MOLECULAR BASIS OF BIOACTIVITY OF THE β-AMYLOID PROTEIN AND INHIBITORS OF ITS NEUROTOXICITY

It is now accepted that excessive deposition of the β-amyloid protein(βA) in specific regions of the brain as a result of either overexpression or abnormal cleavage of βA precursors or acceleration of aggregation of βA molecules in those tissues is prerequisite and most important in induction of Alz...

Full description

Saved in:
Bibliographic Details
Published in:Japanese Journal of Pharmacology 1996, Vol.71 (suppl.1), p.20-20
Main Authors: Tetsuro Mohri, Tsuneo Takadera, Matsumi Yamazaki, Naoki Sakura, Tadashi Hashimoto
Format: Article
Language:Japanese
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites
container_end_page 20
container_issue suppl.1
container_start_page 20
container_title Japanese Journal of Pharmacology
container_volume 71
creator Tetsuro Mohri
Tsuneo Takadera
Matsumi Yamazaki
Naoki Sakura
Tadashi Hashimoto
description It is now accepted that excessive deposition of the β-amyloid protein(βA) in specific regions of the brain as a result of either overexpression or abnormal cleavage of βA precursors or acceleration of aggregation of βA molecules in those tissues is prerequisite and most important in induction of Alzheimer s disease. The specific antiparallel β-sheet structure of lengths of βA were elucidated to be responsible for its neurotoxic effect on cultured brain neurons. Synthetic peptide fragments of βA such as β25-35 had varying degrees of neurotoxicity in cultured rat fetal hippocampal cells depending on the concentration in medium devoid of serum. The neurotoxicity of the peptide fragments was depressed by addition of bovine serum, cAMP and several kinds of insulinrelated hormones to medium. We have found natural iridoid compounds to be capable of depressing the neurotoxicity of β25-35(40 μM) dose-dependently as determined by release of lactate dehydrogenase from cultured rat hippocampal neurons.
format article
fullrecord <record><control><sourceid>medicalonline</sourceid><recordid>TN_cdi_medicalonline_journals_cf6jjopl_1996_0071s1_068_0020_0020934047</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>cf6jjopl_1996_0071s1_068_0020_0020934047</sourcerecordid><originalsourceid>FETCH-medicalonline_journals_cf6jjopl_1996_0071s1_068_0020_00209340473</originalsourceid><addsrcrecordid>eNqtjF1qg0AUhechhUqbPcwGhDuaqvM46ogXjFN0LBUKg7UKitFS6caykKypNmQJeTk_fJyzIxaAw-wXxoNHsl_X4RMc8N3AdbhFPo4qk1GViYKGosSSqoSGqESk8Q11_V91KunlbItjnSmM6WuhtMScijymmKcYolbFdYe6pLmsNq7eMdrWz-Shb6a129_8iSSJ1FFqn7qvoW2mZZ6GuTPj8vszb9y0vTeOy_dkGOeeAfDZygx4wRYduAp3D3Dw3bsd_QEjR1CV</addsrcrecordid><sourcetype>Publisher</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>MOLECULAR BASIS OF BIOACTIVITY OF THE β-AMYLOID PROTEIN AND INHIBITORS OF ITS NEUROTOXICITY</title><source>ScienceDirect Journals</source><creator>Tetsuro Mohri ; Tsuneo Takadera ; Matsumi Yamazaki ; Naoki Sakura ; Tadashi Hashimoto</creator><creatorcontrib>Tetsuro Mohri ; Tsuneo Takadera ; Matsumi Yamazaki ; Naoki Sakura ; Tadashi Hashimoto ; Hokuriku University School of Pharmacy</creatorcontrib><description>It is now accepted that excessive deposition of the β-amyloid protein(βA) in specific regions of the brain as a result of either overexpression or abnormal cleavage of βA precursors or acceleration of aggregation of βA molecules in those tissues is prerequisite and most important in induction of Alzheimer s disease. The specific antiparallel β-sheet structure of lengths of βA were elucidated to be responsible for its neurotoxic effect on cultured brain neurons. Synthetic peptide fragments of βA such as β25-35 had varying degrees of neurotoxicity in cultured rat fetal hippocampal cells depending on the concentration in medium devoid of serum. The neurotoxicity of the peptide fragments was depressed by addition of bovine serum, cAMP and several kinds of insulinrelated hormones to medium. We have found natural iridoid compounds to be capable of depressing the neurotoxicity of β25-35(40 μM) dose-dependently as determined by release of lactate dehydrogenase from cultured rat hippocampal neurons.</description><identifier>ISSN: 0021-5198</identifier><language>jpn</language><publisher>The Japanese Pharmacological Society</publisher><ispartof>Japanese Journal of Pharmacology, 1996, Vol.71 (suppl.1), p.20-20</ispartof><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010</link.rule.ids></links><search><creatorcontrib>Tetsuro Mohri</creatorcontrib><creatorcontrib>Tsuneo Takadera</creatorcontrib><creatorcontrib>Matsumi Yamazaki</creatorcontrib><creatorcontrib>Naoki Sakura</creatorcontrib><creatorcontrib>Tadashi Hashimoto</creatorcontrib><creatorcontrib>Hokuriku University School of Pharmacy</creatorcontrib><title>MOLECULAR BASIS OF BIOACTIVITY OF THE β-AMYLOID PROTEIN AND INHIBITORS OF ITS NEUROTOXICITY</title><title>Japanese Journal of Pharmacology</title><description>It is now accepted that excessive deposition of the β-amyloid protein(βA) in specific regions of the brain as a result of either overexpression or abnormal cleavage of βA precursors or acceleration of aggregation of βA molecules in those tissues is prerequisite and most important in induction of Alzheimer s disease. The specific antiparallel β-sheet structure of lengths of βA were elucidated to be responsible for its neurotoxic effect on cultured brain neurons. Synthetic peptide fragments of βA such as β25-35 had varying degrees of neurotoxicity in cultured rat fetal hippocampal cells depending on the concentration in medium devoid of serum. The neurotoxicity of the peptide fragments was depressed by addition of bovine serum, cAMP and several kinds of insulinrelated hormones to medium. We have found natural iridoid compounds to be capable of depressing the neurotoxicity of β25-35(40 μM) dose-dependently as determined by release of lactate dehydrogenase from cultured rat hippocampal neurons.</description><issn>0021-5198</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid/><recordid>eNqtjF1qg0AUhechhUqbPcwGhDuaqvM46ogXjFN0LBUKg7UKitFS6caykKypNmQJeTk_fJyzIxaAw-wXxoNHsl_X4RMc8N3AdbhFPo4qk1GViYKGosSSqoSGqESk8Q11_V91KunlbItjnSmM6WuhtMScijymmKcYolbFdYe6pLmsNq7eMdrWz-Shb6a129_8iSSJ1FFqn7qvoW2mZZ6GuTPj8vszb9y0vTeOy_dkGOeeAfDZygx4wRYduAp3D3Dw3bsd_QEjR1CV</recordid><startdate>1996</startdate><enddate>1996</enddate><creator>Tetsuro Mohri</creator><creator>Tsuneo Takadera</creator><creator>Matsumi Yamazaki</creator><creator>Naoki Sakura</creator><creator>Tadashi Hashimoto</creator><general>The Japanese Pharmacological Society</general><scope/></search><sort><creationdate>1996</creationdate><title>MOLECULAR BASIS OF BIOACTIVITY OF THE β-AMYLOID PROTEIN AND INHIBITORS OF ITS NEUROTOXICITY</title><author>Tetsuro Mohri ; Tsuneo Takadera ; Matsumi Yamazaki ; Naoki Sakura ; Tadashi Hashimoto</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-medicalonline_journals_cf6jjopl_1996_0071s1_068_0020_00209340473</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>jpn</language><creationdate>1996</creationdate><toplevel>online_resources</toplevel><creatorcontrib>Tetsuro Mohri</creatorcontrib><creatorcontrib>Tsuneo Takadera</creatorcontrib><creatorcontrib>Matsumi Yamazaki</creatorcontrib><creatorcontrib>Naoki Sakura</creatorcontrib><creatorcontrib>Tadashi Hashimoto</creatorcontrib><creatorcontrib>Hokuriku University School of Pharmacy</creatorcontrib><jtitle>Japanese Journal of Pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tetsuro Mohri</au><au>Tsuneo Takadera</au><au>Matsumi Yamazaki</au><au>Naoki Sakura</au><au>Tadashi Hashimoto</au><aucorp>Hokuriku University School of Pharmacy</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>MOLECULAR BASIS OF BIOACTIVITY OF THE β-AMYLOID PROTEIN AND INHIBITORS OF ITS NEUROTOXICITY</atitle><jtitle>Japanese Journal of Pharmacology</jtitle><date>1996</date><risdate>1996</risdate><volume>71</volume><issue>suppl.1</issue><spage>20</spage><epage>20</epage><pages>20-20</pages><issn>0021-5198</issn><abstract>It is now accepted that excessive deposition of the β-amyloid protein(βA) in specific regions of the brain as a result of either overexpression or abnormal cleavage of βA precursors or acceleration of aggregation of βA molecules in those tissues is prerequisite and most important in induction of Alzheimer s disease. The specific antiparallel β-sheet structure of lengths of βA were elucidated to be responsible for its neurotoxic effect on cultured brain neurons. Synthetic peptide fragments of βA such as β25-35 had varying degrees of neurotoxicity in cultured rat fetal hippocampal cells depending on the concentration in medium devoid of serum. The neurotoxicity of the peptide fragments was depressed by addition of bovine serum, cAMP and several kinds of insulinrelated hormones to medium. We have found natural iridoid compounds to be capable of depressing the neurotoxicity of β25-35(40 μM) dose-dependently as determined by release of lactate dehydrogenase from cultured rat hippocampal neurons.</abstract><pub>The Japanese Pharmacological Society</pub></addata></record>
fulltext fulltext
identifier ISSN: 0021-5198
ispartof Japanese Journal of Pharmacology, 1996, Vol.71 (suppl.1), p.20-20
issn 0021-5198
language jpn
recordid cdi_medicalonline_journals_cf6jjopl_1996_0071s1_068_0020_0020934047
source ScienceDirect Journals
title MOLECULAR BASIS OF BIOACTIVITY OF THE β-AMYLOID PROTEIN AND INHIBITORS OF ITS NEUROTOXICITY
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-11T01%3A16%3A06IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-medicalonline&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=MOLECULAR%20BASIS%20OF%20BIOACTIVITY%20OF%20THE%20%CE%B2-AMYLOID%20PROTEIN%20AND%20INHIBITORS%20OF%20ITS%20NEUROTOXICITY&rft.jtitle=Japanese%20Journal%20of%20Pharmacology&rft.au=Tetsuro%20Mohri&rft.aucorp=Hokuriku%20University%20School%20of%20Pharmacy&rft.date=1996&rft.volume=71&rft.issue=suppl.1&rft.spage=20&rft.epage=20&rft.pages=20-20&rft.issn=0021-5198&rft_id=info:doi/&rft_dat=%3Cmedicalonline%3Ecf6jjopl_1996_0071s1_068_0020_0020934047%3C/medicalonline%3E%3Cgrp_id%3Ecdi_FETCH-medicalonline_journals_cf6jjopl_1996_0071s1_068_0020_00209340473%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true