Neurotrophic regulation of mouse muscle β‐amyloid protein precursor and α1‐antichymotrypsin as revealed by axotomy

Mohammed Akaaboune, Jianxin Ma, Barry W. Festoff, Barry Greenberg, Daniel Hantaï

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)503-514
Number of pages12
JournalJournal of Neurobiology
Volume25
Issue number5
DOIs
StatePublished - Jan 1 1994
Externally publishedYes

Fingerprint

Axotomy
Muscle Proteins
Amyloid beta-Protein Precursor
Neuromuscular Junction
Muscles
Synapses
Serpins
Serine Proteinase Inhibitors
Antibodies
Amyloid Plaques
Denervation
Cholinergic Agents
Nervous System
Intercellular Signaling Peptides and Proteins
Alzheimer Disease
Endothelial Cells
Western Blotting
Immunohistochemistry
Wounds and Injuries
Brain

Keywords

  • Alzheimer's disease
  • cholinergic synapse
  • serine protease inhibitors
  • serpin
  • skeletal muscle

ASJC Scopus subject areas

  • Neuroscience(all)
  • Cellular and Molecular Neuroscience

Cite this

Neurotrophic regulation of mouse muscle β‐amyloid protein precursor and α1‐antichymotrypsin as revealed by axotomy. / Akaaboune, Mohammed; Ma, Jianxin; Festoff, Barry W.; Greenberg, Barry; Hantaï, Daniel.

In: Journal of Neurobiology, Vol. 25, No. 5, 01.01.1994, p. 503-514.

Research output: Contribution to journalArticle

Akaaboune, Mohammed ; Ma, Jianxin ; Festoff, Barry W. ; Greenberg, Barry ; Hantaï, Daniel. / Neurotrophic regulation of mouse muscle β‐amyloid protein precursor and α1‐antichymotrypsin as revealed by axotomy. In: Journal of Neurobiology. 1994 ; Vol. 25, No. 5. pp. 503-514.
@article{029a7cb90092421fae0278d6e91a90b5,
title = "Neurotrophic regulation of mouse muscle β‐amyloid protein precursor and α1‐antichymotrypsin as revealed by axotomy",
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. {\circledC} 1994 John Wiley & Sons, Inc.",
keywords = "Alzheimer's disease, cholinergic synapse, serine protease inhibitors, serpin, skeletal muscle",
author = "Mohammed Akaaboune and Jianxin Ma and Festoff, {Barry W.} and Barry Greenberg and Daniel Hanta{\"i}",
year = "1994",
month = "1",
day = "1",
doi = "10.1002/neu.480250505",
language = "English (US)",
volume = "25",
pages = "503--514",
journal = "Developmental Neurobiology",
issn = "1932-8451",
publisher = "John Wiley and Sons Inc.",
number = "5",

}

TY - JOUR

T1 - Neurotrophic regulation of mouse muscle β‐amyloid protein precursor and α1‐antichymotrypsin as revealed by axotomy

AU - Akaaboune, Mohammed

AU - Ma, Jianxin

AU - Festoff, Barry W.

AU - Greenberg, Barry

AU - Hantaï, Daniel

PY - 1994/1/1

Y1 - 1994/1/1

N2 - 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.

AB - 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.

KW - Alzheimer's disease

KW - cholinergic synapse

KW - serine protease inhibitors

KW - serpin

KW - skeletal muscle

UR - http://www.scopus.com/inward/record.url?scp=0028301839&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028301839&partnerID=8YFLogxK

U2 - 10.1002/neu.480250505

DO - 10.1002/neu.480250505

M3 - Article

C2 - 8071658

AN - SCOPUS:0028301839

VL - 25

SP - 503

EP - 514

JO - Developmental Neurobiology

JF - Developmental Neurobiology

SN - 1932-8451

IS - 5

ER -