Instability of mutant Cu/Zn superoxide dismutase (Ala4Thr) associated with familial amyotrophic lateral sclerosis
In about 20–25% of cases of familial amyotrophic lateral sclerosis (FALS) patients have mutations in the Cu/Zn superoxide dismutase (SOD1) gene. The mechanism through which the mutations in the SOD1 gene cause ALS still remains unknown. We performed pulse-chase experiments using a system for the tra...
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| Veröffentlicht in: | Neuroscience letters 1996-06, Vol.211 (2), p.129-131 |
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| container_title | Neuroscience letters |
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| creator | Nakano, Ryoichi Inuzuka, Takashi Kikugawa, Koki Takahashi, Hitoshi Sakimura, Kenji Fujii, Junichi Taniguchi, Naoyuki Tsuji, Shoji |
| description | In about 20–25% of cases of familial amyotrophic lateral sclerosis (FALS) patients have mutations in the Cu/Zn superoxide dismutase (SOD1) gene. The mechanism through which the mutations in the SOD1 gene cause ALS still remains unknown. We performed pulse-chase experiments using a system for the transient expression of human SOD1 in COS7 cells to examine whether the Ala4Thr mutation, which we previously reported, decreases the stability of SOD L The expression vector (pEF-BOS) carrying the wild-type or mutant (Ala4Thr) human SOD1 cDNA was transfected into COS7 cells, and transiently expressed human SOD 1 was then metabolically radiolabeled. Half-lives of the wild-type and the Ala4Thr mutant SOD1 were determined to be 78 h and 18 h, respectively. These results sulgest that the Ala4Thr mutation in SOD1 decreases the stability of SOD1 and that this instability may play an important role in the pathogenesis of the degeneration of motor neurons in FALS. |
| doi_str_mv | 10.1016/0304-3940(96)12701-4 |
| format | Article |
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The mechanism through which the mutations in the SOD1 gene cause ALS still remains unknown. We performed pulse-chase experiments using a system for the transient expression of human SOD1 in COS7 cells to examine whether the Ala4Thr mutation, which we previously reported, decreases the stability of SOD L The expression vector (pEF-BOS) carrying the wild-type or mutant (Ala4Thr) human SOD1 cDNA was transfected into COS7 cells, and transiently expressed human SOD 1 was then metabolically radiolabeled. Half-lives of the wild-type and the Ala4Thr mutant SOD1 were determined to be 78 h and 18 h, respectively. These results sulgest that the Ala4Thr mutation in SOD1 decreases the stability of SOD1 and that this instability may play an important role in the pathogenesis of the degeneration of motor neurons in FALS.</description><identifier>ISSN: 0304-3940</identifier><identifier>EISSN: 1872-7972</identifier><identifier>DOI: 10.1016/0304-3940(96)12701-4</identifier><identifier>PMID: 8830861</identifier><identifier>CODEN: NELED5</identifier><language>eng</language><publisher>Shannon: Elsevier Ireland Ltd</publisher><subject>Amyotrophic lateral sclerosis ; Amyotrophic Lateral Sclerosis - enzymology ; Amyotrophic Lateral Sclerosis - genetics ; Biological and medical sciences ; Cell Line ; Cu/Zn superoxide dismutase ; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases ; DNA, Complementary - biosynthesis ; Exons - physiology ; Gene Expression Regulation, Enzymologic ; Half-Life ; Humans ; Instability ; Medical sciences ; Mutation - physiology ; Nerve Degeneration - physiology ; Neurology ; Pulse-chase ; Recombinant protein ; Superoxide Dismutase - genetics</subject><ispartof>Neuroscience letters, 1996-06, Vol.211 (2), p.129-131</ispartof><rights>1996</rights><rights>1996 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-23f5b7985a5b2ad79253d832dd9e5b56c5b4b08a6bd6add302faa6172f79be0d3</citedby><cites>FETCH-LOGICAL-c417t-23f5b7985a5b2ad79253d832dd9e5b56c5b4b08a6bd6add302faa6172f79be0d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0304-3940(96)12701-4$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3154724$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8830861$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nakano, Ryoichi</creatorcontrib><creatorcontrib>Inuzuka, Takashi</creatorcontrib><creatorcontrib>Kikugawa, Koki</creatorcontrib><creatorcontrib>Takahashi, Hitoshi</creatorcontrib><creatorcontrib>Sakimura, Kenji</creatorcontrib><creatorcontrib>Fujii, Junichi</creatorcontrib><creatorcontrib>Taniguchi, Naoyuki</creatorcontrib><creatorcontrib>Tsuji, Shoji</creatorcontrib><title>Instability of mutant Cu/Zn superoxide dismutase (Ala4Thr) associated with familial amyotrophic lateral sclerosis</title><title>Neuroscience letters</title><addtitle>Neurosci Lett</addtitle><description>In about 20–25% of cases of familial amyotrophic lateral sclerosis (FALS) patients have mutations in the Cu/Zn superoxide dismutase (SOD1) gene. The mechanism through which the mutations in the SOD1 gene cause ALS still remains unknown. We performed pulse-chase experiments using a system for the transient expression of human SOD1 in COS7 cells to examine whether the Ala4Thr mutation, which we previously reported, decreases the stability of SOD L The expression vector (pEF-BOS) carrying the wild-type or mutant (Ala4Thr) human SOD1 cDNA was transfected into COS7 cells, and transiently expressed human SOD 1 was then metabolically radiolabeled. Half-lives of the wild-type and the Ala4Thr mutant SOD1 were determined to be 78 h and 18 h, respectively. These results sulgest that the Ala4Thr mutation in SOD1 decreases the stability of SOD1 and that this instability may play an important role in the pathogenesis of the degeneration of motor neurons in FALS.</description><subject>Amyotrophic lateral sclerosis</subject><subject>Amyotrophic Lateral Sclerosis - enzymology</subject><subject>Amyotrophic Lateral Sclerosis - genetics</subject><subject>Biological and medical sciences</subject><subject>Cell Line</subject><subject>Cu/Zn superoxide dismutase</subject><subject>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</subject><subject>DNA, Complementary - biosynthesis</subject><subject>Exons - physiology</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Half-Life</subject><subject>Humans</subject><subject>Instability</subject><subject>Medical sciences</subject><subject>Mutation - physiology</subject><subject>Nerve Degeneration - physiology</subject><subject>Neurology</subject><subject>Pulse-chase</subject><subject>Recombinant protein</subject><subject>Superoxide Dismutase - genetics</subject><issn>0304-3940</issn><issn>1872-7972</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUuLFDEUhYMoYzv6DxSyEJlZlJN3qjbC0PgYGHAzbtyEm0fRkXr0JCm1_70pu-mlrgI53z3cew5Cryl5TwlVN4QT0fBOkKtOXVOmCW3EE7ShrWaN7jR7ijZn5Dl6kfMPQoikUlygi7blpFV0gx7vplzAxiGWA557PC4FpoK3y833CedlH9L8O_qAfcyrlAO-uh1APOzSNYacZxehBI9_xbLDPYzVBwYM42Euad7vosND1VP9y26oXjnml-hZD0MOr07vJfr26ePD9ktz__Xz3fb2vnGC6tIw3kuru1aCtAy87pjkvuXM-y5IK5WTVljSgrJegfecsB5AUc163dlAPL9E746--zQ_LiEXM8bswjDAFOYlG91y1SnO_wtS2QpSF6mgOIKuHpJT6M0-xRHSwVBi1krMmrdZ8zadMn8rMaKOvTn5L3YM_jx06qDqb086ZAdDn2ByMZ8xXhvTbLX5cMRCDe1nDMlkF8Pkgo8puGL8HP-9xx9soKkQ</recordid><startdate>19960621</startdate><enddate>19960621</enddate><creator>Nakano, Ryoichi</creator><creator>Inuzuka, Takashi</creator><creator>Kikugawa, Koki</creator><creator>Takahashi, Hitoshi</creator><creator>Sakimura, Kenji</creator><creator>Fujii, Junichi</creator><creator>Taniguchi, Naoyuki</creator><creator>Tsuji, Shoji</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>7TK</scope><scope>7X8</scope></search><sort><creationdate>19960621</creationdate><title>Instability of mutant Cu/Zn superoxide dismutase (Ala4Thr) associated with familial amyotrophic lateral sclerosis</title><author>Nakano, Ryoichi ; Inuzuka, Takashi ; Kikugawa, Koki ; Takahashi, Hitoshi ; Sakimura, Kenji ; Fujii, Junichi ; Taniguchi, Naoyuki ; Tsuji, Shoji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-23f5b7985a5b2ad79253d832dd9e5b56c5b4b08a6bd6add302faa6172f79be0d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Amyotrophic lateral sclerosis</topic><topic>Amyotrophic Lateral Sclerosis - enzymology</topic><topic>Amyotrophic Lateral Sclerosis - genetics</topic><topic>Biological and medical sciences</topic><topic>Cell Line</topic><topic>Cu/Zn superoxide dismutase</topic><topic>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</topic><topic>DNA, Complementary - biosynthesis</topic><topic>Exons - physiology</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Half-Life</topic><topic>Humans</topic><topic>Instability</topic><topic>Medical sciences</topic><topic>Mutation - physiology</topic><topic>Nerve Degeneration - physiology</topic><topic>Neurology</topic><topic>Pulse-chase</topic><topic>Recombinant protein</topic><topic>Superoxide Dismutase - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nakano, Ryoichi</creatorcontrib><creatorcontrib>Inuzuka, Takashi</creatorcontrib><creatorcontrib>Kikugawa, Koki</creatorcontrib><creatorcontrib>Takahashi, Hitoshi</creatorcontrib><creatorcontrib>Sakimura, Kenji</creatorcontrib><creatorcontrib>Fujii, Junichi</creatorcontrib><creatorcontrib>Taniguchi, Naoyuki</creatorcontrib><creatorcontrib>Tsuji, Shoji</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><jtitle>Neuroscience letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nakano, Ryoichi</au><au>Inuzuka, Takashi</au><au>Kikugawa, Koki</au><au>Takahashi, Hitoshi</au><au>Sakimura, Kenji</au><au>Fujii, Junichi</au><au>Taniguchi, Naoyuki</au><au>Tsuji, Shoji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Instability of mutant Cu/Zn superoxide dismutase (Ala4Thr) associated with familial amyotrophic lateral sclerosis</atitle><jtitle>Neuroscience letters</jtitle><addtitle>Neurosci Lett</addtitle><date>1996-06-21</date><risdate>1996</risdate><volume>211</volume><issue>2</issue><spage>129</spage><epage>131</epage><pages>129-131</pages><issn>0304-3940</issn><eissn>1872-7972</eissn><coden>NELED5</coden><abstract>In about 20–25% of cases of familial amyotrophic lateral sclerosis (FALS) patients have mutations in the Cu/Zn superoxide dismutase (SOD1) gene. The mechanism through which the mutations in the SOD1 gene cause ALS still remains unknown. We performed pulse-chase experiments using a system for the transient expression of human SOD1 in COS7 cells to examine whether the Ala4Thr mutation, which we previously reported, decreases the stability of SOD L The expression vector (pEF-BOS) carrying the wild-type or mutant (Ala4Thr) human SOD1 cDNA was transfected into COS7 cells, and transiently expressed human SOD 1 was then metabolically radiolabeled. Half-lives of the wild-type and the Ala4Thr mutant SOD1 were determined to be 78 h and 18 h, respectively. These results sulgest that the Ala4Thr mutation in SOD1 decreases the stability of SOD1 and that this instability may play an important role in the pathogenesis of the degeneration of motor neurons in FALS.</abstract><cop>Shannon</cop><pub>Elsevier Ireland Ltd</pub><pmid>8830861</pmid><doi>10.1016/0304-3940(96)12701-4</doi><tpages>3</tpages></addata></record> |
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| ispartof | Neuroscience letters, 1996-06, Vol.211 (2), p.129-131 |
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| subjects | Amyotrophic lateral sclerosis Amyotrophic Lateral Sclerosis - enzymology Amyotrophic Lateral Sclerosis - genetics Biological and medical sciences Cell Line Cu/Zn superoxide dismutase Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases DNA, Complementary - biosynthesis Exons - physiology Gene Expression Regulation, Enzymologic Half-Life Humans Instability Medical sciences Mutation - physiology Nerve Degeneration - physiology Neurology Pulse-chase Recombinant protein Superoxide Dismutase - genetics |
| title | Instability of mutant Cu/Zn superoxide dismutase (Ala4Thr) associated with familial amyotrophic lateral sclerosis |
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