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TDP-43 in neurodegenerative disorders Cook C; Zhang YJ; Xu YF; Dickson DW; Petrucelli LExpert Opin Biol Ther 2008[Jul]; 8 (7): 969-78BACKGROUND: The number of neurodegenerative diseases associated with pathological aggregates of transactivation response element (TAR)-DNA-binding protein 43 (TDP-43) has increased, leading to the new designation 'TDP-43 proteinopathy.' Biochemically, TDP-43 proteinopathies are characterized by decreased solubility, hyperphosphorylation, and cleavage of TDP-43 into 25- and 35-kDa fragments, and by altered cellular localization. OBJECTIVE: This review summarizes research characterizing the distribution of TDP-43 pathology in human postmortem brain tissue and discusses possible therapeutic strategies based on genetic and in vitro studies. METHODS: We reviewed recent studies of TDP-43 proteinopathy. RESULTS/CONCLUSION: Given that several different mutations can lead to TDP-43 proteinopathies, including mutations in progranulin and valosin-containing protein, research is needed to decipher and potentially exploit the link between these mutations and TDP-43 pathology.|Adenosine Triphosphatases/physiology[MESH]|Amyotrophic Lateral Sclerosis/genetics[MESH]|Animals[MESH]|Brain/metabolism[MESH]|Cell Cycle Proteins/physiology[MESH]|DNA-Binding Proteins/metabolism/*physiology[MESH]|Humans[MESH]|Intercellular Signaling Peptides and Proteins/chemistry[MESH]|Mice[MESH]|Models, Genetic[MESH]|Mutation[MESH]|Neurites/metabolism[MESH]|Neurodegenerative Diseases/genetics/*metabolism[MESH]|Phosphorylation[MESH]|Progranulins[MESH]|Response Elements[MESH]|Solubility[MESH]|Valosin Containing Protein[MESH] |
