Identification and characterization of Ich-3, a member of the interleukin-1beta converting enzyme (ICE)/Ced-3 family and an upstream regulator of ICE
We report here the isolation and characterization of a new member of the ice/ced-3 family of cell death genes, named ich-3. The predicted amino acid sequence of Ich-3 protein shares 54% identity with murine interleukin-1beta converting enzyme (ICE). Overexpression of ich-3 in Rat-1 and HeLa cells in...
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| Veröffentlicht in: | The Journal of biological chemistry 1996-08, Vol.271 (34), p.20580 |
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| container_issue | 34 |
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| container_title | The Journal of biological chemistry |
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| creator | Wang, S Miura, M Jung, Y k Zhu, H Gagliardini, V Shi, L Greenberg, A H Yuan, J |
| description | We report here the isolation and characterization of a new member of the ice/ced-3 family of cell death genes, named ich-3. The predicted amino acid sequence of Ich-3 protein shares 54% identity with murine interleukin-1beta converting enzyme (ICE). Overexpression of ich-3 in Rat-1 and HeLa cells induces apoptosis, which can be inhibited by CrmA and Bcl-2. The mRNA and proteins of ich-3 are dramatically induced in vivo upon stimulation with lipopolysaccharide, an inducer of septic shock. The ich-3 gene product can be cleaved by cytotoxic T cells granule serine protease granzyme B, suggesting that Ich-3 may mediate apoptosis induced by granzyme B. Ich-3 does not process proIL-1beta directly but does promote proIL-1beta processing by ICE. These results suggest that Ich-3 may play a very important role in apoptosis and inflammatory responses and may be an upstream regulator of ICE. |
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The predicted amino acid sequence of Ich-3 protein shares 54% identity with murine interleukin-1beta converting enzyme (ICE). Overexpression of ich-3 in Rat-1 and HeLa cells induces apoptosis, which can be inhibited by CrmA and Bcl-2. The mRNA and proteins of ich-3 are dramatically induced in vivo upon stimulation with lipopolysaccharide, an inducer of septic shock. The ich-3 gene product can be cleaved by cytotoxic T cells granule serine protease granzyme B, suggesting that Ich-3 may mediate apoptosis induced by granzyme B. Ich-3 does not process proIL-1beta directly but does promote proIL-1beta processing by ICE. These results suggest that Ich-3 may play a very important role in apoptosis and inflammatory responses and may be an upstream regulator of ICE.</description><identifier>ISSN: 0021-9258</identifier><identifier>PMID: 8702803</identifier><language>eng</language><publisher>United States</publisher><subject>Amino Acid Sequence ; Animals ; Apoptosis ; Base Sequence ; Caspase 1 ; Caspases ; Caspases, Initiator ; Cysteine Endopeptidases - metabolism ; DNA Primers - chemistry ; Gene Expression ; Genes ; Granzymes ; Inflammation ; Lipopolysaccharides - pharmacology ; Mice ; Molecular Sequence Data ; Multigene Family ; Proteins - chemistry ; Proteins - genetics ; Proteins - metabolism ; Rats ; RNA, Messenger - genetics ; Sequence Alignment ; Sequence Homology, Amino Acid ; Serine Endopeptidases - metabolism ; Tissue Distribution</subject><ispartof>The Journal of biological chemistry, 1996-08, Vol.271 (34), p.20580</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8702803$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, S</creatorcontrib><creatorcontrib>Miura, M</creatorcontrib><creatorcontrib>Jung, Y k</creatorcontrib><creatorcontrib>Zhu, H</creatorcontrib><creatorcontrib>Gagliardini, V</creatorcontrib><creatorcontrib>Shi, L</creatorcontrib><creatorcontrib>Greenberg, A H</creatorcontrib><creatorcontrib>Yuan, J</creatorcontrib><title>Identification and characterization of Ich-3, a member of the interleukin-1beta converting enzyme (ICE)/Ced-3 family and an upstream regulator of ICE</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We report here the isolation and characterization of a new member of the ice/ced-3 family of cell death genes, named ich-3. The predicted amino acid sequence of Ich-3 protein shares 54% identity with murine interleukin-1beta converting enzyme (ICE). Overexpression of ich-3 in Rat-1 and HeLa cells induces apoptosis, which can be inhibited by CrmA and Bcl-2. The mRNA and proteins of ich-3 are dramatically induced in vivo upon stimulation with lipopolysaccharide, an inducer of septic shock. The ich-3 gene product can be cleaved by cytotoxic T cells granule serine protease granzyme B, suggesting that Ich-3 may mediate apoptosis induced by granzyme B. Ich-3 does not process proIL-1beta directly but does promote proIL-1beta processing by ICE. These results suggest that Ich-3 may play a very important role in apoptosis and inflammatory responses and may be an upstream regulator of ICE.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Base Sequence</subject><subject>Caspase 1</subject><subject>Caspases</subject><subject>Caspases, Initiator</subject><subject>Cysteine Endopeptidases - metabolism</subject><subject>DNA Primers - chemistry</subject><subject>Gene Expression</subject><subject>Genes</subject><subject>Granzymes</subject><subject>Inflammation</subject><subject>Lipopolysaccharides - pharmacology</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Multigene Family</subject><subject>Proteins - chemistry</subject><subject>Proteins - genetics</subject><subject>Proteins - metabolism</subject><subject>Rats</subject><subject>RNA, Messenger - genetics</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Serine Endopeptidases - metabolism</subject><subject>Tissue Distribution</subject><issn>0021-9258</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNotUFFLwzAYzIMy5_QnCHlUMJg065I-SplaGPiy9_G1_bJFm7SkqdD9D_-vddu93HEcd3BXZM55IliWpPqG3Pb9F5-wzMSMzLTiieZyTn6LGn20xlYQbesp-JpWBwhQRQz2eDZbQ4vqwOQzBerQlRj-rXhAav0Ua3D4tp6JEiPQqvU_GKL1e4r-ODqkj0W-fnrJsWaSGnC2GU8r4OnQ9TEgOBpwPzQQ21PvFL8j1waaHu8vvCDbt_U2_2Cbz_cif92wLpWSVWAkF3olNC-zTGswXCkEFEoqXUOiZMoBl5AYMwkuZZJhxoUELmq1SlO5IA_n2m4oHda7LlgHYdxd3pF_3gVfuQ</recordid><startdate>19960823</startdate><enddate>19960823</enddate><creator>Wang, S</creator><creator>Miura, M</creator><creator>Jung, Y k</creator><creator>Zhu, H</creator><creator>Gagliardini, V</creator><creator>Shi, L</creator><creator>Greenberg, A H</creator><creator>Yuan, J</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope></search><sort><creationdate>19960823</creationdate><title>Identification and characterization of Ich-3, a member of the interleukin-1beta converting enzyme (ICE)/Ced-3 family and an upstream regulator of ICE</title><author>Wang, S ; Miura, M ; Jung, Y k ; Zhu, H ; Gagliardini, V ; Shi, L ; Greenberg, A H ; Yuan, J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p533-caf30186180b9988af077eae17378da27350ae4a2ff50a03329e9013a01d76553</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Base Sequence</topic><topic>Caspase 1</topic><topic>Caspases</topic><topic>Caspases, Initiator</topic><topic>Cysteine Endopeptidases - metabolism</topic><topic>DNA Primers - chemistry</topic><topic>Gene Expression</topic><topic>Genes</topic><topic>Granzymes</topic><topic>Inflammation</topic><topic>Lipopolysaccharides - pharmacology</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Multigene Family</topic><topic>Proteins - chemistry</topic><topic>Proteins - genetics</topic><topic>Proteins - metabolism</topic><topic>Rats</topic><topic>RNA, Messenger - genetics</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Serine Endopeptidases - metabolism</topic><topic>Tissue Distribution</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, S</creatorcontrib><creatorcontrib>Miura, M</creatorcontrib><creatorcontrib>Jung, Y k</creatorcontrib><creatorcontrib>Zhu, H</creatorcontrib><creatorcontrib>Gagliardini, V</creatorcontrib><creatorcontrib>Shi, L</creatorcontrib><creatorcontrib>Greenberg, A H</creatorcontrib><creatorcontrib>Yuan, J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, S</au><au>Miura, M</au><au>Jung, Y k</au><au>Zhu, H</au><au>Gagliardini, V</au><au>Shi, L</au><au>Greenberg, A H</au><au>Yuan, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and characterization of Ich-3, a member of the interleukin-1beta converting enzyme (ICE)/Ced-3 family and an upstream regulator of ICE</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1996-08-23</date><risdate>1996</risdate><volume>271</volume><issue>34</issue><spage>20580</spage><pages>20580-</pages><issn>0021-9258</issn><abstract>We report here the isolation and characterization of a new member of the ice/ced-3 family of cell death genes, named ich-3. The predicted amino acid sequence of Ich-3 protein shares 54% identity with murine interleukin-1beta converting enzyme (ICE). Overexpression of ich-3 in Rat-1 and HeLa cells induces apoptosis, which can be inhibited by CrmA and Bcl-2. The mRNA and proteins of ich-3 are dramatically induced in vivo upon stimulation with lipopolysaccharide, an inducer of septic shock. The ich-3 gene product can be cleaved by cytotoxic T cells granule serine protease granzyme B, suggesting that Ich-3 may mediate apoptosis induced by granzyme B. Ich-3 does not process proIL-1beta directly but does promote proIL-1beta processing by ICE. These results suggest that Ich-3 may play a very important role in apoptosis and inflammatory responses and may be an upstream regulator of ICE.</abstract><cop>United States</cop><pmid>8702803</pmid></addata></record> |
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| ispartof | The Journal of biological chemistry, 1996-08, Vol.271 (34), p.20580 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Apoptosis Base Sequence Caspase 1 Caspases Caspases, Initiator Cysteine Endopeptidases - metabolism DNA Primers - chemistry Gene Expression Genes Granzymes Inflammation Lipopolysaccharides - pharmacology Mice Molecular Sequence Data Multigene Family Proteins - chemistry Proteins - genetics Proteins - metabolism Rats RNA, Messenger - genetics Sequence Alignment Sequence Homology, Amino Acid Serine Endopeptidases - metabolism Tissue Distribution |
| title | Identification and characterization of Ich-3, a member of the interleukin-1beta converting enzyme (ICE)/Ced-3 family and an upstream regulator of ICE |
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