• Bulletin of the Korean Chemical Society
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• v.26 no.8
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• pp.1255-1259
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• 2005

Lewy bodies (LBs) are neuronal inclusions that are closely related to Parkinson's disease (PD). The filamentous component of LB from patients with PD contains biochemically altered $\alpha$-synuclein. We have investigated the effect of the oxidized products of catecholamines on the modification of $\alpha$-synuclein. When $\alpha$-synuclein was incubated with the oxidized 3,4-dihydroxyphenylalanine (L-DOPA) or dopamine, the protein was induced to be aggregated. The oxidized catecholamine-mediated $\alpha$-synuclein aggregation was enhanced by copper ion. Radical scavengers, azide and N-acetyl cysteine significantly prevented the oxidized catecholamine-mediated $\alpha$-synuclein aggregation. The results suggest that free radical may play a role in $\alpha$-synuclein aggregation. Exposure of $\alpha$-synuclein to the oxidized products of catecholamines led to the formation of dityrosine. Antioxidant dipeptides carnosine, homocarnosine and anserine significantly protected $\alpha$-synuclein from the aggregation induced by the oxidized products of catecholamines.

• BMB Reports
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• v.52 no.6
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• pp.349-359
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• 2019

After the first research declaring the generation of human induced pluripotent stem cells (hiPSCs) in 2007, several attempts have been made to model neurodegenerative disease in vitro during the past decade. Parkinson's disease (PD) is the second most common neurodegenerative disorder, which is mainly characterized by motor dysfunction. The formation of unique and filamentous inclusion bodies called Lewy bodies (LBs) is the hallmark of both PD and dementia with LBs. The key pathology in PD is generally considered to be the alpha-synuclein (${\alpha}$-syn) accumulation, although it is still controversial whether this protein aggregation is a cause or consequence of neurodegeneration. In the present work, the recently published researches which recapitulated the ${\alpha}$-syn aggregation phenomena in sporadic and familial PD hiPSC models were reviewed. Furthermore, the advantages and potentials of using patient-derived PD hiPSC with focus on ${\alpha}$-syn aggregation have been discussed.

• Journal of Physiology & Pathology in Korean Medicine
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• v.16 no.4
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• pp.823-829
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• 2002

The thrombosis importantly came to the front as the risk factor of these circulation system's disease. SilsoSanGami(SSG) was used for investigating the inhibitory effect on platelet-activating factor-induced platelet aggregation about drugs that used to improvement various symptoms created by the thrombosis in oriental medicine. In this study, the water-extracted SSG was investigated for its possible antithrombotic action on platelets. The antithrombotic activity of water-extracted SSG was deduced from its ability to suppress platelet aggregation, ATP-exocytosis, and the generation of prostaglandin E₂ and thromboxane A₂ by human platelets, stimulated with arachidonic acid. Water-extracted SSG dose-dependently suppressed the aggregation of human platelets, the release of endogenous ATP, and the formation of PGE₂ and TXB₂, both the latter usually detected to estimate the activity of COX and TXS, respectively. Since the IC/sub 50/ values necessary to inhibit COX (115 ㎍/㎖ SSG) and TXS(74 ㎍/㎖ SSG) were in the same range, inhibition of COX is suggested to be the primary target of water-extracted SSG, thus suppressing the formation of PGE₂ which is metabolized by TXS to TXA₂. We considerated that SSG has practical applicational value of clinical trial in the thrombosis caused by platelet aggregation.

• Journal of The Korean Astronomical Society
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• v.29 no.spc1
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• pp.165-166
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• 1996

A bottom-up model for the formation of GMCs is described, where the observed GMCs are the aggregates of less massive clouds. The aggregates are getting more and more massive in the process of consecutive collision between clouds.

• Bulletin of the Korean Chemical Society
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• v.8 no.2
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• pp.118-122
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• 1987

The micelle formation of NaDC was studied by fluorometric and viscometric measurements. The thermodynamic parameters of the primary and secondary micellization of the bile salt were evaluated. The primary micelle formation was appeared to be an entropy driven process due to hydrophobic effect, while the major driving force for secondary micelle formation of the bile salt is the large negative enthalpy. The secondary micelle provides less hydrophobic environment to pyrene than the primary micelle does. The cooperative aggregation of primary micelles via hvdrogen bond formation was proposed for the secondary micelle formation.

• Bulletin of the Korean Chemical Society
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• v.33 no.3
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• pp.848-854
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• 2012

We have studied the oligomerization of a fibril-forming segment of ${\alpha}$-Synulcein using a replica exchange molecular dynamics (REMD) simulation. The simulation was performed with trimers and tetramers of a 12 amino acid residue stretch (residues 71-82) of ${\alpha}$-Synulcein. From extensive REMD simulations, we observed the spontaneous formation of both trimer and tetramer, demonstrating the self-aggregating and fibril-forming properties of the peptides. Secondary structure profile and clustering analysis illustrated that antiparallel ${\beta}$-sheet structures are major species corresponding to the global free energy minimum. As the size of the oligomer increases from a dimer to a tetramer, conformational stability is increased. We examined the evolution of simple order parameters and their free energy profiles to identify the process of aggregation. It was found that the degree of aggregation increased as time passed. Tetramer formation was slower than trimer formation and a transition in order parameters was observed, indicating the full development of tetramer conformation which is more stable than that of the trimer. The shape of free energy surface and change of order parameter distributions indicate that the oligomer formation follows a dock-and-lock process.

• Bulletin of the Korean Chemical Society
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• v.35 no.5
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• pp.1343-1348
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• 2014

A cholesterol-bridge-naphthopyran dyad (NP-MCB) was designed and synthesized. NP-MCB can readily self-assemble into gels under ultrasound-radiation in several organic solvents and the formed gels easily transfer to solution by heat. This reversible process can be repeated many times. Scanning Electron Microscopy results showed that the morphologies of all formed xerogels in different solvents have fibrillar microstructure. The gels formation was due to energy and pressure afforded by the ultrasonic process, resulting in formation of molecular hydrogen bonding and molecular aggregation. NP-MCB displayed the normal photochromism both in solution and gel states. The kinetic results confirm that the colored merocyanine in gels show a slower fading speed than that in solution due to the compact aggregation of NP-MCB molecules in gels. The xerogel film formed in polar gelling solvent had large surface wettability than that in nonpolar gelling solvent.

• Journal of Microbiology and Biotechnology
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• v.8 no.6
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• pp.663-668
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• 1998

Several neurodegenerative diseases such as Huntington's disease, dentatorubralpallidoluysian atrophy, spinobulbar muscular atrophy, Machado-Joseph disease, and spinocerebellar ataxias type 1 are associated with the aggregation of expanded glutamine repeats within their proteins. Generally, in clinically affected individuals, the expansion of the polyglutamine sequences is beyond 40 residues. To address the length of polyglutamine that forms aggregation, we have constructed plasmids encoding glutathione S-transferase (GST) Machado-Joseph disease gene fusion proteins containing polyglutamine and investigated the formation of aggregates in E. coli. Surprisingly, even $(Gin)_8$, in the normal range as well as $(Gin)_{65}$ in the pathogenic range enhanced the formation of insoluble protein aggregates, whereas $(Ser)_8$, and $(Aia)_8$, did not form aggregates. Our results indicate that the formation of protein aggregates in GST-polyglutamine proteins is specifically mediated by the polyglutamine repeat sequence within their protein structure. Our study may contribute to the understanding of the molecular mechanism of the formation of protein aggregates in neurodegenerative disorders and the development of preventative strategies.

• BMB Reports
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• v.41 no.9
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• pp.635-639
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• 2008

Acrolein is a highly reactive by product of lipid peroxidation and individuals with neurodegenerative disorders have been shown to contain elevated concentrations of this molecule in the brain. In the present study, we examined the pattern of neurofilament-L (NF-L) modification elicited by acrolein. When NF-L was incubated with acrolein, protein aggregation occurred in a acrolein concentration-dependent manner. Exposure of NF-L to acrolein also led to the generation of protein carbonyl compounds. Through the addition of free radical scavengers we observed a significant decrease in acrolein-mediated NF-L aggregation. These results indicate that free radicals may be involved in the modification of NF-L by acrolein. In addition, dityrosine crosslink formation was observed in acrolein-mediated NF-L aggregates and these aggregates displayed thioflavin T reactivity, reminiscent of amyloid. This study suggests that acrolein-mediated NF-L aggregation might be closely related to oxidative reactions, thus these reactions may play a critical role in neuro-degenerative diseases.

• Korean Journal of Veterinary Research
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• v.55 no.4
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• pp.233-240
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• 2015

Although the effects of the rice bran have recently been investigated, there is no information regarding platelet physiology available. However, it is well known that fermented natural plants have a beneficial effect on cardiovascular diseases. Therefore, this study was conducted to investigate whether fermented rice bran extract (FRBE) with several plants (Artemisia princeps, Angelica Gigantis Radix, Cnidium officinale, and Camellia sinensis) affected agonist-induced platelet aggregation, and if so, what the underlying mechanism of its activity was. We performed several experiments, including in vitro platelet aggregation, intracellular calcium concentration and adenosine triphosphate release. In addition, the activation of integrin ${\alpha}_{II}b{\beta}3$ was determined using fibrinogen binding. Thrombus formation was also evaluated in vivo using an arterio-venous shunt model. The FRBE inhibited collagen-induced platelet aggregation in a concentration-dependent manner. FRBE significantly and dose dependently attenuated thrombus formation using rat arterio-venous shunt. FRBE suppressed the intracellular calcium mobilization in collagen-stimulated platelets. We also found that FRBE inhibited extracellular stimuli-responsive kinase 1/2, p38-mitogen-activated protein kinases and c-Jun N-terminal kinase phosphorylation. These results suggested that FRBE inhibited collagen-induced platelet aggregation, which was mediated by modulation of downstream signaling molecules. In conclusion, FRBE could be developed as a functional food against aberrant platelet activation-related cardiovascular diseases.