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 Dabir, D. V. Articles by Forman, M. S. Search for Related Content PubMed PubMed Citation Articles by Dabir, D. V. Articles by Forman, M. S.

(American Journal of Pathology. 2004;164:155-166.)
© 2004 American Society for Investigative Pathology

Expression of the Small Heat-Shock Protein B-Crystallin in Tauopathies with Glial Pathology

Deepa V. Dabir^*, John Q. Trojanowski^*, Christiane Richter-Landsberg, Virginia M.-Y. Lee^* and Mark S. Forman^*

From the Department of Pathology and Laboratory Medicine,^* Center for Neurodegenerative Disease Research, and the Institute on Aging, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania, and the Department of Biology, University of Oldenburg, Germany

Intracellular accumulations of filamentous material composed of tau proteins are defining features of sporadic and familial neurodegenerative disorders termed "tauopathies." In Alzheimer’s disease, the most common tauopathy, tau pathology is predominantly localized within neurons; however, robust glial pathology occurs in other tauopathies. Although the pathogenesis of tauopathies remains primarily unknown, molecular chaperones such as heat-shock proteins (HSPs) are implicated in these tau disorders as well as other neurodegenerative diseases characterized by the accumulation of insoluble protein aggregates such as -synuclein in Parkinson’s disease and polyglutamine in Huntington’s disease. We analyzed a variety of tauopathies with antibodies to a panel of HSPs to determine their role in the pathogenesis of these disorders. Although HSPs are not found in neuronal tau inclusions, we demonstrate increased expression of the small HSP B-crystallin in glial inclusions of both sporadic and familial tauopathies. B-crystallin was observed in a subset of astrocytic and oligodendrocytic tau inclusions as well as the neuropil thread pathology in cellular processes, but the co-expression of B-crystallin with tau inclusions was relatively specific to tauopathies with extensive glial pathology. Thus, increased B-crystallin expression in glial tau inclusions may represent a response by glia to the accumulation of misfolded or aggregated tau protein that is linked to the pathogenesis of the glial pathology and distinct from mechanisms underlying neuronal tau pathology in neurodegenerative disease.

This article has been cited by other articles:

				C. K. Iwahashi, D. H. Yasui, H.-J. An, C. M. Greco, F. Tassone, K. Nannen, B. Babineau, C. B. Lebrilla, R. J. Hagerman, and P. J. Hagerman Protein composition of the intranuclear inclusions of FXTAS Brain, January 1, 2006; 129(1): 256 - 271. [Abstract] [Full Text] [PDF]

				H.-Y. Shen, J.-C. He, Y. Wang, Q.-Y. Huang, and J.-F. Chen Geldanamycin Induces Heat Shock Protein 70 and Protects against MPTP-induced Dopaminergic Neurotoxicity in Mice J. Biol. Chem., December 2, 2005; 280(48): 39962 - 39969. [Abstract] [Full Text] [PDF]

				D. G. Arocena, C. K. Iwahashi, N. Won, A. Beilina, A. L. Ludwig, F. Tassone, P. H. Schwartz, and P. J. Hagerman Induction of inclusion formation and disruption of lamin A/C structure by premutation CGG-repeat RNA in human cultured neural cells Hum. Mol. Genet., December 1, 2005; 14(23): 3661 - 3671. [Abstract] [Full Text] [PDF]

				A. J. Macario and E. C. de Macario Sick Chaperones, Cellular Stress, and Disease N. Engl. J. Med., October 6, 2005; 353(14): 1489 - 1501. [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]

				M. S. Forman, D. Lal, B. Zhang, D. V. Dabir, E. Swanson, V. M.-Y. Lee, and J. Q. Trojanowski Transgenic Mouse Model of Tau Pathology in Astrocytes Leading to Nervous System Degeneration J. Neurosci., April 6, 2005; 25(14): 3539 - 3550. [Abstract] [Full Text] [PDF]

				C. W. Strey, D. Spellman, A. Stieber, J. O. Gonatas, X. Wang, J. D. Lambris, and N. K. Gonatas Dysregulation of Stathmin, a Microtubule-Destabilizing Protein, and Up-Regulation of Hsp25, Hsp27, and the Antioxidant Peroxiredoxin 6 in a Mouse Model of Familial Amyotrophic Lateral Sclerosis Am. J. Pathol., November 1, 2004; 165(5): 1701 - 1718. [Abstract] [Full Text] [PDF]