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Pathological mechanism
Name
Abeta inhibits LTP both in soluble and fibrillar conformational states
Description
Abeta1-40 peptide in soluble and fibrillar forms (beta pleated sheets) that are morphologically distinct can both attenuate hippocampal long-term potentiation (LTP) in the CA1 in vivo. The fibrillar form may also influence transmitter release.
Hypothesis
LTP hypothesis
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Extracelular pathological element
β-Amyloid
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Intracelular pathological element
Pathological action
Inhibits
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Process
LTP
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Process action
Transmitter(s)
Receptor(s)
Channel(s)
Pharmacological Agent
Pharmacological Action
Brain region
Hippocampus
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Neuron
CA1 pyramidal neuron
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Cell model
Cellular compartment
General or unspecified
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PubMed ID
18237717
Citation
AlzWeb
Notes
Abeta1-40 peptide in soluble and fibrillar forms (beta pleated sheets) that are morphologically distinct can both attenuate hippocampal long-term potentiation (LTP) in the CA1 in vivo. The fibrillar form may also influence transmitter release.Schmid, A. W., Freir, D. B., & Herron, C. E. (2008). Inhibition of LTP in vivo by beta-amyloid peptide in different conformational states. Brain Res, 1197, 135-142.
Pathology
Alzheimer
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Stage
Early
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Question
Claim
Other categories referring to "
Abeta inhibits LTP both in soluble and fibrillar conformational states
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Revisions:
4
Last time:
7/31/2008 12:04:03 PM
Reviewer:
Pradeep Mutalik
Owner:
EAV/CR Schema Administrator
This database was supported by the Human Brain Project (NIDCD, NIMH, NIA, NICD, NINDS) and MURI (Multidisciplinary University Research Initiative). It is now supported by RO1 DC 009977 from the National Institute for Deafness and other Communication Disorders.
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