Chronic nicotine treatment reduces β‐amyloidosis in the brain of a mouse model of Alzheimer's disease (APPsw)
Alzheimer's disease neuropathology is characterised by β‐amyloid plaques and neurofibrillary tangles. Inhibition of β‐amyloid accumulation may be essential for effective therapy in Alzheimer's disease. In this study we have treated transgenic mice carrying the Swedish mutation of human amy...
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| Veröffentlicht in: | Journal of neurochemistry 2002-05, Vol.81 (3), p.655-658 |
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| creator | Nordberg, Agneta Hellström‐Lindahl, Ewa Lee, Mandy Johnson, Mary Mousavi, Malahat Hall, Ros Perry, Elaine Bednar, Ivan Court, Jennifer |
| description | Alzheimer's disease neuropathology is characterised by β‐amyloid plaques and neurofibrillary tangles. Inhibition of β‐amyloid accumulation may be essential for effective therapy in Alzheimer's disease. In this study we have treated transgenic mice carrying the Swedish mutation of human amyloid precursor protein [Tg(Hu.APP695.K670N‐M671L)2576], which develop brain β‐amyloid deposits, with nicotine in drinking fluid (200 µg/mL) from 9–14.5 months of age (5.5 months). A significant reduction in amyloid β peptide 1–42 positive plaques by more than 80% (p |
| doi_str_mv | 10.1046/j.1471-4159.2002.00874.x |
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Inhibition of β‐amyloid accumulation may be essential for effective therapy in Alzheimer's disease. In this study we have treated transgenic mice carrying the Swedish mutation of human amyloid precursor protein [Tg(Hu.APP695.K670N‐M671L)2576], which develop brain β‐amyloid deposits, with nicotine in drinking fluid (200 µg/mL) from 9–14.5 months of age (5.5 months). A significant reduction in amyloid β peptide 1–42 positive plaques by more than 80% (p < 0.03) was observed in the brains of nicotine treated compared to sucrose treated transgenic mice. In addition, there was a selective reduction in extractable amyloid β peptides in nicotine treated mice; cortical insoluble 1–40 and 1–42 peptide levels were lower by 48 and 60%, respectively (p < 0.005), whilst there was no significant change in soluble 1–40 or 1–42 levels. The expression of glial fibrillary acidic protein was not affected by nicotine treatment. These results indicate that nicotine may effectively reduce amyloid β peptide aggregation in brain and that nicotinic drug treatment may be a novel protective therapy in Alzheimer's disease.</description><identifier>ISSN: 0022-3042</identifier><identifier>EISSN: 1471-4159</identifier><identifier>DOI: 10.1046/j.1471-4159.2002.00874.x</identifier><identifier>PMID: 12065674</identifier><identifier>CODEN: JONRA9</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>Administration, Oral ; Alzheimer Disease - drug therapy ; Alzheimer Disease - metabolism ; Alzheimer Disease - pathology ; Alzheimer's disease ; Amyloid beta-Peptides - analysis ; Amyloid beta-Peptides - biosynthesis ; amyloid β peptide ; Animals ; APPsw transgenic mice ; Astrocytes - metabolism ; Astrocytes - pathology ; Biological and medical sciences ; Brain Chemistry ; Cell Count ; Cerebral Cortex - drug effects ; Cerebral Cortex - metabolism ; Cerebral Cortex - pathology ; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases ; Disease Models, Animal ; Disease Progression ; Drug Administration Schedule ; Female ; Glial Fibrillary Acidic Protein - biosynthesis ; Hippocampus - chemistry ; Humans ; Immunohistochemistry ; Male ; Medical sciences ; Mice ; Mice, Transgenic ; Neurology ; nicotine ; Nicotine - administration & dosage ; nicotinic receptors ; Olfactory Pathways - chemistry ; Peptide Fragments - analysis ; Peptide Fragments - biosynthesis ; Plaque, Amyloid - drug effects ; Plaque, Amyloid - metabolism ; Plaque, Amyloid - pathology ; Sex Factors ; Treatment Outcome</subject><ispartof>Journal of neurochemistry, 2002-05, Vol.81 (3), p.655-658</ispartof><rights>2002 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4644-ec7bfdc25f1c7f87475f9827026fc9571115b23a5a094707c5bbca65e38b8843</citedby><cites>FETCH-LOGICAL-c4644-ec7bfdc25f1c7f87475f9827026fc9571115b23a5a094707c5bbca65e38b8843</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1046%2Fj.1471-4159.2002.00874.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1046%2Fj.1471-4159.2002.00874.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,314,777,781,882,1412,1428,27905,27906,45555,45556,46390,46814</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13657865$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12065674$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttp://kipublications.ki.se/Default.aspx?queryparsed=id:1960843$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Nordberg, Agneta</creatorcontrib><creatorcontrib>Hellström‐Lindahl, Ewa</creatorcontrib><creatorcontrib>Lee, Mandy</creatorcontrib><creatorcontrib>Johnson, Mary</creatorcontrib><creatorcontrib>Mousavi, Malahat</creatorcontrib><creatorcontrib>Hall, Ros</creatorcontrib><creatorcontrib>Perry, Elaine</creatorcontrib><creatorcontrib>Bednar, Ivan</creatorcontrib><creatorcontrib>Court, Jennifer</creatorcontrib><title>Chronic nicotine treatment reduces β‐amyloidosis in the brain of a mouse model of Alzheimer's disease (APPsw)</title><title>Journal of neurochemistry</title><addtitle>J Neurochem</addtitle><description>Alzheimer's disease neuropathology is characterised by β‐amyloid plaques and neurofibrillary tangles. Inhibition of β‐amyloid accumulation may be essential for effective therapy in Alzheimer's disease. In this study we have treated transgenic mice carrying the Swedish mutation of human amyloid precursor protein [Tg(Hu.APP695.K670N‐M671L)2576], which develop brain β‐amyloid deposits, with nicotine in drinking fluid (200 µg/mL) from 9–14.5 months of age (5.5 months). A significant reduction in amyloid β peptide 1–42 positive plaques by more than 80% (p < 0.03) was observed in the brains of nicotine treated compared to sucrose treated transgenic mice. In addition, there was a selective reduction in extractable amyloid β peptides in nicotine treated mice; cortical insoluble 1–40 and 1–42 peptide levels were lower by 48 and 60%, respectively (p < 0.005), whilst there was no significant change in soluble 1–40 or 1–42 levels. The expression of glial fibrillary acidic protein was not affected by nicotine treatment. These results indicate that nicotine may effectively reduce amyloid β peptide aggregation in brain and that nicotinic drug treatment may be a novel protective therapy in Alzheimer's disease.</description><subject>Administration, Oral</subject><subject>Alzheimer Disease - drug therapy</subject><subject>Alzheimer Disease - metabolism</subject><subject>Alzheimer Disease - pathology</subject><subject>Alzheimer's disease</subject><subject>Amyloid beta-Peptides - analysis</subject><subject>Amyloid beta-Peptides - biosynthesis</subject><subject>amyloid β peptide</subject><subject>Animals</subject><subject>APPsw transgenic mice</subject><subject>Astrocytes - metabolism</subject><subject>Astrocytes - pathology</subject><subject>Biological and medical sciences</subject><subject>Brain Chemistry</subject><subject>Cell Count</subject><subject>Cerebral Cortex - drug effects</subject><subject>Cerebral Cortex - metabolism</subject><subject>Cerebral Cortex - pathology</subject><subject>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</subject><subject>Disease Models, Animal</subject><subject>Disease Progression</subject><subject>Drug Administration Schedule</subject><subject>Female</subject><subject>Glial Fibrillary Acidic Protein - biosynthesis</subject><subject>Hippocampus - chemistry</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>Male</subject><subject>Medical sciences</subject><subject>Mice</subject><subject>Mice, Transgenic</subject><subject>Neurology</subject><subject>nicotine</subject><subject>Nicotine - administration & dosage</subject><subject>nicotinic receptors</subject><subject>Olfactory Pathways - chemistry</subject><subject>Peptide Fragments - analysis</subject><subject>Peptide Fragments - biosynthesis</subject><subject>Plaque, Amyloid - drug effects</subject><subject>Plaque, Amyloid - metabolism</subject><subject>Plaque, Amyloid - pathology</subject><subject>Sex Factors</subject><subject>Treatment Outcome</subject><issn>0022-3042</issn><issn>1471-4159</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUuO1DAQhi0EYpqBKyBveC0S7MSvLGbRavHUCGYxe8txymo3eTR2op5mxRE4CwfhEJwEh45mlrCw_avqq3KVfoQwJTklTLze5ZRJmjHKq7wgpMgJUZLlN_fQ6jZxH61SpshKwooz9CjGHSFUMEEfojNaEMGFZCu032zD0HuL0xlG3wMeA5ixg37EAZrJQsS_fv7-_sN0x3bwzRB9xL7H4xZwHUxSg8MGd8MUId0NtHNg3X7bgu8gvIi48RFMSr5cX13Fw6vH6IEzbYQny3uOrt--ud68zy4_v_uwWV9mlgnGMrCydo0tuKNWurSc5K5ShSSFcLbiklLK66I03JCKSSItr2trBIdS1Uqx8hxlp7bxAPup1vvgOxOOejBeL6EvSYHmVSmpSPzzE78Pw9cJ4qg7Hy20rekh7aYlVVQIKv8JUsWIZHwG1Qm0YYgxgLudgRI9u6h3ejZLz2bp2UX910V9k0qfLn9MdQfNXeFiWwKeLYCJ1rQumN76eMeVgksleOIuTtzBt3D87wH0x0-bWZV_AKtIufI</recordid><startdate>200205</startdate><enddate>200205</enddate><creator>Nordberg, Agneta</creator><creator>Hellström‐Lindahl, Ewa</creator><creator>Lee, Mandy</creator><creator>Johnson, Mary</creator><creator>Mousavi, Malahat</creator><creator>Hall, Ros</creator><creator>Perry, Elaine</creator><creator>Bednar, Ivan</creator><creator>Court, Jennifer</creator><general>Blackwell Science Ltd</general><general>Blackwell</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>7TK</scope><scope>7X8</scope><scope>ADTPV</scope><scope>AOWAS</scope></search><sort><creationdate>200205</creationdate><title>Chronic nicotine treatment reduces β‐amyloidosis in the brain of a mouse model of Alzheimer's disease (APPsw)</title><author>Nordberg, Agneta ; Hellström‐Lindahl, Ewa ; Lee, Mandy ; Johnson, Mary ; Mousavi, Malahat ; Hall, Ros ; Perry, Elaine ; Bednar, Ivan ; Court, Jennifer</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4644-ec7bfdc25f1c7f87475f9827026fc9571115b23a5a094707c5bbca65e38b8843</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Administration, Oral</topic><topic>Alzheimer Disease - drug therapy</topic><topic>Alzheimer Disease - metabolism</topic><topic>Alzheimer Disease - pathology</topic><topic>Alzheimer's disease</topic><topic>Amyloid beta-Peptides - analysis</topic><topic>Amyloid beta-Peptides - biosynthesis</topic><topic>amyloid β peptide</topic><topic>Animals</topic><topic>APPsw transgenic mice</topic><topic>Astrocytes - metabolism</topic><topic>Astrocytes - pathology</topic><topic>Biological and medical sciences</topic><topic>Brain Chemistry</topic><topic>Cell Count</topic><topic>Cerebral Cortex - drug effects</topic><topic>Cerebral Cortex - metabolism</topic><topic>Cerebral Cortex - pathology</topic><topic>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</topic><topic>Disease Models, Animal</topic><topic>Disease Progression</topic><topic>Drug Administration Schedule</topic><topic>Female</topic><topic>Glial Fibrillary Acidic Protein - biosynthesis</topic><topic>Hippocampus - chemistry</topic><topic>Humans</topic><topic>Immunohistochemistry</topic><topic>Male</topic><topic>Medical sciences</topic><topic>Mice</topic><topic>Mice, Transgenic</topic><topic>Neurology</topic><topic>nicotine</topic><topic>Nicotine - administration & dosage</topic><topic>nicotinic receptors</topic><topic>Olfactory Pathways - chemistry</topic><topic>Peptide Fragments - analysis</topic><topic>Peptide Fragments - biosynthesis</topic><topic>Plaque, Amyloid - drug effects</topic><topic>Plaque, Amyloid - metabolism</topic><topic>Plaque, Amyloid - pathology</topic><topic>Sex Factors</topic><topic>Treatment Outcome</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nordberg, Agneta</creatorcontrib><creatorcontrib>Hellström‐Lindahl, Ewa</creatorcontrib><creatorcontrib>Lee, Mandy</creatorcontrib><creatorcontrib>Johnson, Mary</creatorcontrib><creatorcontrib>Mousavi, Malahat</creatorcontrib><creatorcontrib>Hall, Ros</creatorcontrib><creatorcontrib>Perry, Elaine</creatorcontrib><creatorcontrib>Bednar, Ivan</creatorcontrib><creatorcontrib>Court, Jennifer</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>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><collection>SwePub</collection><collection>SwePub Articles</collection><jtitle>Journal of neurochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nordberg, Agneta</au><au>Hellström‐Lindahl, Ewa</au><au>Lee, Mandy</au><au>Johnson, Mary</au><au>Mousavi, Malahat</au><au>Hall, Ros</au><au>Perry, Elaine</au><au>Bednar, Ivan</au><au>Court, Jennifer</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chronic nicotine treatment reduces β‐amyloidosis in the brain of a mouse model of Alzheimer's disease (APPsw)</atitle><jtitle>Journal of neurochemistry</jtitle><addtitle>J Neurochem</addtitle><date>2002-05</date><risdate>2002</risdate><volume>81</volume><issue>3</issue><spage>655</spage><epage>658</epage><pages>655-658</pages><issn>0022-3042</issn><eissn>1471-4159</eissn><coden>JONRA9</coden><abstract>Alzheimer's disease neuropathology is characterised by β‐amyloid plaques and neurofibrillary tangles. Inhibition of β‐amyloid accumulation may be essential for effective therapy in Alzheimer's disease. In this study we have treated transgenic mice carrying the Swedish mutation of human amyloid precursor protein [Tg(Hu.APP695.K670N‐M671L)2576], which develop brain β‐amyloid deposits, with nicotine in drinking fluid (200 µg/mL) from 9–14.5 months of age (5.5 months). A significant reduction in amyloid β peptide 1–42 positive plaques by more than 80% (p < 0.03) was observed in the brains of nicotine treated compared to sucrose treated transgenic mice. In addition, there was a selective reduction in extractable amyloid β peptides in nicotine treated mice; cortical insoluble 1–40 and 1–42 peptide levels were lower by 48 and 60%, respectively (p < 0.005), whilst there was no significant change in soluble 1–40 or 1–42 levels. The expression of glial fibrillary acidic protein was not affected by nicotine treatment. These results indicate that nicotine may effectively reduce amyloid β peptide aggregation in brain and that nicotinic drug treatment may be a novel protective therapy in Alzheimer's disease.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>12065674</pmid><doi>10.1046/j.1471-4159.2002.00874.x</doi><tpages>4</tpages></addata></record> |
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| subjects | Administration, Oral Alzheimer Disease - drug therapy Alzheimer Disease - metabolism Alzheimer Disease - pathology Alzheimer's disease Amyloid beta-Peptides - analysis Amyloid beta-Peptides - biosynthesis amyloid β peptide Animals APPsw transgenic mice Astrocytes - metabolism Astrocytes - pathology Biological and medical sciences Brain Chemistry Cell Count Cerebral Cortex - drug effects Cerebral Cortex - metabolism Cerebral Cortex - pathology Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases Disease Models, Animal Disease Progression Drug Administration Schedule Female Glial Fibrillary Acidic Protein - biosynthesis Hippocampus - chemistry Humans Immunohistochemistry Male Medical sciences Mice Mice, Transgenic Neurology nicotine Nicotine - administration & dosage nicotinic receptors Olfactory Pathways - chemistry Peptide Fragments - analysis Peptide Fragments - biosynthesis Plaque, Amyloid - drug effects Plaque, Amyloid - metabolism Plaque, Amyloid - pathology Sex Factors Treatment Outcome |
| title | Chronic nicotine treatment reduces β‐amyloidosis in the brain of a mouse model of Alzheimer's disease (APPsw) |
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