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RISS 인기검색어
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- 저자 : Buxbaum, (검색결과 7 건)
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The Role of Preseniline in Apoptosis
Buxbaum, Joseph D. 한림대학교 한림과학원 부설 환경ㆍ생명과학연구소 1997 국제학술회의 Vol.1997 No.-
Because the presenilin mutations account for the majority of cases of inherited early onset forms of AD, understanding the normal function of the presenilins and how mutations in these proteins lead to Alzheimer disease are central questions in Alzheimer's research. In the following sections, the possible role of presenilins in apoptosis will be reviewed. Particularly, evidence that th COOH-terminus of presenilin-2 and, by analogy, of presenilin-1 cause apoptosis by interaction with as yet unidentified protein will be discussed. It will then be argued that identifying protein which interacts with the COOH-terminus of PS-2 and mediates its effects on apoptosis is an important goal in Alzheimer's research. As a means of achieving this goal, we propose to use the yeast two-hybrid system to identify proteins which bind to the COOH-terminus of PS-2 and to then study their effects on apoptosis.
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Kwang Rok Kim(김광록),Hannah Buxbaum(한나 벅스바움) 강원대학교 비교법학연구소 2018 江原法學 Vol.55 No.-
우리나라는 최근 자본시장과 금융투자업에 관한 법률(“자본시장법”)을 제 · 개정하여 집합투자기구에 대한 매우 다양한 형태의 운용을 제시한 바 있다. 그 중 회사형 집합투자기구는 미국을 비롯한 세계 금융시장에서 하나의 새로운 트렌드가 된 지 이미 오래고, 미국 금융시장을 성장시키는 매우 중요한 동력으로서 역할과 기능을 했다고 평가된다. 그러나 이러한 회사형 집합투자기구는 우리나라 시장에서 만큼은 그 역할과 기능을 다 하지 못한 것으로 평가된다. 따라서 이 연구는 기본적으로 미국 및 세계 금융시장에서의 회사형 집합투자기구에 대한 법적 프레임과 투자자 보호체계를 살펴봄으로써 우리나라 자본시장법상 회사형 집합투자기구 및 투자자보호방안을 제시하는 것을 목적으로 한다. 이를 위하여 이 연구는 회사형 집합투자기구에 대한 미국의 관련법을 분석하고 그에 따른 투자자보호에 대한 법적 쟁점을 살펴보고자 한다. 구체적으로는 회사형 집합투자기구에 대한 미국의 연방법을 살펴본다. 특히 투자자 보호 문제는 미국 연방 증권거래위원회의 Rule 482(g)를 비롯하여 1933년 증권법, 1934년 증권거래법 및 1940년 투자회사법의 입장에서 정부차원의 제한 및 자율보호프로그램 등을 살펴본다. Even though the Korean government enacted the CMA which allowed CISC as well as collective investment scheme in the form of a limited partnership and of a limited liability company, expanding the type of investment companies in order to promote various types of invest companies, the collective investment scheme in the form of corporation is not active in the Korean Financial market. In the contrast, it has been largely spreaded to all over the U.S. and there are abundant research and study materials related to CISC. In that, this research is to analyze CISC in the United States, including in the international financial markets and its limitation on investor protection in order to suggest some betterment from the perspective of the related U.S. laws to the collective investment scheme in Korean financial market.
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Phosphorylation of calsenilin at Ser63 regulates its cleavage by caspase-3
Choi, Eun-Kyoung,Miller, J.S.,Zaidi, N.F.,Salih, E.,Buxbaum, J.D.,Wasco, W. 한림대학교 환경·생명과학연구소 2003 [일송 국제심포지엄] 노화와 만성퇴행성 신경질환 Vol.- No.5
Calsenilin is a member of the neuronal calcium sensor(NCS) family of proteins that interacts with the presenilins. Casenilin has been found to act as a Kv4α channel interactor and as a transcriptional repressor. We have recently shown that calsenilin can be cleaved by caspase-3 and that its cleavage separates the conserved calcium-binding domain from the variable N-terminal domain. Here we demonstrate that calsenilin can be phosphorylated by casein kinase I and that its phosphorylation can be regulated by intracellular calcium. In addition, phosphorylate calsenilin is a substrate for serine/threonine protein phosphatase(PP) 1 and/or 2A. Phosphorylation within the N-terminal domain at Ser63, the major phosphorylation site of calsenilin, inhibits cleavage of the molecule by caspase-3. Given that the N-terminal domain of calsenilin is not conserved in the larger NCS family including other KChIP/CALP proteins, phosphorylation of calsenilin may regulate a functional role that is unique to this member of the superfamily
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Calsenilin, a Presenilin Interactor, Regulates RhoA Signaling and Neurite Outgrowth
Kim, Hee-Jun,Lee, Won-Haeng,Kim, Mo-Jong,Shin, Sunmee,Jang, Byungki,Park, Jae-Bong,Wasco, Wilma,Buxbaum, Joseph D.,Kim, Yong-Sun,Choi, Eun-Kyoung MDPI 2018 INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES Vol.19 No.4
<P>Calsenilin modulates A-type potassium channels, regulates presenilin-mediated γ-secretase activity, and represses prodynorphin and <I>c-fos</I> genes expression. RhoA is involved in various cellular functions including proliferation, differentiation, migration, transcription, and regulation of the actin cytoskeleton. Although recent studies demonstrate that calsenilin can directly interact with RhoA and that RhoA inactivation is essential for neuritogenesis, it is uncertain whether there is a link between calsenilin and RhoA-regulated neuritogenesis. Here, we investigated the role of calsenilin in RhoA-regulated neuritogenesis using in vitro and in vivo systems. We found that calsenilin induced RhoA inactivation, which accompanied RhoA phosphorylation and the reduced phosphorylation levels of LIM kinase (LIMK) and cofilin. Interestingly, PC12 cells overexpressing either full-length (FL) or the caspase 3-derived C-terminal fragment (CTF) of calsenilin significantly inactivated RhoA through its interaction with RhoA and p190 Rho GTPase-activating protein (p190RhoGAP). In addition, cells expressing FL and the CTF of calsenilin had increased neurite outgrowth compared to cells expressing the N-terminal fragment (NTF) of calsenilin or vector alone. Moreover, Tat-C3 and Y27632 treatment significantly increased the percentage of neurite-bearing cells, neurite length, and the number of neurites in cells. Finally, calsenilin deficiency in the brains of calsenilin-knockout mice significantly interfered with RhoA inactivation. These findings suggest that calsenilin contributes to neuritogenesis through RhoA inactivation.</P>
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Calsenilin regulates presenilin 1/γ‐secretase‐mediated N‐cadherin ∊‐cleavage and β‐catenin signaling
Jang, Changhwan,Choi, Jin‐,Kyu,Na, Yeo‐,Jung,Jang, Byungki,Wasco, Wilma,Buxbaum, Joseph D.,Kim, Yong‐,Sun,Choi, Eun‐,Kyoung Federation of American Society for Experimental Bi 2011 The FASEB Journal Vol.25 No.12
<P>Presenilin 1 (PS1) is a component of the γ-secretase complex that cleaves a variety of type I membrane proteins, including the β-amyloid precursor protein (β-APP), Notch, and neuronal (N)- and epithelial (E)-cadherins. N-cadherin is an essential adhesion molecule that forms a complex with, and is cleaved by, PS1/γ-secretase and β-catenin in the plasma membrane. The purpose of this study was to determine whether calsenilin, a presenilin-interacting protein, has a functional role in PS1/γ-secretase-mediated N-cadherin ε-cleavage using Western blot analysis, RT-PCR, immunoprecipitation, subcellular fractionation, biotinylation, and a luciferase reporter assay in SH-SY5Y neuroblastoma cells. Here, we demonstrate that the expression of calsenilin leads to a disruption of PS1/γ-secretase-mediated ε-cleavage of N-cadherin, which results in the significant accumulation of N-cadherin C-terminal fragment 1 (Ncad/CTF1), the reduction of cytoplasmic Ncad/CTF2 release, and a deceleration of PS1-CTF delivery to the cell surface. Interestingly, we also found that the expression of calsenilin is associated with the redistribution of β-catenin from the cell surface to a cytoplasmic pool, as well as with the negative regulation of genes that are targets of T-cell factor/β-catenin nuclear signaling. Taken together, our findings suggest that calsenilin is a novel negative regulator of N-cadherin processing that plays an important role in β-catenin signaling.</P>
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