Amyloid-β-protein (Aβ) (25–35)-associated free radical generation is strongly influenced by the aggregational state of the peptides
We investigated whether or not the Amyloid-β-protein (Aβ) itself spontaneously generates free radicals using electron spin resonance (ESR) spectroscopy while also monitoring the aggregational state of Aβ and Aβ-induced cytotoxicity. The present results demonstrated a four-line spectrum in the presen...
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| Veröffentlicht in: | Life sciences (1973) 2002-01, Vol.70 (7), p.833-841 |
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| container_title | Life sciences (1973) |
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| creator | Monji, Akira Utsumi, Hideo Ueda, Tadashi Imoto, Taiji Yoshida, Ichiro Hashioka, Sadayuki Tashiro, Ken-ichiro Tashiro, Nobutada |
| description | We investigated whether or not the Amyloid-β-protein (Aβ) itself spontaneously generates free radicals using electron spin resonance (ESR) spectroscopy while also monitoring the aggregational state of Aβ and Aβ-induced cytotoxicity. The present results demonstrated a four-line spectrum in the presence of Aβ25–35 with
N-tert-butyl-α-phenylnitrone (PBN) but not in the presence of PBN alone in phosphate-buffered saline (PBS). The fact that the four-line spectrum obtained for the Aβ25–35/PBN in PBS was completely abolished in the presence of the iron-chelating agent Desferal demonstrated the observed four-line spectrum to be iron-dependent. On the other hand, Aβ25–35 with PBN in phosphate buffer (PB) did not produce any definite four-line spectrum. the present results showed the amyloid fibril formation of Aβ25–35 in PBS to be much higher than that of Aβ25–35 in PB. Moreover, Aβ-induced cytotoxicity assays showed Aβ incubated in PBS to be more cytotoxic than that incubated in PB. These results thus demonstrate that Aβ(25–35) - associated free radical generation is strongly influenced by the aggregational state of the peptides. |
| doi_str_mv | 10.1016/S0024-3205(01)01451-5 |
| format | Article |
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N-tert-butyl-α-phenylnitrone (PBN) but not in the presence of PBN alone in phosphate-buffered saline (PBS). The fact that the four-line spectrum obtained for the Aβ25–35/PBN in PBS was completely abolished in the presence of the iron-chelating agent Desferal demonstrated the observed four-line spectrum to be iron-dependent. On the other hand, Aβ25–35 with PBN in phosphate buffer (PB) did not produce any definite four-line spectrum. the present results showed the amyloid fibril formation of Aβ25–35 in PBS to be much higher than that of Aβ25–35 in PB. Moreover, Aβ-induced cytotoxicity assays showed Aβ incubated in PBS to be more cytotoxic than that incubated in PB. These results thus demonstrate that Aβ(25–35) - associated free radical generation is strongly influenced by the aggregational state of the peptides.</description><identifier>ISSN: 0024-3205</identifier><identifier>EISSN: 1879-0631</identifier><identifier>DOI: 10.1016/S0024-3205(01)01451-5</identifier><identifier>PMID: 11833745</identifier><language>eng</language><publisher>Netherlands: Elsevier Inc</publisher><subject>Aggregation ; Alzheimer Disease - metabolism ; Alzheimer's disease ; Amyloid beta-Peptides - metabolism ; Amyloid beta-Peptides - toxicity ; Animals ; Beta amyloid ; Cyclic N-Oxides ; Cytotoxicity ; Deferoxamine - pharmacology ; Drug Antagonism ; Electron spin resonance ; Electron Spin Resonance Spectroscopy ; Formazans - metabolism ; Free radical ; Free Radicals - analysis ; Free Radicals - metabolism ; Iron ; Nitrogen Oxides - metabolism ; PC12 Cells - drug effects ; PC12 Cells - metabolism ; Peptide Fragments - metabolism ; Peptide Fragments - toxicity ; Protein Structure, Quaternary ; Rats ; Tetrazolium Salts - metabolism</subject><ispartof>Life sciences (1973), 2002-01, Vol.70 (7), p.833-841</ispartof><rights>2002 Elsevier Science Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-5ed88693dc50ee965657307cf2c4f8025898f705a3496fe1ca2c8049cb7981773</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0024320501014515$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11833745$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Monji, Akira</creatorcontrib><creatorcontrib>Utsumi, Hideo</creatorcontrib><creatorcontrib>Ueda, Tadashi</creatorcontrib><creatorcontrib>Imoto, Taiji</creatorcontrib><creatorcontrib>Yoshida, Ichiro</creatorcontrib><creatorcontrib>Hashioka, Sadayuki</creatorcontrib><creatorcontrib>Tashiro, Ken-ichiro</creatorcontrib><creatorcontrib>Tashiro, Nobutada</creatorcontrib><title>Amyloid-β-protein (Aβ) (25–35)-associated free radical generation is strongly influenced by the aggregational state of the peptides</title><title>Life sciences (1973)</title><addtitle>Life Sci</addtitle><description>We investigated whether or not the Amyloid-β-protein (Aβ) itself spontaneously generates free radicals using electron spin resonance (ESR) spectroscopy while also monitoring the aggregational state of Aβ and Aβ-induced cytotoxicity. The present results demonstrated a four-line spectrum in the presence of Aβ25–35 with
N-tert-butyl-α-phenylnitrone (PBN) but not in the presence of PBN alone in phosphate-buffered saline (PBS). The fact that the four-line spectrum obtained for the Aβ25–35/PBN in PBS was completely abolished in the presence of the iron-chelating agent Desferal demonstrated the observed four-line spectrum to be iron-dependent. On the other hand, Aβ25–35 with PBN in phosphate buffer (PB) did not produce any definite four-line spectrum. the present results showed the amyloid fibril formation of Aβ25–35 in PBS to be much higher than that of Aβ25–35 in PB. Moreover, Aβ-induced cytotoxicity assays showed Aβ incubated in PBS to be more cytotoxic than that incubated in PB. These results thus demonstrate that Aβ(25–35) - associated free radical generation is strongly influenced by the aggregational state of the peptides.</description><subject>Aggregation</subject><subject>Alzheimer Disease - metabolism</subject><subject>Alzheimer's disease</subject><subject>Amyloid beta-Peptides - metabolism</subject><subject>Amyloid beta-Peptides - toxicity</subject><subject>Animals</subject><subject>Beta amyloid</subject><subject>Cyclic N-Oxides</subject><subject>Cytotoxicity</subject><subject>Deferoxamine - pharmacology</subject><subject>Drug Antagonism</subject><subject>Electron spin resonance</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Formazans - metabolism</subject><subject>Free radical</subject><subject>Free Radicals - analysis</subject><subject>Free Radicals - metabolism</subject><subject>Iron</subject><subject>Nitrogen Oxides - metabolism</subject><subject>PC12 Cells - drug effects</subject><subject>PC12 Cells - metabolism</subject><subject>Peptide Fragments - metabolism</subject><subject>Peptide Fragments - toxicity</subject><subject>Protein Structure, Quaternary</subject><subject>Rats</subject><subject>Tetrazolium Salts - metabolism</subject><issn>0024-3205</issn><issn>1879-0631</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1uFDEQhS0EIkPgCCCv0MzCUG63u90rNIrCjxSJRWBtedzlxqinPdgepNmxywG4SQ6SQ-QkOD0jWLKqRX2vSu89Ql5yeMOBN2-vAaqaiQrkEvgKeC05k4_Igqu2Y9AI_pgs_iJn5FlK3wFAylY8JWecKyHaWi7IzXp7GIPv2d0t28WQ0U90ub67XdFlJe9__RZyxUxKwXqTsacuItJoem_NSAecMJrsw0R9oinHMA3jgfrJjXucbME3B5q_ITXDEHGYySJLuZyiwc2rHe6y7zE9J0-cGRO-OM1z8vX95ZeLj-zq84dPF-srZkVXZSaxV6rpRG8lIHaNbIohaK2rbO0UVFJ1yrUgjai7xiG3prIK6s5u2k7xthXn5PXxbjH7Y48p661PFsfRTBj2SXMllYIGCiiPoI0hpYhO76LfmnjQHPRDA3puQD_Eq4HruQEti-7V6cF-s8X-n-oUeQHeHQEsNn96jDpZP8flI9qs--D_8-IPv6iXpA</recordid><startdate>20020104</startdate><enddate>20020104</enddate><creator>Monji, Akira</creator><creator>Utsumi, Hideo</creator><creator>Ueda, Tadashi</creator><creator>Imoto, Taiji</creator><creator>Yoshida, Ichiro</creator><creator>Hashioka, Sadayuki</creator><creator>Tashiro, Ken-ichiro</creator><creator>Tashiro, Nobutada</creator><general>Elsevier Inc</general><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></search><sort><creationdate>20020104</creationdate><title>Amyloid-β-protein (Aβ) (25–35)-associated free radical generation is strongly influenced by the aggregational state of the peptides</title><author>Monji, Akira ; Utsumi, Hideo ; Ueda, Tadashi ; Imoto, Taiji ; Yoshida, Ichiro ; Hashioka, Sadayuki ; Tashiro, Ken-ichiro ; Tashiro, Nobutada</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-5ed88693dc50ee965657307cf2c4f8025898f705a3496fe1ca2c8049cb7981773</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Aggregation</topic><topic>Alzheimer Disease - metabolism</topic><topic>Alzheimer's disease</topic><topic>Amyloid beta-Peptides - metabolism</topic><topic>Amyloid beta-Peptides - toxicity</topic><topic>Animals</topic><topic>Beta amyloid</topic><topic>Cyclic N-Oxides</topic><topic>Cytotoxicity</topic><topic>Deferoxamine - pharmacology</topic><topic>Drug Antagonism</topic><topic>Electron spin resonance</topic><topic>Electron Spin Resonance Spectroscopy</topic><topic>Formazans - metabolism</topic><topic>Free radical</topic><topic>Free Radicals - analysis</topic><topic>Free Radicals - metabolism</topic><topic>Iron</topic><topic>Nitrogen Oxides - metabolism</topic><topic>PC12 Cells - drug effects</topic><topic>PC12 Cells - metabolism</topic><topic>Peptide Fragments - metabolism</topic><topic>Peptide Fragments - toxicity</topic><topic>Protein Structure, Quaternary</topic><topic>Rats</topic><topic>Tetrazolium Salts - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Monji, Akira</creatorcontrib><creatorcontrib>Utsumi, Hideo</creatorcontrib><creatorcontrib>Ueda, Tadashi</creatorcontrib><creatorcontrib>Imoto, Taiji</creatorcontrib><creatorcontrib>Yoshida, Ichiro</creatorcontrib><creatorcontrib>Hashioka, Sadayuki</creatorcontrib><creatorcontrib>Tashiro, Ken-ichiro</creatorcontrib><creatorcontrib>Tashiro, Nobutada</creatorcontrib><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><jtitle>Life sciences (1973)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Monji, Akira</au><au>Utsumi, Hideo</au><au>Ueda, Tadashi</au><au>Imoto, Taiji</au><au>Yoshida, Ichiro</au><au>Hashioka, Sadayuki</au><au>Tashiro, Ken-ichiro</au><au>Tashiro, Nobutada</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Amyloid-β-protein (Aβ) (25–35)-associated free radical generation is strongly influenced by the aggregational state of the peptides</atitle><jtitle>Life sciences (1973)</jtitle><addtitle>Life Sci</addtitle><date>2002-01-04</date><risdate>2002</risdate><volume>70</volume><issue>7</issue><spage>833</spage><epage>841</epage><pages>833-841</pages><issn>0024-3205</issn><eissn>1879-0631</eissn><abstract>We investigated whether or not the Amyloid-β-protein (Aβ) itself spontaneously generates free radicals using electron spin resonance (ESR) spectroscopy while also monitoring the aggregational state of Aβ and Aβ-induced cytotoxicity. The present results demonstrated a four-line spectrum in the presence of Aβ25–35 with
N-tert-butyl-α-phenylnitrone (PBN) but not in the presence of PBN alone in phosphate-buffered saline (PBS). The fact that the four-line spectrum obtained for the Aβ25–35/PBN in PBS was completely abolished in the presence of the iron-chelating agent Desferal demonstrated the observed four-line spectrum to be iron-dependent. On the other hand, Aβ25–35 with PBN in phosphate buffer (PB) did not produce any definite four-line spectrum. the present results showed the amyloid fibril formation of Aβ25–35 in PBS to be much higher than that of Aβ25–35 in PB. Moreover, Aβ-induced cytotoxicity assays showed Aβ incubated in PBS to be more cytotoxic than that incubated in PB. These results thus demonstrate that Aβ(25–35) - associated free radical generation is strongly influenced by the aggregational state of the peptides.</abstract><cop>Netherlands</cop><pub>Elsevier Inc</pub><pmid>11833745</pmid><doi>10.1016/S0024-3205(01)01451-5</doi><tpages>9</tpages></addata></record> |
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| subjects | Aggregation Alzheimer Disease - metabolism Alzheimer's disease Amyloid beta-Peptides - metabolism Amyloid beta-Peptides - toxicity Animals Beta amyloid Cyclic N-Oxides Cytotoxicity Deferoxamine - pharmacology Drug Antagonism Electron spin resonance Electron Spin Resonance Spectroscopy Formazans - metabolism Free radical Free Radicals - analysis Free Radicals - metabolism Iron Nitrogen Oxides - metabolism PC12 Cells - drug effects PC12 Cells - metabolism Peptide Fragments - metabolism Peptide Fragments - toxicity Protein Structure, Quaternary Rats Tetrazolium Salts - metabolism |
| title | Amyloid-β-protein (Aβ) (25–35)-associated free radical generation is strongly influenced by the aggregational state of the peptides |
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