Reelin in plaques of β-amyloid precursor protein and presenilin-1 double-transgenic mice
There is circumstantial evidence that the reelin signaling pathway may contribute to neurodegeneration in the adult brain and could be linked to Alzheimer's disease (AD). In the present immunohistochemical report we studied the reelin expression profile in double-transgenic mice that express bo...
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| Veröffentlicht in: | Neuroscience letters 2001-12, Vol.316 (3), p.145-148 |
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| creator | Wirths, Oliver Multhaup, Gerd Czech, Christian Blanchard, Véronique Tremp, Günter Pradier, Laurent Beyreuther, Konrad Bayer, Thomas A. |
| description | There is circumstantial evidence that the reelin signaling pathway may contribute to neurodegeneration in the adult brain and could be linked to Alzheimer's disease (AD). In the present immunohistochemical report we studied the reelin expression profile in double-transgenic mice that express both human mutant β-amyloid precursor protein (APP) and human mutant presenilin-1. We were able to demonstrate that reelin immunostaining was found together with human APP in the neuritic component of many AD-typical plaques in both hippocampus and neocortex. This observation gives the first evidence for the association of reelin with amyloid deposits. |
| doi_str_mv | 10.1016/S0304-3940(01)02399-0 |
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In the present immunohistochemical report we studied the reelin expression profile in double-transgenic mice that express both human mutant β-amyloid precursor protein (APP) and human mutant presenilin-1. We were able to demonstrate that reelin immunostaining was found together with human APP in the neuritic component of many AD-typical plaques in both hippocampus and neocortex. This observation gives the first evidence for the association of reelin with amyloid deposits.</description><identifier>ISSN: 0304-3940</identifier><identifier>EISSN: 1872-7972</identifier><identifier>DOI: 10.1016/S0304-3940(01)02399-0</identifier><identifier>PMID: 11744223</identifier><identifier>CODEN: NELED5</identifier><language>eng</language><publisher>Shannon: Elsevier Ireland Ltd</publisher><subject>Alzheimer Disease - genetics ; Alzheimer Disease - metabolism ; Alzheimer Disease - pathology ; Alzheimer's disease ; Amyloid beta-Protein Precursor - genetics ; Amyloid beta-Protein Precursor - metabolism ; Amyloid deposits ; Animals ; Biological and medical sciences ; Cell Adhesion Molecules, Neuronal - genetics ; Cell Adhesion Molecules, Neuronal - metabolism ; Cerebral Cortex - metabolism ; Cerebral Cortex - pathology ; Cerebral Cortex - physiopathology ; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases ; Extracellular Matrix Proteins - genetics ; Extracellular Matrix Proteins - metabolism ; Female ; Hippocampus - metabolism ; Hippocampus - pathology ; Hippocampus - physiopathology ; Immunohistochemistry ; Immunostaining ; Interneurons - metabolism ; Interneurons - pathology ; Male ; Medical sciences ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Mice ; Mice, Knockout ; Mice, Transgenic ; Nerve Tissue Proteins ; Neuritic plaques ; Neurology ; Plaque, Amyloid - genetics ; Plaque, Amyloid - metabolism ; Plaque, Amyloid - pathology ; Presenilin ; Presenilin-1 ; Pyramidal Cells - metabolism ; Pyramidal Cells - pathology ; Serine Endopeptidases ; Transgenic mice ; β-Amyloid precursor protein</subject><ispartof>Neuroscience letters, 2001-12, Vol.316 (3), p.145-148</ispartof><rights>2001 Elsevier Science Ireland Ltd</rights><rights>2002 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c443t-9f905fe3779f02aed2d0add77118c615e1ec44db2fee366318cc3d1698821dff3</citedby><cites>FETCH-LOGICAL-c443t-9f905fe3779f02aed2d0add77118c615e1ec44db2fee366318cc3d1698821dff3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0304-3940(01)02399-0$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13414389$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11744223$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wirths, Oliver</creatorcontrib><creatorcontrib>Multhaup, Gerd</creatorcontrib><creatorcontrib>Czech, Christian</creatorcontrib><creatorcontrib>Blanchard, Véronique</creatorcontrib><creatorcontrib>Tremp, Günter</creatorcontrib><creatorcontrib>Pradier, Laurent</creatorcontrib><creatorcontrib>Beyreuther, Konrad</creatorcontrib><creatorcontrib>Bayer, Thomas A.</creatorcontrib><title>Reelin in plaques of β-amyloid precursor protein and presenilin-1 double-transgenic mice</title><title>Neuroscience letters</title><addtitle>Neurosci Lett</addtitle><description>There is circumstantial evidence that the reelin signaling pathway may contribute to neurodegeneration in the adult brain and could be linked to Alzheimer's disease (AD). In the present immunohistochemical report we studied the reelin expression profile in double-transgenic mice that express both human mutant β-amyloid precursor protein (APP) and human mutant presenilin-1. We were able to demonstrate that reelin immunostaining was found together with human APP in the neuritic component of many AD-typical plaques in both hippocampus and neocortex. This observation gives the first evidence for the association of reelin with amyloid deposits.</description><subject>Alzheimer Disease - genetics</subject><subject>Alzheimer Disease - metabolism</subject><subject>Alzheimer Disease - pathology</subject><subject>Alzheimer's disease</subject><subject>Amyloid beta-Protein Precursor - genetics</subject><subject>Amyloid beta-Protein Precursor - metabolism</subject><subject>Amyloid deposits</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell Adhesion Molecules, Neuronal - genetics</subject><subject>Cell Adhesion Molecules, Neuronal - metabolism</subject><subject>Cerebral Cortex - metabolism</subject><subject>Cerebral Cortex - pathology</subject><subject>Cerebral Cortex - physiopathology</subject><subject>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</subject><subject>Extracellular Matrix Proteins - genetics</subject><subject>Extracellular Matrix Proteins - metabolism</subject><subject>Female</subject><subject>Hippocampus - metabolism</subject><subject>Hippocampus - pathology</subject><subject>Hippocampus - physiopathology</subject><subject>Immunohistochemistry</subject><subject>Immunostaining</subject><subject>Interneurons - metabolism</subject><subject>Interneurons - pathology</subject><subject>Male</subject><subject>Medical sciences</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Mice, Transgenic</subject><subject>Nerve Tissue Proteins</subject><subject>Neuritic plaques</subject><subject>Neurology</subject><subject>Plaque, Amyloid - genetics</subject><subject>Plaque, Amyloid - metabolism</subject><subject>Plaque, Amyloid - pathology</subject><subject>Presenilin</subject><subject>Presenilin-1</subject><subject>Pyramidal Cells - metabolism</subject><subject>Pyramidal Cells - pathology</subject><subject>Serine Endopeptidases</subject><subject>Transgenic mice</subject><subject>β-Amyloid precursor protein</subject><issn>0304-3940</issn><issn>1872-7972</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMuKFTEQhoMozpnRR1B6o4yLaFWS7nRWgwzeYEDwsnAVcpKKRPpyTLqFeS0fxGcy54KzFAIJP1-lfj7GniC8RMDu1WeQoLg0Ci4BX4CQxnC4xzbYa8G10eI-2_xDzth5KT8AoMVWPWRniFopIeSGfftENKSpqWc3uJ8rlWaOzZ_f3I23w5xCs8vk11zmXF_zQpVz0yEtNKU6ybEJ87odiC_ZTeV7TX0zJk-P2IPohkKPT_cF-_r2zZfr9_zm47sP169vuFdKLtxEA20kqbWJIBwFEcCFoDVi7ztsCamCYSsikew6WVMvA3am7wWGGOUFe378t_bb91_smIqnYXATzWuxWsi2VdJUsD2CPs-lZIp2l9Po8q1FsHun9uDU7oVZQHtwaqHOPT0tWLcjhbupk8QKPDsBrng3xOrBp3LHSYVK9vsCV0eOqo5fibItPtHkKaQqebFhTv-p8he54ZRn</recordid><startdate>20011228</startdate><enddate>20011228</enddate><creator>Wirths, Oliver</creator><creator>Multhaup, Gerd</creator><creator>Czech, Christian</creator><creator>Blanchard, Véronique</creator><creator>Tremp, Günter</creator><creator>Pradier, Laurent</creator><creator>Beyreuther, Konrad</creator><creator>Bayer, Thomas A.</creator><general>Elsevier Ireland Ltd</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20011228</creationdate><title>Reelin in plaques of β-amyloid precursor protein and presenilin-1 double-transgenic mice</title><author>Wirths, Oliver ; Multhaup, Gerd ; Czech, Christian ; Blanchard, Véronique ; Tremp, Günter ; Pradier, Laurent ; Beyreuther, Konrad ; Bayer, Thomas A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-9f905fe3779f02aed2d0add77118c615e1ec44db2fee366318cc3d1698821dff3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Alzheimer Disease - genetics</topic><topic>Alzheimer Disease - metabolism</topic><topic>Alzheimer Disease - pathology</topic><topic>Alzheimer's disease</topic><topic>Amyloid beta-Protein Precursor - genetics</topic><topic>Amyloid beta-Protein Precursor - metabolism</topic><topic>Amyloid deposits</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cell Adhesion Molecules, Neuronal - genetics</topic><topic>Cell Adhesion Molecules, Neuronal - metabolism</topic><topic>Cerebral Cortex - metabolism</topic><topic>Cerebral Cortex - pathology</topic><topic>Cerebral Cortex - physiopathology</topic><topic>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</topic><topic>Extracellular Matrix Proteins - genetics</topic><topic>Extracellular Matrix Proteins - metabolism</topic><topic>Female</topic><topic>Hippocampus - metabolism</topic><topic>Hippocampus - pathology</topic><topic>Hippocampus - physiopathology</topic><topic>Immunohistochemistry</topic><topic>Immunostaining</topic><topic>Interneurons - metabolism</topic><topic>Interneurons - pathology</topic><topic>Male</topic><topic>Medical sciences</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Mice, Transgenic</topic><topic>Nerve Tissue Proteins</topic><topic>Neuritic plaques</topic><topic>Neurology</topic><topic>Plaque, Amyloid - genetics</topic><topic>Plaque, Amyloid - metabolism</topic><topic>Plaque, Amyloid - pathology</topic><topic>Presenilin</topic><topic>Presenilin-1</topic><topic>Pyramidal Cells - metabolism</topic><topic>Pyramidal Cells - pathology</topic><topic>Serine Endopeptidases</topic><topic>Transgenic mice</topic><topic>β-Amyloid precursor protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wirths, Oliver</creatorcontrib><creatorcontrib>Multhaup, Gerd</creatorcontrib><creatorcontrib>Czech, Christian</creatorcontrib><creatorcontrib>Blanchard, Véronique</creatorcontrib><creatorcontrib>Tremp, Günter</creatorcontrib><creatorcontrib>Pradier, Laurent</creatorcontrib><creatorcontrib>Beyreuther, Konrad</creatorcontrib><creatorcontrib>Bayer, Thomas A.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Neuroscience letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wirths, Oliver</au><au>Multhaup, Gerd</au><au>Czech, Christian</au><au>Blanchard, Véronique</au><au>Tremp, Günter</au><au>Pradier, Laurent</au><au>Beyreuther, Konrad</au><au>Bayer, Thomas A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reelin in plaques of β-amyloid precursor protein and presenilin-1 double-transgenic mice</atitle><jtitle>Neuroscience letters</jtitle><addtitle>Neurosci Lett</addtitle><date>2001-12-28</date><risdate>2001</risdate><volume>316</volume><issue>3</issue><spage>145</spage><epage>148</epage><pages>145-148</pages><issn>0304-3940</issn><eissn>1872-7972</eissn><coden>NELED5</coden><abstract>There is circumstantial evidence that the reelin signaling pathway may contribute to neurodegeneration in the adult brain and could be linked to Alzheimer's disease (AD). In the present immunohistochemical report we studied the reelin expression profile in double-transgenic mice that express both human mutant β-amyloid precursor protein (APP) and human mutant presenilin-1. We were able to demonstrate that reelin immunostaining was found together with human APP in the neuritic component of many AD-typical plaques in both hippocampus and neocortex. This observation gives the first evidence for the association of reelin with amyloid deposits.</abstract><cop>Shannon</cop><pub>Elsevier Ireland Ltd</pub><pmid>11744223</pmid><doi>10.1016/S0304-3940(01)02399-0</doi><tpages>4</tpages></addata></record> |
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| ispartof | Neuroscience letters, 2001-12, Vol.316 (3), p.145-148 |
| issn | 0304-3940 1872-7972 |
| language | eng |
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| subjects | Alzheimer Disease - genetics Alzheimer Disease - metabolism Alzheimer Disease - pathology Alzheimer's disease Amyloid beta-Protein Precursor - genetics Amyloid beta-Protein Precursor - metabolism Amyloid deposits Animals Biological and medical sciences Cell Adhesion Molecules, Neuronal - genetics Cell Adhesion Molecules, Neuronal - metabolism Cerebral Cortex - metabolism Cerebral Cortex - pathology Cerebral Cortex - physiopathology Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases Extracellular Matrix Proteins - genetics Extracellular Matrix Proteins - metabolism Female Hippocampus - metabolism Hippocampus - pathology Hippocampus - physiopathology Immunohistochemistry Immunostaining Interneurons - metabolism Interneurons - pathology Male Medical sciences Membrane Proteins - genetics Membrane Proteins - metabolism Mice Mice, Knockout Mice, Transgenic Nerve Tissue Proteins Neuritic plaques Neurology Plaque, Amyloid - genetics Plaque, Amyloid - metabolism Plaque, Amyloid - pathology Presenilin Presenilin-1 Pyramidal Cells - metabolism Pyramidal Cells - pathology Serine Endopeptidases Transgenic mice β-Amyloid precursor protein |
| title | Reelin in plaques of β-amyloid precursor protein and presenilin-1 double-transgenic mice |
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