Neurotrophic regulation of mouse muscle β‐amyloid protein precursor and α1‐antichymotrypsin as revealed by axotomy
- 1 May 1994
- journal article
- research article
- Published by Wiley in Journal of Neurobiology
- Vol. 25 (5), 503-514
- https://doi.org/10.1002/neu.480250505
Abstract
Kunitz-inhibitor containing forms of the β-amyloid precursor protein (βAPP), known also as protease nexin II (PNII), and α1-antichymotrypsin (α1-ACT), a serpin, are important components of the serine protease and inhibitor balance in many tissues. In the nervous system, this balance may have trophic or growth factor activity at different stages of development, after injury and in disease states. In the current study, using immunocytochemistry and Western blotting with antibodies against the human homologues, we analyzed whether denervation affected the localization of βAPP and α1-ACT in adult mouse muscle following axotomy. In mouse muscle, antitive band and anti-human βAPP antibody a band at 92 kD in both normal and denervated extracts. βAPP was present in normal mouse muscle at both neuromuscular junctions and within intramuscular nerves. α1-ACT was also detected at neuromuscular junctions, on the perineruim and endothelial cell surfaces. Following axotomy, both βAPP and α1-ACT disappeared from intramuscular nerves simultaneously. However, at the neuromuscular junction, α1-ACT decreased more rapidly with βAPP lingering before disappearing. Since both α1-ACT as well as βAPP are present within senile plaques in Alzheimer's disease brains such experiments with the nicotinic, cholinergic neuromuscular synapse in denervated muscle may help to focus experiments on the mechanism of synapse loss as well as plaque deposition in this disease. © 1994 John Wiley & Sons, Inc.Keywords
This publication has 65 references indexed in Scilit:
- Lounging in a lysosome: the intracellular lifestyle of Coxiella burnetiiCellular Microbiology, 2007
- Synaptic structure and development: The neuromuscular junctionCell, 1993
- Characterization of the Serpin, α1‐Antichymotrypsin, in Normal Human Cerebrospinal FluidJournal of Neurochemistry, 1992
- Crystal structure of cleaved human α1-antichymotrypsin at 2.7 å resolution and its comparison with other serpinsJournal of Molecular Biology, 1991
- Platelet Coagulation Factor XI a -Inhibitor, a Form of Alzheimer Amyloid Precursor ProteinScience, 1990
- Characterization and Chromosomal Localization of a cDNA Encoding Brain Amyloid of Alzheimer's DiseaseScience, 1987
- Plasminogen activator in mammalian skeletal muscle: characteristics of effect of denervation on urokinase-like and tissue activator.The Journal of cell biology, 1986
- Sequence homology between human .alpha.1-antichymotrypsin, .alpha.1-antitrypsin, and antithrombin IIIBiochemistry, 1983
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences of the United States of America, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970