Searching for just a few words should be enough to get started. If you need to make more complex queries, use the tips below to guide you.
Article type: Research Article
Authors: Puig, B.a | Ferrer, I.a; b; * | Ludueña, R.F.c | Ávila, J.d
Affiliations: [a] Instituto de Neuropatología, IDIBELL-Hospital Universitario de Bellvitge, Spain | [b] Unidad de Neuropatología Experimental, Universidad de Barcelona, Campus Bellvitge, 08907, Spain | [c] Hospitalet de Llobregat, Barcelona; University of Texas Health Science Center, Department of Biochemistry, San Antonio, TX 78229-3900, USA | [d] Centro de Biología Molecular, CSIC, Universidad Autínoma de Madrid, Cantoblanco, 28049 Madrid, Spain
Correspondence: [*] Corresponding author: I. Ferrer, Instituto de Neuropatología, Servicio de Anatomía Patológica, Hospital Universitario de Bellvitge, calle Feixa Llarga sn, 08907 Hospitalet de Llobregat, Spain. Tel.: +34 93 4035808; E-mail: 8082ifa@comb.es; iferrer@csub.scs.es.
Abstract: The expression of βI-, βII- and βIII-tubulin isotypes was examined by immunohistochemistry in the entorhinal and transentorhinal cortices, hippocampus and dentate gyrus in normal human brains and in cases with Alzheimer's disease (AD), Pick's disease (PiD) and in argyrophilic grain disease (AGD). The results showed that βII-tubulin predominated in the upper layers (mainly layer II) and βIII-tubulin in the inner layers of the entorhinal and transentorhinal cortices in control brains. βII-tubulin immunoreactivity was higher than βIII-tubulin immunoreactivity in granular neurons of the dentate gyrus, whereas pyramidal neurons of the hippocampus proper were stained equally with anti-βII-tubulin and βIII-tubulin antibodies. No preferential layering distribution was observed for βI-tubulin. Polymerization assays with tubulin peptides following the method of microtubule-associated protein displacement demonstrated that the βI and βIII isotypes have a higher binding capacity for tau than does the βII isotype. Interestingly, about 60% of neurons with neurofibrillary tangles in layer II of the entorhinal and transentorhinal cortices in AD were selectively stained with anti-βII-tubulin antibodies. Moderate βII-tubulin immunoreactivity was also observed in Pick bodies in PiD. Taken together, these findings support the view that high βII-tubulin content is a contributing factor in the formation of abnormal hyper-phosphorylated tau aggregates.
Keywords: Alzheimer's disease, Pick's disease, tubulin, tau
DOI: 10.3233/JAD-2005-7303
Journal: Journal of Alzheimer's Disease, vol. 7, no. 3, pp. 213-220, 2005
IOS Press, Inc.
6751 Tepper Drive
Clifton, VA 20124
USA
Tel: +1 703 830 6300
Fax: +1 703 830 2300
sales@iospress.com
For editorial issues, like the status of your submitted paper or proposals, write to editorial@iospress.nl
IOS Press
Nieuwe Hemweg 6B
1013 BG Amsterdam
The Netherlands
Tel: +31 20 688 3355
Fax: +31 20 687 0091
info@iospress.nl
For editorial issues, permissions, book requests, submissions and proceedings, contact the Amsterdam office info@iospress.nl
Inspirees International (China Office)
Ciyunsi Beili 207(CapitaLand), Bld 1, 7-901
100025, Beijing
China
Free service line: 400 661 8717
Fax: +86 10 8446 7947
china@iospress.cn
For editorial issues, like the status of your submitted paper or proposals, write to editorial@iospress.nl
如果您在出版方面需要帮助或有任何建, 件至: editorial@iospress.nl