Caspase-mediated cleavage of the U snRNP-associated Sm-F protein during apoptosis
Recent studies have implicated the dying cell as a potential reservoir of modified autoantigens that might initiate and drive systemic autoimmunity in susceptible hosts. The spliceosomal Sm proteins are recognized by the so-called anti-Sm autoantibodies, an antibody population found exclusively in p...
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| Veröffentlicht in: | Cell death and differentiation 2003-05, Vol.10 (5), p.570-579 |
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| creator | Malmegrim de Farias, K C R Saelens, X Pruijn, G J M Vandenabeele, P van Venrooij, W J |
| description | Recent studies have implicated the dying cell as a potential reservoir of modified autoantigens that might initiate and drive systemic autoimmunity in susceptible hosts. The spliceosomal Sm proteins are recognized by the so-called anti-Sm autoantibodies, an antibody population found exclusively in patients suffering from systemic lupus erythematosus. We have studied the effects of apoptosis on the Sm proteins and demonstrate that one of the Sm proteins, the Sm-F protein, is proteolytically cleaved in apoptotic cells. Cleavage of the Sm-F protein generates a 9-kDa apoptotic fragment, which remains associated with the U snRNP complexes in apoptotic cells. Sm-F cleavage is dependent on caspase activation and the cleavage site has been located near the C-terminus, EEED
81
↓G. Use of different caspase inhibitors suggests that besides caspase-8 other caspases are implicated in Sm-F cleavage. A C-terminally truncated mutant of the Sm-F protein, representing the modified form of the protein, is capable of forming an Sm E–F–G complex
in vitro
that is recognized by many anti-Sm patient sera. |
| doi_str_mv | 10.1038/sj.cdd.4401196 |
| format | Article |
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81
↓G. Use of different caspase inhibitors suggests that besides caspase-8 other caspases are implicated in Sm-F cleavage. A C-terminally truncated mutant of the Sm-F protein, representing the modified form of the protein, is capable of forming an Sm E–F–G complex
in vitro
that is recognized by many anti-Sm patient sera.</description><identifier>ISSN: 1350-9047</identifier><identifier>EISSN: 1476-5403</identifier><identifier>DOI: 10.1038/sj.cdd.4401196</identifier><identifier>PMID: 12728255</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Antibodies, Monoclonal - pharmacology ; Antigens ; Apoptosis ; Apoptosis - drug effects ; Apoptosis - immunology ; Autoantibodies - blood ; Autoantigens ; Biochemistry ; Biomedical and Life Sciences ; Blotting, Western ; Caspase Inhibitors ; Caspases - metabolism ; Cell Biology ; Cell Cycle Analysis ; Cell death ; Cell Line, Tumor ; Cysteine Proteinase Inhibitors - pharmacology ; Electrophoresis, Polyacrylamide Gel ; fas Receptor - immunology ; HeLa Cells ; Humans ; Jurkat Cells ; Life Sciences ; Lupus ; Lupus Erythematosus, Systemic - blood ; Lupus Erythematosus, Systemic - immunology ; Monoclonal antibodies ; original-paper ; Proteins ; Ribonucleoprotein, U1 Small Nuclear - metabolism ; Ribonucleoproteins, Small Nuclear - genetics ; Ribonucleoproteins, Small Nuclear - immunology ; Ribonucleoproteins, Small Nuclear - metabolism ; snRNP Core Proteins ; Stem Cells ; Time Factors</subject><ispartof>Cell death and differentiation, 2003-05, Vol.10 (5), p.570-579</ispartof><rights>Springer Nature Limited 2003</rights><rights>Copyright Nature Publishing Group May 2003</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c398t-9a01761ca098a5a13b2c0076ac93bbfd5d6f7de72f336372b00e8e536ed675db3</citedby><cites>FETCH-LOGICAL-c398t-9a01761ca098a5a13b2c0076ac93bbfd5d6f7de72f336372b00e8e536ed675db3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/sj.cdd.4401196$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/sj.cdd.4401196$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12728255$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Malmegrim de Farias, K C R</creatorcontrib><creatorcontrib>Saelens, X</creatorcontrib><creatorcontrib>Pruijn, G J M</creatorcontrib><creatorcontrib>Vandenabeele, P</creatorcontrib><creatorcontrib>van Venrooij, W J</creatorcontrib><title>Caspase-mediated cleavage of the U snRNP-associated Sm-F protein during apoptosis</title><title>Cell death and differentiation</title><addtitle>Cell Death Differ</addtitle><addtitle>Cell Death Differ</addtitle><description>Recent studies have implicated the dying cell as a potential reservoir of modified autoantigens that might initiate and drive systemic autoimmunity in susceptible hosts. The spliceosomal Sm proteins are recognized by the so-called anti-Sm autoantibodies, an antibody population found exclusively in patients suffering from systemic lupus erythematosus. We have studied the effects of apoptosis on the Sm proteins and demonstrate that one of the Sm proteins, the Sm-F protein, is proteolytically cleaved in apoptotic cells. Cleavage of the Sm-F protein generates a 9-kDa apoptotic fragment, which remains associated with the U snRNP complexes in apoptotic cells. Sm-F cleavage is dependent on caspase activation and the cleavage site has been located near the C-terminus, EEED
81
↓G. Use of different caspase inhibitors suggests that besides caspase-8 other caspases are implicated in Sm-F cleavage. A C-terminally truncated mutant of the Sm-F protein, representing the modified form of the protein, is capable of forming an Sm E–F–G complex
in vitro
that is recognized by many anti-Sm patient sera.</description><subject>Antibodies, Monoclonal - pharmacology</subject><subject>Antigens</subject><subject>Apoptosis</subject><subject>Apoptosis - drug effects</subject><subject>Apoptosis - immunology</subject><subject>Autoantibodies - blood</subject><subject>Autoantigens</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Blotting, Western</subject><subject>Caspase Inhibitors</subject><subject>Caspases - metabolism</subject><subject>Cell Biology</subject><subject>Cell Cycle Analysis</subject><subject>Cell death</subject><subject>Cell Line, Tumor</subject><subject>Cysteine Proteinase Inhibitors - pharmacology</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>fas Receptor - immunology</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Jurkat Cells</subject><subject>Life Sciences</subject><subject>Lupus</subject><subject>Lupus Erythematosus, Systemic - blood</subject><subject>Lupus Erythematosus, Systemic - immunology</subject><subject>Monoclonal antibodies</subject><subject>original-paper</subject><subject>Proteins</subject><subject>Ribonucleoprotein, U1 Small Nuclear - metabolism</subject><subject>Ribonucleoproteins, Small Nuclear - genetics</subject><subject>Ribonucleoproteins, Small Nuclear - immunology</subject><subject>Ribonucleoproteins, Small Nuclear - metabolism</subject><subject>snRNP Core Proteins</subject><subject>Stem Cells</subject><subject>Time Factors</subject><issn>1350-9047</issn><issn>1476-5403</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp1kE1Lw0AQhhdRbK1ePUrw4C3tbDbZTY5SrArF756Xze6kprRJzCSC_94tLRQETzOHZ955eRi75DDmINIJrcbWuXEcA-eZPGJDHisZJjGIY7-LBMIMYjVgZ0QrAJAqk6dswCMVpVGSDNnr1FBjCMMNutJ06AK7RvNtlhjURdB9YrAIqHp7egkNUW13yPsmnAVNW3dYVoHr27JaBqapm66mks7ZSWHWhBf7OWKL2d3H9CGcP98_Tm_noRVZ2oWZAa4ktway1CSGizyyAEoam4k8L1ziZKEcqqgQQgoV5QCYYiIkOqkSl4sRu9nl-iJfPVKnNyVZXK9NhXVPWokolgpiD17_AVd131a-m464UsIXkB4a7yDb1kQtFrppy41pfzQHvTWtaaW9ab037Q-u9ql97t0d8L1aD0x2ADVbQdge3v4T-Qt42IkX</recordid><startdate>20030501</startdate><enddate>20030501</enddate><creator>Malmegrim de Farias, K C R</creator><creator>Saelens, X</creator><creator>Pruijn, G J M</creator><creator>Vandenabeele, P</creator><creator>van Venrooij, W J</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</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>3V.</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20030501</creationdate><title>Caspase-mediated cleavage of the U snRNP-associated Sm-F protein during apoptosis</title><author>Malmegrim de Farias, K C R ; Saelens, X ; Pruijn, G J M ; Vandenabeele, P ; van Venrooij, W J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c398t-9a01761ca098a5a13b2c0076ac93bbfd5d6f7de72f336372b00e8e536ed675db3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Antibodies, Monoclonal - pharmacology</topic><topic>Antigens</topic><topic>Apoptosis</topic><topic>Apoptosis - drug effects</topic><topic>Apoptosis - immunology</topic><topic>Autoantibodies - blood</topic><topic>Autoantigens</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Blotting, Western</topic><topic>Caspase Inhibitors</topic><topic>Caspases - metabolism</topic><topic>Cell Biology</topic><topic>Cell Cycle Analysis</topic><topic>Cell death</topic><topic>Cell Line, Tumor</topic><topic>Cysteine Proteinase Inhibitors - pharmacology</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>fas Receptor - immunology</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Jurkat Cells</topic><topic>Life Sciences</topic><topic>Lupus</topic><topic>Lupus Erythematosus, Systemic - blood</topic><topic>Lupus Erythematosus, Systemic - immunology</topic><topic>Monoclonal antibodies</topic><topic>original-paper</topic><topic>Proteins</topic><topic>Ribonucleoprotein, U1 Small Nuclear - metabolism</topic><topic>Ribonucleoproteins, Small Nuclear - genetics</topic><topic>Ribonucleoproteins, Small Nuclear - immunology</topic><topic>Ribonucleoproteins, Small Nuclear - metabolism</topic><topic>snRNP Core Proteins</topic><topic>Stem Cells</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Malmegrim de Farias, K C R</creatorcontrib><creatorcontrib>Saelens, X</creatorcontrib><creatorcontrib>Pruijn, G J M</creatorcontrib><creatorcontrib>Vandenabeele, P</creatorcontrib><creatorcontrib>van Venrooij, W J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell death and differentiation</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Malmegrim de Farias, K C R</au><au>Saelens, X</au><au>Pruijn, G J M</au><au>Vandenabeele, P</au><au>van Venrooij, W J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Caspase-mediated cleavage of the U snRNP-associated Sm-F protein during apoptosis</atitle><jtitle>Cell death and differentiation</jtitle><stitle>Cell Death Differ</stitle><addtitle>Cell Death Differ</addtitle><date>2003-05-01</date><risdate>2003</risdate><volume>10</volume><issue>5</issue><spage>570</spage><epage>579</epage><pages>570-579</pages><issn>1350-9047</issn><eissn>1476-5403</eissn><abstract>Recent studies have implicated the dying cell as a potential reservoir of modified autoantigens that might initiate and drive systemic autoimmunity in susceptible hosts. The spliceosomal Sm proteins are recognized by the so-called anti-Sm autoantibodies, an antibody population found exclusively in patients suffering from systemic lupus erythematosus. We have studied the effects of apoptosis on the Sm proteins and demonstrate that one of the Sm proteins, the Sm-F protein, is proteolytically cleaved in apoptotic cells. Cleavage of the Sm-F protein generates a 9-kDa apoptotic fragment, which remains associated with the U snRNP complexes in apoptotic cells. Sm-F cleavage is dependent on caspase activation and the cleavage site has been located near the C-terminus, EEED
81
↓G. Use of different caspase inhibitors suggests that besides caspase-8 other caspases are implicated in Sm-F cleavage. A C-terminally truncated mutant of the Sm-F protein, representing the modified form of the protein, is capable of forming an Sm E–F–G complex
in vitro
that is recognized by many anti-Sm patient sera.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>12728255</pmid><doi>10.1038/sj.cdd.4401196</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Antibodies, Monoclonal - pharmacology Antigens Apoptosis Apoptosis - drug effects Apoptosis - immunology Autoantibodies - blood Autoantigens Biochemistry Biomedical and Life Sciences Blotting, Western Caspase Inhibitors Caspases - metabolism Cell Biology Cell Cycle Analysis Cell death Cell Line, Tumor Cysteine Proteinase Inhibitors - pharmacology Electrophoresis, Polyacrylamide Gel fas Receptor - immunology HeLa Cells Humans Jurkat Cells Life Sciences Lupus Lupus Erythematosus, Systemic - blood Lupus Erythematosus, Systemic - immunology Monoclonal antibodies original-paper Proteins Ribonucleoprotein, U1 Small Nuclear - metabolism Ribonucleoproteins, Small Nuclear - genetics Ribonucleoproteins, Small Nuclear - immunology Ribonucleoproteins, Small Nuclear - metabolism snRNP Core Proteins Stem Cells Time Factors |
| title | Caspase-mediated cleavage of the U snRNP-associated Sm-F protein during apoptosis |
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