The recombinant C-terminal fragment of tetanus toxin protects against cholinotoxicity by intraseptal injection of β-amyloid peptide (25–35) in rats

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Published inNeuroscience Vol. 315; pp. 18 - 30
Main Authors Patricio-Martínez, A, Mendieta, L, Martínez, I, Aguilera, J, Limón, I.D
Format Journal Article
LanguageEnglish
Published United States Elsevier Ltd 19.02.2016
Subjects
acetylcholinesterase
Acetylcholinesterase - metabolism
Amyloid beta-Peptides - toxicity
amyloid-β(25–35)
Animals
Caspase 3 - metabolism
choline acetyltransferase
Choline O-Acetyltransferase - metabolism
Hc-TeTx
Hippocampus - drug effects
Hippocampus - metabolism
Hippocampus - pathology
Immunohistochemistry
Male
Maze Learning - drug effects
Maze Learning - physiology
medial septum
Neurology
Neuroprotective Agents - pharmacology
Nootropic Agents - pharmacology
Peptide Fragments - pharmacology
Peptide Fragments - toxicity
Random Allocation
Rats, Wistar
Septum of Brain - drug effects
Septum of Brain - metabolism
Septum of Brain - pathology
spatial memory
Spatial Memory - drug effects
Spatial Memory - physiology
Tetanus Toxin - pharmacology
reference errors
ACh
vesicular acetylcholine transporter
amino-cupric-silver
CNS
phosphate-buffered saline
medial septum
Aβ
amyloid-β (25–35)
nerve growth factor
WM
tropomyosin receptor kinases
ChAT
PBS
AChE
Trks
AD
Hematoxylin and eosin
Alzheimer’s disease
C-terminal domain of tetanus toxin
H&E
MS
spatial memory
SSI
acetylcholinesterase
NGF
isotonic saline solution
working memory errors
β amyloid peptide
central nervous system
A-Cu-Ag
choline acetyltransferase
Hc-TeTx
acetylcholine
RM
VAChT
amyloid-β(25–35)
amyloid-β((25–35))
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Abstract Graphical abstract
AbstractList Graphical abstract
[Display omitted] •The Hc-TeTx fragment has a cholino-trophic effect on rats with Aβ(25–35).•The Hc-TeTx fragment prevents neuronal death induced by Aβ(25–35) peptide.•The Hc-TeTx fragment prevents impairment of the spatial memory caused by Aβ(25–35). The recombinant C-terminal domain of tetanus toxin (Hc-TeTx) is a new non-toxic peptide of the tetanus toxin that exerts a protective action against glutamate excitotoxicity in motoneurons. Moreover, its efficacy as a neuroprotective agent has been demonstrated in several animal models of neurodegeneration. The eleven amino acids in the β amyloid peptide (Aβ25–35) mimic the toxic effects of the full β amyloid peptide (Aβ1–42), causing the impairment of the cholinergic system in the medial septum (MS) which, in turn, alters the septo-hippocampal pathway and leads to learning and memory impairments. The aim of this study was to examine the neuroprotective effects of the Hc-TeTx fragment against cholinotoxicity. The Hc-TeTx fragment (100ng) was injected into the rats intercranially, with the Aβ(25–35) (2μg) then injected into their MS. The animals were tested for spatial learning and memory in the eight-arm radial maze. The brains were removed to assess cholinergic markers, such as choline acetyltransferase (ChAT) and acetylcholinesterase (AChE), and to explore neurodegeneration in the MS and hippocampus, using amino-cupric silver and H&E staining. Finally, capase-3, a marker of apoptosis, was examined in the MS. Our results clearly demonstrate that the application of Hc-TeTx prevents the loss of cholinergic markers (ChAT and AChE), the activation of capase-3, and neurodegeneration in the MS and the CA1 and CA3 subfields of the hippocampus. All these improvements were reflected in spatial learning and memory performance, and were significantly higher compared with animals treated with Aβ(25–35). Interestingly, the single administration of Hc-TeTx into the MS modified the ChAT and AChE expression that affect cognitive processes, without inducing neurodegeneration or an increase in capase-3 expression in the MS and hippocampus. In summary, our findings suggest that the recombinant Hc-TeTx fragment offers effective protection for the septo-hippocampal pathway, given that it reduces the neurodegeneration caused by Aβ(25–35) and improves learning and memory processes.
The recombinant C-terminal domain of tetanus toxin (Hc-TeTx) is a new non-toxic peptide of the tetanus toxin that exerts a protective action against glutamate excitotoxicity in motoneurons. Moreover, its efficacy as a neuroprotective agent has been demonstrated in several animal models of neurodegeneration. The eleven amino acids in the β amyloid peptide (Aβ25-35) mimic the toxic effects of the full β amyloid peptide (Aβ1-42), causing the impairment of the cholinergic system in the medial septum (MS) which, in turn, alters the septo-hippocampal pathway and leads to learning and memory impairments. The aim of this study was to examine the neuroprotective effects of the Hc-TeTx fragment against cholinotoxicity. The Hc-TeTx fragment (100 ng) was injected into the rats intercranially, with the Aβ(25-35) (2 μg) then injected into their MS. The animals were tested for spatial learning and memory in the eight-arm radial maze. The brains were removed to assess cholinergic markers, such as choline acetyltransferase (ChAT) and acetylcholinesterase (AChE), and to explore neurodegeneration in the MS and hippocampus, using amino-cupric silver and H&E staining. Finally, capase-3, a marker of apoptosis, was examined in the MS. Our results clearly demonstrate that the application of Hc-TeTx prevents the loss of cholinergic markers (ChAT and AChE), the activation of capase-3, and neurodegeneration in the MS and the CA1 and CA3 subfields of the hippocampus. All these improvements were reflected in spatial learning and memory performance, and were significantly higher compared with animals treated with Aβ(25-35). Interestingly, the single administration of Hc-TeTx into the MS modified the ChAT and AChE expression that affect cognitive processes, without inducing neurodegeneration or an increase in capase-3 expression in the MS and hippocampus. In summary, our findings suggest that the recombinant Hc-TeTx fragment offers effective protection for the septo-hippocampal pathway, given that it reduces the neurodegeneration caused by Aβ(25-35) and improves learning and memory processes.
The recombinant C-terminal domain of tetanus toxin (Hc-TeTx) is a new non-toxic peptide of the tetanus toxin that exerts a protective action against glutamate excitotoxicity in motoneurons. Moreover, its efficacy as a neuroprotective agent has been demonstrated in several animal models of neurodegeneration. The eleven amino acids in the beta amyloid peptide (A beta 25-35) mimic the toxic effects of the full beta amyloid peptide (A beta 1 - 42), causing the impairment of the cholinergic system in the medial septum (MS) which, in turn, alters the septo-hippocampal pathway and leads to learning and memory impairments. The aim of this study was to examine the neuroprotective effects of the Hc-TeTx fragment against cholinotoxicity. The Hc-TeTx fragment (100ng) was injected into the rats intercranially, with the A beta (25 - 35) (2 mu g) then injected into their MS. The animals were tested for spatial learning and memory in the eight-arm radial maze. The brains were removed to assess cholinergic markers, such as choline acetyltransferase (ChAT) and acetylcholinesterase (AChE), and to explore neurodegeneration in the MS and hippocampus, using amino-cupric silver and H&E staining. Finally, capase-3, a marker of apoptosis, was examined in the MS. Our results clearly demonstrate that the application of Hc-TeTx prevents the loss of cholinergic markers (ChAT and AChE), the activation of capase-3, and neurodegeneration in the MS and the CA1 and CA3 subfields of the hippocampus. All these improvements were reflected in spatial learning and memory performance, and were significantly higher compared with animals treated with A beta (25 - 35). Interestingly, the single administration of Hc-TeTx into the MS modified the ChAT and AChE expression that affect cognitive processes, without inducing neurodegeneration or an increase in capase-3 expression in the MS and hippocampus. In summary, our findings suggest that the recombinant Hc-TeTx fragment offers effective protection for the septo-hippocampal pathway, given that it reduces the neurodegeneration caused by A beta (25 - 35) and improves learning and memory processes.
Author Martínez, I
Aguilera, J
Patricio-Martínez, A
Limón, I.D
Mendieta, L
Author_xml – sequence: 1
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  fullname: Martínez, I
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  fullname: Aguilera, J
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Keywords reference errors
ACh
vesicular acetylcholine transporter
amino-cupric-silver
CNS
phosphate-buffered saline
medial septum
Aβ
amyloid-β (25–35)
nerve growth factor
WM
tropomyosin receptor kinases
ChAT
PBS
AChE
Trks
AD
Hematoxylin and eosin
Alzheimer’s disease
C-terminal domain of tetanus toxin
H&E
MS
spatial memory
SSI
acetylcholinesterase
NGF
isotonic saline solution
working memory errors
β amyloid peptide
central nervous system
A-Cu-Ag
choline acetyltransferase
Hc-TeTx
acetylcholine
RM
VAChT
amyloid-β(25–35)
amyloid-β((25–35))
Language English
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  article-title: Inhibition by tetanus toxin of sodium-dependent, high-affinity [3H]5-hydroxytryptamine uptake in rat synaptosomes
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  article-title: Amyloid-beta (25–35) impairs memory and increases NO in the temporal cortex of rats
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  doi: 10.1016/j.neures.2008.11.006
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Snippet Graphical abstract
[Display omitted] •The Hc-TeTx fragment has a cholino-trophic effect on rats with Aβ(25–35).•The Hc-TeTx fragment prevents neuronal death induced by Aβ(25–35)...
The recombinant C-terminal domain of tetanus toxin (Hc-TeTx) is a new non-toxic peptide of the tetanus toxin that exerts a protective action against glutamate...
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SubjectTerms acetylcholinesterase
Acetylcholinesterase - metabolism
Amyloid beta-Peptides - toxicity
amyloid-β(25–35)
Animals
Caspase 3 - metabolism
choline acetyltransferase
Choline O-Acetyltransferase - metabolism
Hc-TeTx
Hippocampus - drug effects
Hippocampus - metabolism
Hippocampus - pathology
Immunohistochemistry
Male
Maze Learning - drug effects
Maze Learning - physiology
medial septum
Neurology
Neuroprotective Agents - pharmacology
Nootropic Agents - pharmacology
Peptide Fragments - pharmacology
Peptide Fragments - toxicity
Random Allocation
Rats, Wistar
Septum of Brain - drug effects
Septum of Brain - metabolism
Septum of Brain - pathology
spatial memory
Spatial Memory - drug effects
Spatial Memory - physiology
Tetanus Toxin - pharmacology
Title The recombinant C-terminal fragment of tetanus toxin protects against cholinotoxicity by intraseptal injection of β-amyloid peptide (25–35) in rats
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https://dx.doi.org/10.1016/j.neuroscience.2015.11.066
https://www.ncbi.nlm.nih.gov/pubmed/26687435
https://search.proquest.com/docview/1762374169
Volume 315
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