help button home button Am J Pathol R & D Systems
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 Crain, B. J.
Right arrow Articles by Sisodia, S. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Crain, B. J.
Right arrow Articles by Sisodia, S. S.

American Journal of Pathology, Vol 149, 1087-1095, Copyright © 1996 by American Society for Investigative Pathology


REGULAR ARTICLES

Expression and distribution of amyloid precursor protein-like protein-2 in Alzheimer's disease and in normal brain

BJ Crain, W Hu, CI Sze, HH Slunt, EH Koo, DL Price, G Thinakaran and SS Sisodia
Department of Pathology (Neuropathology Laboratory), Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.

Amyloid precursor-like protein-2 (APLP-2) belongs to a family of homologous amyloid precursor-like proteins. In the present study we report on the expression and distribution of APLP-2 in fetal and adult human brain and in brains of patients with Alzheimer's disease. We demonstrate that APLP-2 mRNAs encoding isoforms predicted to undergo post-translational modification by chondroitin sulfate glycosaminoglycans are elevated in fetal and aging brains relative to the brains of young adults. Immunocytochemical labeling with APLP-2- specific antibodies demonstrates APLP-2 immunoreactivity in cytoplasmic compartments in neurons and astrocytes, in large part overlapping the distribution of the amyloid precursor protein. In Alzheimer's disease brain, APLP-2 antibodies also label a subset of neuritic plaques. APLP- 2 immunoreactivity is particularly conspicuous in large dystrophic neurites that also label with antibodies specific for APP and chromogranin A. In view of the age-dependent increase in levels of chondroitin sulfate glycosaminoglycan-modified forms of APLP-2 in aging brain and the accumulation of APLP-2 in dystrophic presynaptic elements, we suggest that APLP-2 may play roles in neuronal sprouting or in the aggregation, deposition, and/or persistence of beta-amyloid deposits.


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
H. J. Huttunen, J. Kuja-Panula, and H. Rauvala
Receptor for Advanced Glycation End Products (RAGE) Signaling Induces CREB-dependent Chromogranin Expression during Neuronal Differentiation
J. Biol. Chem., October 4, 2002; 277(41): 38635 - 38646.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. Ciesielski-Treska, G. Ulrich, L. Taupenot, S. Chasserot-Golaz, A. Corti, D. Aunis, and M.-F. Bader
Chromogranin A Induces a Neurotoxic Phenotype in Brain Microglial Cells
J. Biol. Chem., June 5, 1998; 273(23): 14339 - 14346.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. Ciesielski-Treska, G. Ulrich, S. Chasserot-Golaz, J. Zwiller, M.-O. Revel, D. Aunis, and M.-F. Bader
Mechanisms Underlying Neuronal Death Induced by Chromogranin A-activated Microglia
J. Biol. Chem., April 13, 2001; 276(16): 13113 - 13120.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1996 by the American Society for Investigative Pathology.