Tohoku University · Medicine
K. Kawahata 교수의 연구실은 신경퇴행성질환, 특히 파킨슨병과 관련된 단백질의 기능과 병리학적 역할을 중심으로 연구를 진행하고 있습니다. 주로 α-시뉴클레인의 비정상적 축적과 관련된 단백질 상호작용, 지방산 수용체인 FABP3의 역할, 도파민성 신경세포의 대사 및 단백질 분해 경로에 초점을 맞추고 있습니다. 또한, 뇌에서의 전기적 신호 전달과 세포 내 환경 변화를 실시간으로 측정할 수 있는 고해상도 레이저 간섭계 기술 개발도 함께 수행하고 있습니다.
Figures are computed from collected data and may differ slightly.
A multichannel far-infrared laser interferometer system has been developed for the measurement of the spatial and temporal behaviors of the electron density on the Large Helical Device (LHD) at the National Institute for Fusion Science. Of several candidates for high power laser sources a 119 μm CH3OH laser was taken as a probing light. The optical configuration is of the Michelson interferometer type with 13 channels. The optical system of the interferometer is mounted on a massive stainless fr
α-Synuclein is a protein with a molecular weight of 14.5 kDa and consists of 140 amino acids encoded by the <i>SNCA</i> gene. Missense mutations and gene duplications in the <i>SNCA</i> gene cause hereditary Parkinson's disease. Highly phosphorylated and abnormally aggregated α-synuclein is a major component of Lewy bodies found in neuronal cells of patients with sporadic Parkinson's disease, dementia with Lewy bodies, and glial cytoplasmic inclusion bodies in oligodendrocytes with multiple syst
Nigrostriatal dopaminergic systems govern physiological functions related to locomotion, and their dysfunction leads to movement disorders, such as Parkinson's disease and dopa-responsive dystonia (Segawa disease). Previous studies revealed that expression of the gene encoding nigrostriatal tyrosine hydroxylase (TH), a rate-limiting enzyme of dopamine biosynthesis, is reduced in Parkinson's disease and dopa-responsive dystonia; however, the mechanism of TH depletion in these disorders remains un
α-Synuclein is an abundant neuronal protein that accumulates in insoluble inclusions in Parkinson's disease and other synucleinopathies. Fatty acids partially regulate α-Synuclein accumulation, and mesencephalic dopaminergic neurons highly express fatty acid-binding protein 3 (FABP3). We previously demonstrated that FABP3 knockout mice show decreased α-Synuclein oligomerization and neuronal degeneration of tyrosine hydroxylase (TH)-positive neurons <i>in vivo</i>. In this study, we newly investi
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