C-terminal fragment of amyloid precursor protein (APP). The solution structure of CT16 was investigated using NMR spectroscopy in various membrane-mimicking environments. According to Circular Dichroim (CD) spectra, CT16 has a random structure in aqueous solution, while conformational change was induced by addition of TFE and SDS micelle. Tertiary structure as determined by NMR spectroscopy shows that CT16 has a ${\beta}$-turn conformation in trifluoroethanol-containing aqueous solution.

• Journal of Physiology & Pathology in Korean Medicine
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• v.17 no.4
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• pp.1037-1049
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• 2003

Numerous lines of evidence indicate that some of the neurotoxicity associated with Alzheimer's disease (AD) is due to proteolytic fragments of the amyloid precursor protein (APP). Most research has focused on the amyloid 6 (M). However, the possible role of other cleaved products of APP is less clear. Lately It has been reported that a recombinant carboxy-terminal 105 amino acid fragment (CT105) of APP induced strong nonselective inward currents in Xenopus oocyte. In a brain with Alzheimer's disease (AD), to investigate the roles of carboxyl-terminal fragment (CT105) of amyloid precursor protein (APP) in apoptosis processes possibly linked to neurodegeneration associated with AD, we examined the effects of the CT of APP with 105 amino acid residues (CT105) on the alteration of apoptosis triggers in neubroblastoma cells. We have investigated whether Radix Polygalae and Rhizoma Acori Graminei mixture extract (RP+RAG) inhibits CT105-induced apoptosis of neuroblastoma cells. We found that RP+RAG inhibits CT105-induced apoptosis in SK-N-SH cells. Treatment of the cells with RP+RAG inhibited CT105-induced DNA fragmentation and Tunel assay of nuclear chromatin and inhibited the caspase-3 expression in SK-N-SH cells. As the result of this study, In RP+RAG group, the apoptosis in the nervous system is inhibited, the repair against the degerneration of neuroblastoma cells by CT105 expression is promoted. These results indicate that RP+RAG possess strong inhibitory effect of apoptosis in the nervous system and repair effect against the degeneration of neuroblastoma cells by CT105 expression