help button home button Am J Pathol Epitomics Buy 2 Antibodies Get 1 Free Special Offer
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Order Full text via Infotrieve
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Funato, H.
Right arrow Articles by Ihara, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Funato, H.
Right arrow Articles by Ihara, Y.

American Journal of Pathology, Vol 152, 983-992, Copyright © 1998 by American Society for Investigative Pathology


REGULAR ARTICLES

Astrocytes containing amyloid beta-protein (Abeta)-positive granules are associated with Abeta40-positive diffuse plaques in the aged human brain

H Funato, M Yoshimura, T Yamazaki, TC Saido, Y Ito, J Yokofujita, R Okeda and Y Ihara
Department of Neuropathology, Faculty of Medicine, University of Tokyo, Japan.

Amyloid beta-protein (Abeta) is the major component of senile plaques that emerge in the cortex during aging and appear most abundantly in Alzheimer's disease. In the course of our immunocytochemical study on a large number of autopsy cases, we noticed, in many aged nondemented cases, the presence of unique diffuse plaques in the cortex distinct from ordinary diffuse plaques by immunocytochemistry. The former were amorphous, very faintly Abeta-immunoreactive plaques resembling diffuse plaques, but they stained for Abeta40 and were associated with small cells containing Abeta-positive granules. A panel of amino- and carboxyl-terminal-specific Abeta antibodies showed that such Abeta40- positive diffuse plaques and cell-associated granules were composed exclusively of amino-terminally deleted Abeta terminating at Abeta40, - 42, and -43. Double immunostaining also showed that those Abeta- immunoreactive granules are located in astrocytes and not in microglia or neurons. Immunoelectron microscopy revealed that nonfibrillar Abeta immunoreactivity was located within lipofuscin-like granules in somewhat swollen astrocytes. These findings raise the possibility that astrocytes take up Abeta and attempt to degrade it in lysosomes in the aged brain.


This article has been cited by other articles:


Home page
J. Neurosci.Home page
M. Kitazawa, S. Oddo, T. R. Yamasaki, K. N. Green, and F. M. LaFerla
Lipopolysaccharide-Induced Inflammation Exacerbates Tau Pathology by a Cyclin-Dependent Kinase 5-Mediated Pathway in a Transgenic Model of Alzheimer's Disease
J. Neurosci., September 28, 2005; 25(39): 8843 - 8853.
[Abstract] [Full Text] [PDF]


Home page
Ann. N. Y. Acad. Sci.Home page
M. KITAZAWA, T. R. YAMASAKI, and F. M. LAFERLA
Microglia as a Potential Bridge between the Amyloid {beta}-Peptide and Tau
Ann. N.Y. Acad. Sci., December 1, 2004; 1035(1): 85 - 103.
[Abstract] [Full Text] [PDF]


Home page
Ann. N. Y. Acad. Sci.Home page
N. H. GREIG, M. P. MATTSON, T. PERRY, S. L. CHAN, T. GIORDANO, K. SAMBAMURTI, J. T. ROGERS, H. OVADIA, and D. K. LAHIRI
New Therapeutic Strategies and Drug Candidates for Neurodegenerative Diseases: p53 and TNF-{alpha} Inhibitors, and GLP-1 Receptor Agonists
Ann. N.Y. Acad. Sci., December 1, 2004; 1035(1): 290 - 315.
[Abstract] [Full Text] [PDF]


Home page
AJGPHome page
L. D. Baker, K. Sambamurti, S. Craft, M. Cherrier, M. A. Raskind, F. Z. Stanczyk, S. R. Plymate, and S. Asthana
17{beta}-Estradiol Reduces Plasma A{beta}40 for HRT-Naive Postmenopausal Women With Alzheimer Disease: A Preliminary Study
Am J Geriatr Psychiatry, April 1, 2003; 11(2): 239 - 244.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
K. T. Y. Shaw, T. Utsuki, J. Rogers, Q.-S. Yu, K. Sambamurti, A. Brossi, Y.-W. Ge, D. K. Lahiri, and N. H. Greig
Phenserine regulates translation of beta -amyloid precursor protein mRNA by a putative interleukin-1 responsive element, a target for drug development
PNAS, June 7, 2001; (2001) 131152998.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
K. T. Y. Shaw, T. Utsuki, J. Rogers, Q.-S. Yu, K. Sambamurti, A. Brossi, Y.-W. Ge, D. K. Lahiri, and N. H. Greig
Phenserine regulates translation of beta -amyloid precursor protein mRNA by a putative interleukin-1 responsive element, a target for drug development
PNAS, June 19, 2001; 98(13): 7605 - 7610.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1998 by the American Society for Investigative Pathology.