This Article Full Text Full Text (PDF) Purchase Article View Shopping Cart Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kinoshita, A. Articles by Kimura, J. Search for Related Content PubMed PubMed Citation Articles by Kinoshita, A. Articles by Kimura, J.

(American Journal of Pathology. 1998;153:1551-1560.)
© 1998 American Society for Investigative Pathology

Regular Articles

Identification of Septins in Neurofibrillary Tangles in Alzheimer's Disease

Ayae Kinoshita* , Makoto Kinoshita , Haruhiko Akiyama§ , Hidekazu Tomimoto* , Ichiro Akiguchi* , Sharad Kumar¶ , Makoto Noda and Jun Kimura*

From the Departments of Neurology* and Molecular Oncology, Kyoto University Graduate School of Medicine, Yoshida Konoe-cho, Sakyo-ku, Kyoto, Japan; the Department of Neuropathology,§ Tokyo Institute of Psychiatry, Tokyo, Japan; and the Hanson Centre for Cancer Research,^¶ Institute of Medical and Veterinary Science, Adelaide, Australia

Septins are evolutionarily conserved cytoskeletal GTPases that can form heteropolymer complexes involved in cytokinesis and other cellular processes. We detected expression of the human septin genes Nedd5, H5, Diff6, and hCDC10 in postmortem brain tissues using the reverse transcription-coupled polymerase chain reaction and their products by immunoblot analysis. Four antibodies directed against three septins, Nedd5, H5, and Diff6, consistently labeled neurofibrillary tangles, neuropil threads, and dystrophic neurites in the senile plaques in brains affected by Alzheimer's disease but did not label obvious structures in young control brains. Immunoelectron microscopy revealed that Nedd5 localized to the paired helical filaments. Pre-tangles, the precursory granular deposits that accumulate in the neuronal cytoplasm, also were labeled with the antibodies. These findings suggest that at least the three septins are associated with tau-based paired helical filament core, and may contribute to the formation of neurofibrillary tangle as integral constituents of paired helical filaments.

This article has been cited by other articles:

				X. Xin, M. Pache, B. Zieger, I. Bartsch, C. Prunte, J. Flammer, and P. Meyer Septin Expression in Proliferative Retinal Membranes J. Histochem. Cytochem., November 1, 2007; 55(11): 1089 - 1094. [Abstract] [Full Text] [PDF]

				E. E. Benarroch Lipid rafts, protein scaffolds, and neurologic disease Neurology, October 16, 2007; 69(16): 1635 - 1639. [Full Text] [PDF]

				G. VALESINI, C. ALESSANDRI, D. CELESTINO, and F. CONTI Anti-Endothelial Antibodies and Neuropsychiatric Systemic Lupus Erythematosus Ann. N.Y. Acad. Sci., June 1, 2006; 1069(1): 118 - 128. [Abstract] [Full Text] [PDF]

				M. Pache, B. Zieger, S. Blaser, and P. Meyer Immunoreactivity of the Septins SEPT4, SEPT5, and SEPT8 in the Human Eye J. Histochem. Cytochem., September 1, 2005; 53(9): 1139 - 1147. [Abstract] [Full Text] [PDF]

				D. C. David, S. Hauptmann, I. Scherping, K. Schuessel, U. Keil, P. Rizzu, R. Ravid, S. Drose, U. Brandt, W. E. Muller, et al. Proteomic and Functional Analyses Reveal a Mitochondrial Dysfunction in P301L Tau Transgenic Mice J. Biol. Chem., June 24, 2005; 280(25): 23802 - 23814. [Abstract] [Full Text] [PDF]

				C. Martinez and J. Ware Mammalian Septin Function in Hemostasis and Beyond Experimental Biology and Medicine, December 1, 2004; 229(11): 1111 - 1119. [Abstract] [Full Text] [PDF]

				M. Versele, B. Gullbrand, M. J. Shulewitz, V. J. Cid, S. Bahmanyar, R. E. Chen, P. Barth, T. Alber, and J. Thorner Protein-Protein Interactions Governing Septin Heteropentamer Assembly and Septin Filament Organization in Saccharomyces cerevisiae Mol. Biol. Cell, October 1, 2004; 15(10): 4568 - 4583. [Abstract] [Full Text] [PDF]

				L. Liao, D. Cheng, J. Wang, D. M. Duong, T. G. Losik, M. Gearing, H. D. Rees, J. J. Lah, A. I. Levey, and J. Peng Proteomic Characterization of Postmortem Amyloid Plaques Isolated by Laser Capture Microdissection J. Biol. Chem., August 27, 2004; 279(35): 37061 - 37068. [Abstract] [Full Text] [PDF]

				N. Kinoshita, K. Kimura, N. Matsumoto, M. Watanabe, M. Fukaya, and C. Ide Mammalian septin Sept2 modulates the activity of GLAST, a glutamate transporter in astrocytes Genes Cells, January 1, 2004; 9(1): 1 - 14. [Abstract] [Full Text] [PDF]

				M. Ihara, H. Tomimoto, H. Kitayama, Y. Morioka, I. Akiguchi, H. Shibasaki, M. Noda, and M. Kinoshita Association of the Cytoskeletal GTP-binding Protein Sept4/H5 with Cytoplasmic Inclusions Found in Parkinson's Disease and Other Synucleinopathies J. Biol. Chem., June 20, 2003; 278(26): 24095 - 24102. [Abstract] [Full Text] [PDF]

				Y. Zhang, J. Gao, K. K. K. Chung, H. Huang, V. L. Dawson, and T. M. Dawson Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1 PNAS, November 8, 2000; (2000) 240347797. [Abstract] [Full Text]

				J. Xue, X. Wang, C. S. Malladi, M. Kinoshita, P. J. Milburn, I. Lengyel, J. A. P. Rostas, and P. J. Robinson Phosphorylation of a New Brain-specific Septin, G-septin, by cGMP-dependent Protein Kinase J. Biol. Chem., March 31, 2000; 275(14): 10047 - 10056. [Abstract] [Full Text] [PDF]

				Y. Zhang, J. Gao, K. K. K. Chung, H. Huang, V. L. Dawson, and T. M. Dawson Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1 PNAS, November 21, 2000; 97(24): 13354 - 13359. [Abstract] [Full Text] [PDF]