help button home button Am J Pathol ASIP 2008 Summer Academy, Molecular Methcanisms of Human Disease: Injury, Inflammation, and Tissue Repair
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 Yamaguchi, H.
Right arrow Articles by Harigaya, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yamaguchi, H.
Right arrow Articles by Harigaya, Y.

American Journal of Pathology, Vol 135, 593-597, Copyright © 1989 by American Society for Investigative Pathology


REGULAR ARTICLES

Electron micrograph of diffuse plaques. Initial stage of senile plaque formation in the Alzheimer brain

H Yamaguchi, Y Nakazato, S Hirai, M Shoji and Y Harigaya
College of Medical Care and Technology, Gunma University, Japan.

The ultrastructure of diffuse plaques (devoid of both amyloid core and swollen neurites) in the frontal cortex of an Alzheimer brain was examined, using paired routine electron microscopic ultrathin sections and adjacent 0.4-micron-thick semithin sections. The semithin sections, treated with formic acid and beta protein immunostain, showed abundant diffuse plaques. In the adjacent ultrathin section, diffuse plaques usually showed some scattered bundles of amyloid fibrils between focally blurred membranes of cell process. The diffuse plaques were nearly undetectable without the semithin beta protein immunostained preparations, because the neuropils within these plaques appeared almost normal morphologically. Capillaries, which rarely appeared in the center of the diffuse plaques, demonstrated no amyloid fibrils in their walls. These findings suggest that in the initial stages of senile plaque formation amyloid fibrils are formed sporadically between cell processes, but not around the capillaries.


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
J. McLaurin, T. Franklin, P. E. Fraser, and A. Chakrabartty
Structural Transitions Associated with the Interaction of Alzheimer beta -Amyloid Peptides with Gangliosides
J. Biol. Chem., February 20, 1998; 273(8): 4506 - 4515.
[Abstract] [Full Text] [PDF]


Home page
J. Neurosci.Home page
R.-W. Shin, K. Ogino, A. Kondo, T. C. Saido, J. Q. Trojanowski, T. Kitamoto, and J. Tateishi
Amyloid beta -Protein (Abeta ) 1-40 But Not Abeta 1-42 Contributes to the Experimental Formation of Alzheimer Disease Amyloid Fibrils in Rat Brain
J. Neurosci., November 1, 1997; 17(21): 8187 - 8193.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. H. J. Huang, D.-S. Yang, P. E. Fraser, and A. Chakrabartty
Alternate Aggregation Pathways of the Alzheimer beta -Amyloid Peptide. AN IN VITRO MODEL OF PREAMYLOID
J. Biol. Chem., November 10, 2000; 275(46): 36436 - 36440.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1989 by the American Society for Investigative Pathology.