DJ-1 is present in a large molecular complex in human brain tissue and interacts with [alpha]-synuclein

• Published in: Journal of neurochemistry Vol. 93; no. 6; p. 1524
• Main Authors: Meulener, Marc C, Graves, Charles L, Sampathu, Deepak M, Armstrong-Gold, Cecilia E, Bonini, Nancy M, Giasson, Benoit I
• Format: Journal Article
• Language: English
• Published: New York Blackwell Publishing Ltd 01.06.2005
• Subjects: Brain; Molecular biology; Neurological disorders; Proteins
• ISSN: 0022-3042; 1471-4159
• DOI: 10.1111/j.1471-4159.2005.03145.x

DJ-1 is a ubiquitously expressed protein involved in various cellular processes including cell proliferation, RNA-binding, and oxidative stress. Mutations that result in loss of DJ-1 function lead to early onset parkinsonism in humans, and DJ-1 protein is present in pathological lesions of several tauopathies and synucleinopathies. In order to further investigate the role of DJ-1 in human neurodegenerative disease, we have generated novel polyclonal and monoclonal antibodies to human DJ-1 protein. We have characterized these antibodies and confirmed the pathological co-localization of DJ-1 with other neurodegenerative disease-associated proteins, as well as the decrease in DJ-1 solubility in disease tissue. In addition, we report the presence of DJ-1 in a large molecular complex (> 2000 kDa), and provide evidence for an interaction between endogenous DJ-1 and alpha-synuclein in normal and diseased tissue. These findings provide new avenues towards the study of DJ-1 function and how loss of its activity may lead to parkinsonism. Furthermore, our results provide further evidence for the interplay between neurodegenerative disease-associated proteins. [PUBLICATION ABSTRACT]