HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Ksiezak-Reding, H. Articles by Yen, S. H. Search for Related Content PubMed PubMed Citation Articles by Ksiezak-Reding, H. Articles by Yen, S. H. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 263, Issue 17, 7948-7953, 06, 1988

Immunochemical and biochemical characterization of tau proteins in normal and Alzheimer's disease brains with Alz 50 and Tau-1

H Ksiezak-Reding, LI Binder and SH Yen
Department of Pathology, Albert Einstein College of Medicine, Bronx, New York 10461.

Microtubule-associated protein tau was characterized in 5 Alzheimer and 5 control brains using two monoclonal antibodies, Alz 50 and Tau-1. Quantitative analysis of immunoblots with the antibodies showed that both homogenate and supernatant fractions (12,000 x g) from Alzheimer brains contained 38-65% less tau immunoreactivity compared to normal brains. The reduction was found in all brain regions studied (frontal and temporal lobes and thalamus) and in both gray and white matter. In partially purified tau preparations, the yield of protein was lower in Alzheimer (by 35%) than in control brain. Incubation of brain proteins, transferred onto nitrocellulose paper, with alkaline phosphatase had either no effect or slightly increased the antibody binding to tau proteins from both brain tissues. Immunoblots of tau-enriched preparations subjected to two-dimensional gel electrophoresis showed no major changes in the staining pattern of tau isoforms in Alzheimer samples except for a weaker reactivity of the basic isovariants as compared to non-Alzheimer samples. The elution volume of tau from Alzheimer brain supernatant on a Sepharose CL-6B column was similar to that from non-Alzheimer brain and equal to that of aldolase (Mr = 158,000). Our data suggest that most of tau proteins from both types of brain have similar biochemical properties. The reduction in tau reactivity in Alzheimer tissue may be due to a reduction in neuronal cell population or incorporation of soluble tau into stable structures such as neurofibrillary tangles, since the tangles have been shown to react with anti-tau antibodies.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				A. Yuan, A. Kumar, C. Peterhoff, K. Duff, and R. A. Nixon Axonal Transport Rates In Vivo Are Unaffected by Tau Deletion or Overexpression in Mice J. Neurosci., February 13, 2008; 28(7): 1682 - 1687. [Abstract] [Full Text] [PDF]