Susceptibility of Amyloid β Peptide Degrading Enzymes to Oxidative Damage: A Potential Alzheimer's Disease Spiral
Insulysin (IDE) and neprilysin (NEP) were found to be inactivated by oxidation with hydrogen peroxide, an iron−ascorbate oxidation system, and by treatment with 2,2‘-azobis(2-amidinopropane) dihydrochloride (AAPH). In each case reaction led to the introduction of protein carbonyl groups as judged by...
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| Veröffentlicht in: | Biochemistry (Easton) 2005-11, Vol.44 (46), p.15345-15350 |
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| creator | Shinall, Heather Song, Eun Suk Hersh, Louis B |
| description | Insulysin (IDE) and neprilysin (NEP) were found to be inactivated by oxidation with hydrogen peroxide, an iron−ascorbate oxidation system, and by treatment with 2,2‘-azobis(2-amidinopropane) dihydrochloride (AAPH). In each case reaction led to the introduction of protein carbonyl groups as judged by reaction with 2,4-dintrophenylhydrazine. IDE was inactivated by reaction with 4-hydroxy-2-nonenal (HNE) with the concomitant formation of protein adducts. NEP was not inactivated to a significant extent by HNE, but some HNE-adduct formation did occur. Prior reaction with hydrogen peroxide or AAPH led to enhanced formation of HNE adducts. Treatment of IDE with AAHP or hydrogen peroxide increased its susceptibility to proteolysis, while treatment of NEP with iron/ascorbate or hydrogen peroxide increased its susceptibility to proteolysis. Since IDE and NEP play a prominent role in the clearance of amyloid β peptides, their oxidative inactivation and enhanced proteolysis can contribute to the onset and/or progression of Alzheimer's disease. |
| doi_str_mv | 10.1021/bi050650l |
| format | Article |
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In each case reaction led to the introduction of protein carbonyl groups as judged by reaction with 2,4-dintrophenylhydrazine. IDE was inactivated by reaction with 4-hydroxy-2-nonenal (HNE) with the concomitant formation of protein adducts. NEP was not inactivated to a significant extent by HNE, but some HNE-adduct formation did occur. Prior reaction with hydrogen peroxide or AAPH led to enhanced formation of HNE adducts. Treatment of IDE with AAHP or hydrogen peroxide increased its susceptibility to proteolysis, while treatment of NEP with iron/ascorbate or hydrogen peroxide increased its susceptibility to proteolysis. Since IDE and NEP play a prominent role in the clearance of amyloid β peptides, their oxidative inactivation and enhanced proteolysis can contribute to the onset and/or progression of Alzheimer's disease.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi050650l</identifier><identifier>PMID: 16285738</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Aldehydes - chemistry ; Alzheimer Disease - etiology ; Alzheimer Disease - physiopathology ; Amidines - chemistry ; Amyloid beta-Peptides - metabolism ; Ascorbic Acid - chemistry ; Chlorides ; Chymotrypsin - metabolism ; Ferric Compounds - chemistry ; Hydrogen Peroxide - chemistry ; Insulysin - antagonists & inhibitors ; Neprilysin - antagonists & inhibitors ; Oxidation-Reduction ; Trypsin - metabolism</subject><ispartof>Biochemistry (Easton), 2005-11, Vol.44 (46), p.15345-15350</ispartof><rights>Copyright © 2005 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a351t-9b062d68f660e14d7b1bd2273984385c9d2fe0256f29c5888b27fa73c43195133</citedby><cites>FETCH-LOGICAL-a351t-9b062d68f660e14d7b1bd2273984385c9d2fe0256f29c5888b27fa73c43195133</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi050650l$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi050650l$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16285738$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shinall, Heather</creatorcontrib><creatorcontrib>Song, Eun Suk</creatorcontrib><creatorcontrib>Hersh, Louis B</creatorcontrib><title>Susceptibility of Amyloid β Peptide Degrading Enzymes to Oxidative Damage: A Potential Alzheimer's Disease Spiral</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Insulysin (IDE) and neprilysin (NEP) were found to be inactivated by oxidation with hydrogen peroxide, an iron−ascorbate oxidation system, and by treatment with 2,2‘-azobis(2-amidinopropane) dihydrochloride (AAPH). In each case reaction led to the introduction of protein carbonyl groups as judged by reaction with 2,4-dintrophenylhydrazine. IDE was inactivated by reaction with 4-hydroxy-2-nonenal (HNE) with the concomitant formation of protein adducts. NEP was not inactivated to a significant extent by HNE, but some HNE-adduct formation did occur. Prior reaction with hydrogen peroxide or AAPH led to enhanced formation of HNE adducts. Treatment of IDE with AAHP or hydrogen peroxide increased its susceptibility to proteolysis, while treatment of NEP with iron/ascorbate or hydrogen peroxide increased its susceptibility to proteolysis. Since IDE and NEP play a prominent role in the clearance of amyloid β peptides, their oxidative inactivation and enhanced proteolysis can contribute to the onset and/or progression of Alzheimer's disease.</description><subject>Aldehydes - chemistry</subject><subject>Alzheimer Disease - etiology</subject><subject>Alzheimer Disease - physiopathology</subject><subject>Amidines - chemistry</subject><subject>Amyloid beta-Peptides - metabolism</subject><subject>Ascorbic Acid - chemistry</subject><subject>Chlorides</subject><subject>Chymotrypsin - metabolism</subject><subject>Ferric Compounds - chemistry</subject><subject>Hydrogen Peroxide - chemistry</subject><subject>Insulysin - antagonists & inhibitors</subject><subject>Neprilysin - antagonists & inhibitors</subject><subject>Oxidation-Reduction</subject><subject>Trypsin - metabolism</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkMtKw0AUhgdRbK0ufAGZjYiL6Fwyk8Rd6cUKhQZa18MkM6lTk6bMpNJ25dbX8UF8CJ_ElEjduDoc_o_zcz4ALjG6w4jg-8QghjhD-RFoY0aQ50cROwZthBD3SMRRC5w5t6hXHwX-KWhhTkIW0LAN1tO1S_WqMonJTbWFZQa7xTYvjYJfnzDeJ0rDvp5bqcxyDgfL3bbQDlYlnGyMkpV5q2NZyLl--H7_gF0Yl5VeVkbmsJvvXrQptL1xsG-clk7D6cpYmZ-Dk0zmTl_8zg54Hg5mvZE3njw-9bpjT1KGKy9KECeKhxnnSGNfBQlOFCEBjUKfhiyNFMk0IoxnJEpZGIYJCTIZ0NSnOGKY0g64be6mtnTO6kysrCmk3QqMxF6dOKir2auGXa2TQqs_8tdVDXgNYFylN4dc2lfBAxowMYunwh_HnAxHM7Evv254mTqxKNd2Wb_6T_EPj6qFcQ</recordid><startdate>20051122</startdate><enddate>20051122</enddate><creator>Shinall, Heather</creator><creator>Song, Eun Suk</creator><creator>Hersh, Louis B</creator><general>American Chemical Society</general><scope>BSCLL</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></search><sort><creationdate>20051122</creationdate><title>Susceptibility of Amyloid β Peptide Degrading Enzymes to Oxidative Damage: A Potential Alzheimer's Disease Spiral</title><author>Shinall, Heather ; Song, Eun Suk ; Hersh, Louis B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a351t-9b062d68f660e14d7b1bd2273984385c9d2fe0256f29c5888b27fa73c43195133</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Aldehydes - chemistry</topic><topic>Alzheimer Disease - etiology</topic><topic>Alzheimer Disease - physiopathology</topic><topic>Amidines - chemistry</topic><topic>Amyloid beta-Peptides - metabolism</topic><topic>Ascorbic Acid - chemistry</topic><topic>Chlorides</topic><topic>Chymotrypsin - metabolism</topic><topic>Ferric Compounds - chemistry</topic><topic>Hydrogen Peroxide - chemistry</topic><topic>Insulysin - antagonists & inhibitors</topic><topic>Neprilysin - antagonists & inhibitors</topic><topic>Oxidation-Reduction</topic><topic>Trypsin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shinall, Heather</creatorcontrib><creatorcontrib>Song, Eun Suk</creatorcontrib><creatorcontrib>Hersh, Louis B</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shinall, Heather</au><au>Song, Eun Suk</au><au>Hersh, Louis B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Susceptibility of Amyloid β Peptide Degrading Enzymes to Oxidative Damage: A Potential Alzheimer's Disease Spiral</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>2005-11-22</date><risdate>2005</risdate><volume>44</volume><issue>46</issue><spage>15345</spage><epage>15350</epage><pages>15345-15350</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Insulysin (IDE) and neprilysin (NEP) were found to be inactivated by oxidation with hydrogen peroxide, an iron−ascorbate oxidation system, and by treatment with 2,2‘-azobis(2-amidinopropane) dihydrochloride (AAPH). In each case reaction led to the introduction of protein carbonyl groups as judged by reaction with 2,4-dintrophenylhydrazine. IDE was inactivated by reaction with 4-hydroxy-2-nonenal (HNE) with the concomitant formation of protein adducts. NEP was not inactivated to a significant extent by HNE, but some HNE-adduct formation did occur. Prior reaction with hydrogen peroxide or AAPH led to enhanced formation of HNE adducts. Treatment of IDE with AAHP or hydrogen peroxide increased its susceptibility to proteolysis, while treatment of NEP with iron/ascorbate or hydrogen peroxide increased its susceptibility to proteolysis. Since IDE and NEP play a prominent role in the clearance of amyloid β peptides, their oxidative inactivation and enhanced proteolysis can contribute to the onset and/or progression of Alzheimer's disease.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>16285738</pmid><doi>10.1021/bi050650l</doi><tpages>6</tpages></addata></record> |
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| ispartof | Biochemistry (Easton), 2005-11, Vol.44 (46), p.15345-15350 |
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| source | MEDLINE; American Chemical Society Web Editions |
| subjects | Aldehydes - chemistry Alzheimer Disease - etiology Alzheimer Disease - physiopathology Amidines - chemistry Amyloid beta-Peptides - metabolism Ascorbic Acid - chemistry Chlorides Chymotrypsin - metabolism Ferric Compounds - chemistry Hydrogen Peroxide - chemistry Insulysin - antagonists & inhibitors Neprilysin - antagonists & inhibitors Oxidation-Reduction Trypsin - metabolism |
| title | Susceptibility of Amyloid β Peptide Degrading Enzymes to Oxidative Damage: A Potential Alzheimer's Disease Spiral |
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