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      KCI등재 SCOPUS

      Hopea chinensis (Merr.) Hand.-Mazz. 메탄올 추출물이 신경세포에서 아밀로이드 전구 단백질 대사에 미치는 영향 = The Effects of MeOH Extract of Hopea chinensis (Merr.) Hand.-Mazz. on the Metabolism of Amyloid Precursor Protein in Neuroblastoma Cells

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      https://www.riss.kr/link?id=A106063806

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      다국어 초록 (Multilingual Abstract)

      Many plant derived phytochemicals have been considered as the main therapeutic strategy against Alzheimer’s disease (AD). AD is a progressive neurodegenerative disorder, and the most predominant cause of dementia in the elderly. Cholinergic deficit, senile plaque/b-amyloid (Ab) peptide deposition and oxidative stress have been identified as three main pathogenic pathways which contribute to the progression of AD. We screened many different plant species for their effective use in both modern and traditional system of medicines. In this study, we tested that MeOH extract of the stem bark of Hopea chinensis (Merr.) Hand.-Mazz. (HCM) affects on the processing of Amyloid precursor portein (APP) from the APPswe over-expressing Neuro2a cell line. We showed that HCM reduced the secretion level of Ab42 and Ab40 in a dose dependent manner. We found that HCM increased over 1.5 folds of the secretion level of sAPPa, a metabolite of a-secretase. Furthermore, we found that HCM inhibited acetylcholinesterase activity in vitro. We suggest that the stem bark of Hopea chinensis may be a useful source to develop a therapeutics for AD.
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      Many plant derived phytochemicals have been considered as the main therapeutic strategy against Alzheimer’s disease (AD). AD is a progressive neurodegenerative disorder, and the most predominant cause of dementia in the elderly. Cholinergic deficit,...

      Many plant derived phytochemicals have been considered as the main therapeutic strategy against Alzheimer’s disease (AD). AD is a progressive neurodegenerative disorder, and the most predominant cause of dementia in the elderly. Cholinergic deficit, senile plaque/b-amyloid (Ab) peptide deposition and oxidative stress have been identified as three main pathogenic pathways which contribute to the progression of AD. We screened many different plant species for their effective use in both modern and traditional system of medicines. In this study, we tested that MeOH extract of the stem bark of Hopea chinensis (Merr.) Hand.-Mazz. (HCM) affects on the processing of Amyloid precursor portein (APP) from the APPswe over-expressing Neuro2a cell line. We showed that HCM reduced the secretion level of Ab42 and Ab40 in a dose dependent manner. We found that HCM increased over 1.5 folds of the secretion level of sAPPa, a metabolite of a-secretase. Furthermore, we found that HCM inhibited acetylcholinesterase activity in vitro. We suggest that the stem bark of Hopea chinensis may be a useful source to develop a therapeutics for AD.

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      참고문헌 (Reference)

      1 "통계청 자료"

      2 Kuo, Y. M., "Water-soluble Abeta (N-40, N-42) oligomers in normal and Alzheimer disease brains" 271 : 4077-4081, 1996

      3 Selkoe, D. J., "Translating cell biology into therapeutic advances in Alzheimer's disease" 399 : 23-31, 1999

      4 Wang, R., "The profile of soluble amyloid ${\beta}$ protein in cultured cell media" 271 : 31894-31902, 1996

      5 Selkoe, D. J., "The cell biology of beta-amyloid precursor protein and presenilin in Alzheimer's disease" 8 : 447-453, 1998

      6 Hardy, J., "The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics" 297 : 353-356, 2002

      7 Sambamurti, K., "Targeting APP metabolism for the treatment of Alzheimer's disease" 56 : 211-227, 2002

      8 Takahashi, Y., "Sulindac sulfide is a noncompetitive gamma-secretase inhibitor that preferentially reduces Abeta 42 generation" 278 : 18664-18670, 2003

      9 Obregon, D., "Soluble amyloid precursor protein-${\alpha}$ modulates ${\beta}$-secretase activity and amyloid-${\beta}$ generation" 3 : 777-, 2012

      10 Jann, M. W., "Rivastigmine, a new-generation cholinesterase inhibitor for the treatment of Alzheimer's disease" 20 : 1-12, 2000

      1 "통계청 자료"

      2 Kuo, Y. M., "Water-soluble Abeta (N-40, N-42) oligomers in normal and Alzheimer disease brains" 271 : 4077-4081, 1996

      3 Selkoe, D. J., "Translating cell biology into therapeutic advances in Alzheimer's disease" 399 : 23-31, 1999

      4 Wang, R., "The profile of soluble amyloid ${\beta}$ protein in cultured cell media" 271 : 31894-31902, 1996

      5 Selkoe, D. J., "The cell biology of beta-amyloid precursor protein and presenilin in Alzheimer's disease" 8 : 447-453, 1998

      6 Hardy, J., "The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics" 297 : 353-356, 2002

      7 Sambamurti, K., "Targeting APP metabolism for the treatment of Alzheimer's disease" 56 : 211-227, 2002

      8 Takahashi, Y., "Sulindac sulfide is a noncompetitive gamma-secretase inhibitor that preferentially reduces Abeta 42 generation" 278 : 18664-18670, 2003

      9 Obregon, D., "Soluble amyloid precursor protein-${\alpha}$ modulates ${\beta}$-secretase activity and amyloid-${\beta}$ generation" 3 : 777-, 2012

      10 Jann, M. W., "Rivastigmine, a new-generation cholinesterase inhibitor for the treatment of Alzheimer's disease" 20 : 1-12, 2000

      11 Nunan, J., "Regulation of APP cleavage by alpha-, beta- and gamma-secretases" 483 : 6-10, 2000

      12 Skovronsky, D. M., "Protein kinase C-dependent alpha-secretase competes with beta-secretase for cleavage of amyloid-beta precursor protein in the trans-golgi network" 275 : 2568-2575, 2000

      13 Li, N., "Protective effects of ginsenosides Rg1 and Rb1 on an Alzheimer's disease mouse model: A metabolomics study" 985 : 54-61, 2015

      14 Fu, H., "Promising multifunctional anti-Alzheimer's dimer bis(7)-Cognitin acting as an activator of protein kinase C regulates activities of alpha-secretase and BACE-1 concurrently" 623 : 14-21, 2009

      15 Yan, T., "Polyphenolic acetylcholinesterase inhibitors from Hopea chinensis" 78 : 1015-1019, 2012

      16 Steiner, H., "PEN-2 is an integral component of the ${\gamma}$-secretase complex required for coordinated expression of presenilin and nicastrin" 277 : 39062-39065, 2002

      17 Citron, M., "Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice" 3 : 67-72, 1997

      18 Ge, H. M., "Immunosuppressive resveratrol aneuploids from Hopea chinensis" 16 : 6338-6345, 2010

      19 Ge, H. M., "Hoeahainol A: an acetylcholinesterase inhibitor from Hopea hainanensis" 14 : 376-381, 2008

      20 Corder, E. H., "Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families" 261 : 921-923, 1993

      21 Zarotsky, V., "Galantamine hydrobromide. an agent for Alzheimer's disease" 60 : 446-452, 2003

      22 Sugimoto, H., "Donepezil hydrochloride. a treatment drug for Alzheimer's disease" 1 : 63-73, 2001

      23 Tung, J. S., "Design of substrate-based inhibitors of human beta-secretase" 45 : 259-262, 2002

      24 Morris, J. C., "Classification of dementia and Alzheimer's disease" 165 : 41-50, 1996

      25 Uchida N, "Cholinergic involvement and synaptic dynamin 1 expression in Yokukansan-mediated improvement of spatial memory in a rat model of early Alzheimer's disease" 27 : 966-972, 2013

      26 Strittmatter, W. J., "Binding of human apolipoprotein E to synthetic amyloid beta peptide isoform-specific effects and implications for late-onset Alzheimer disease" 90 : 8098-8102, 1993

      27 Cai, H., "BACE1 is the major ${\beta}$-secretase for generation of $A{\beta}$ peptides by neurons" 4 : 233-234, 2001

      28 Harun A., "BACE1 inhibitory activity of fungal endophytic extracts from Malaysian medicinal plants" 11 : 79-, 2011

      29 Iqbal, K., "Alzheimer's disease. Advances in etiology, pathogenesis and therapeutics" John Wiley & Sons, Ltd 2001

      30 Leem, J. Y., "A role for presenilin 1 in regulating the delivery of amyloid precursor protein to the cell surface" 11 : 64-82, 2002

      31 Vassar, R., "${\beta}$-Secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE" 286 : 735-741, 1999

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      학술지 이력

      학술지 이력
      연월일 이력구분 이력상세 등재구분
      2023 평가예정 해외DB학술지평가 신청대상 (해외등재 학술지 평가)
      2020-01-01 평가 등재학술지 유지 (해외등재 학술지 평가) KCI등재
      2010-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2008-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2005-01-01 평가 등재학술지 선정 (등재후보2차) KCI등재
      2004-01-01 평가 등재후보 1차 PASS (등재후보1차) KCI등재후보
      2003-01-01 평가 등재후보학술지 유지 (등재후보1차) KCI등재후보
      2001-07-01 평가 등재후보학술지 선정 (신규평가) KCI등재후보
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      학술지 인용정보

      학술지 인용정보
      기준연도 WOS-KCI 통합IF(2년) KCIF(2년) KCIF(3년)
      2016 0.42 0.42 0.39
      KCIF(4년) KCIF(5년) 중심성지수(3년) 즉시성지수
      0.42 0.41 0.803 0.05
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