12月9日研究生进展类讲座(医学)

发布时间:十博体育官网2011-12-05浏览次数:544

 

 
主讲人:Prof. Jiming Kong, PhD 
Department of Human Anatomy and Cell Science 
University of Manitoba, Canada 
讲座时间:2011129(周五)下午400-500
地点:十博体育官网最新网站丁家桥校区综合楼二楼报告厅
主办单位:十博体育官网最新网站研究生院
承办单位:十博体育官网最新网站医学院
 
主讲人简介:
        孔吉明,博士研究生,师从于第一军医大学钟世镇院士。现为加拿大曼尼托巴大学解剖与细胞科学系终身教授、曼尼托巴大学医学院亚细胞研究中心主任。主要从事神经退行性疾病和精神性疾病的发病机理及治疗的研究工作。他在神经细胞死亡的分子调控研究中率先报道了一条新的细胞死亡通路,该研究处于国际领先地位。近年来主持美国、加拿大及中国-加拿大等全国和国际性研究项目10项,参与主持5项(含1项中国国家自然科学基金重点项目),获科研经费逾350万美元。孔教授与中国的科研合作,与重庆医科大学、南方医科大学和第三军医大学等科研院所有密切的合作。目前已发表论文60余篇。单篇论文最高引用达337次(J Kong, Z Xu - Journal of Neuroscience, 1998)。主持的实验室为国家级脑卒中研究中心(Canadian Stroke Network, Centers of Excellence of Canada) 成员,至今实验室已接收了20余名来自中国的研究生、博士后和访问学者的访问。自2002年至今,受到近20 所美国、加拿大和中国的大学的邀请作学术报告,多次担任美国、中国和加拿大科研课题评委,并参与国家自然科学奖评审。多次受邀在美国、加拿大及中国的国际学术会议上作大会主题报告。获得Heart and Stroke Foundation of Canada New Investigator Award (加拿大心脏和中风协会新研究员奖)和第三届中国青年科技奖等。
 
讲座内容:Neurodegenerative diseases: the risk factor of aging
Aging is the biggest risk factor for almost all neurodegenerative diseases. A progressive and irreversible accumulation of oxidative damage caused by reactive oxygen species has been suggested to impact on critical aspects of the aging process and contribute to pathogenesis of neurodegenerative diseases. In the lecture, I would like to present our recent data on posttranslational modification of the primary antioxidant SOD1 as a biomarker of the risk factor of aging. SOD1 is a 16KD protein with a known function of converting superoxide to water and hydrogen peroxide. Mutations in the SOD1 gene are linked to amyotrophic lateral sclerosis (ALS) and cause motoneuron degeneration by a gain of toxic properties. Recent studies from my laboratory support that the gain of toxic properties of mutant SOD1 may result from posttranslational oxidative modification of its cysteine 111 residue. Using a redox Western blot assay to detect oxidized SOD1, we have found that oxidization of total SOD1 protein in spinal cord tissues of transgenic mice expressing the G93A and G37R mutations of human SOD1, two mouse models of ALS, is increased by more than tenfold at the onset of the diseases as compared to the age-matched controls. I would also like to discuss how oxidation of SOD1 occurs. We have found that compromised protein disulfide isomerase function plays a role in the mismatching of disulfide bonds in SOD1 leading to its oxidation. Given the abundance of SOD1 in the brain, SOD1’s extremely slow turnover rates and its close association with reactive oxygen species, oxidative modification of SOD1 may play a role in other neurodegenerative diseases such as Alzheimer’s disease and Parkinson’s disease.

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