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Recognition by TNF-α of the GPI-anchor glycan induces apoptosis of U937 cells
Tumor necrosis factor-α (TNF-α) binds to TNF-α receptors (TNFR) to produce a hexameric (TNF-α) 3–(TNFR) 3 structure that stimulates apoptosis. We found by using ELISA that TNF-α binds to the glycosylphosphatidylinositol (GPI) anchor glycans of carcinoembryonic antigen, human placental alkaline phosp...
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| Published in: | Archives of biochemistry and biophysics 2004-06, Vol.426 (2), p.298-305 |
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| cites | cdi_FETCH-LOGICAL-c349t-5d8dcc3976da1e1c985519237d152e6ae9236cb26c88d1dfd3d988461455c57a3 |
| container_end_page | 305 |
| container_issue | 2 |
| container_start_page | 298 |
| container_title | Archives of biochemistry and biophysics |
| container_volume | 426 |
| creator | Fukushima, Keiko Ishiyama, Chikako Yamashita, Katsuko |
| description | Tumor necrosis factor-α (TNF-α) binds to TNF-α receptors (TNFR) to produce a hexameric (TNF-α)
3–(TNFR)
3 structure that stimulates apoptosis. We found by using ELISA that TNF-α binds to the glycosylphosphatidylinositol (GPI) anchor glycans of carcinoembryonic antigen, human placental alkaline phosphatase (hAP), and Tamm–Horsfall glycoprotein. These binding abilities were inhibited by 10
−6
M mannose-6-phosphate. Treatment of hAP with mild acid and phosphatase, which releases the
N-acetylglucosamine (GlcNAc) β1
→
phosphate
→
6 residue from the GPI-anchor glycan of hAP, abrogated the binding of TNF-α to hAP. Thus, TNF-α binds to the GlcNAcβ1
→
phosphate
→
6Man residue in GPI-anchor glycans. To investigate whether the carbohydrate-binding ability of TNF-α is related to its physiological functions, human lymphoma U937 cells were used. TNF-α stimulates U937 cell apoptosis in a dose-dependent manner and the presence of mannose-6-phosphate inhibited this. TNF-α-dependent tyrosine phosphorylation of several proteins in U937 cells was also diminished by mannose-6-phosphate. Phosphatidylinositol-specific phospholipase C-pretreatment also inhibited this tyrosine phosphorylation. These data suggest that TNF-α stimulates U937 cell apoptosis by forming a high-affinity nanomeric (TNF-α)
3–(TNFR)
3–(GPI-anchored glycan)
3 complex. The GPI-anchored glycoprotein involved remains to be identified. |
| doi_str_mv | 10.1016/j.abb.2004.02.028 |
| format | article |
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3–(TNFR)
3 structure that stimulates apoptosis. We found by using ELISA that TNF-α binds to the glycosylphosphatidylinositol (GPI) anchor glycans of carcinoembryonic antigen, human placental alkaline phosphatase (hAP), and Tamm–Horsfall glycoprotein. These binding abilities were inhibited by 10
−6
M mannose-6-phosphate. Treatment of hAP with mild acid and phosphatase, which releases the
N-acetylglucosamine (GlcNAc) β1
→
phosphate
→
6 residue from the GPI-anchor glycan of hAP, abrogated the binding of TNF-α to hAP. Thus, TNF-α binds to the GlcNAcβ1
→
phosphate
→
6Man residue in GPI-anchor glycans. To investigate whether the carbohydrate-binding ability of TNF-α is related to its physiological functions, human lymphoma U937 cells were used. TNF-α stimulates U937 cell apoptosis in a dose-dependent manner and the presence of mannose-6-phosphate inhibited this. TNF-α-dependent tyrosine phosphorylation of several proteins in U937 cells was also diminished by mannose-6-phosphate. Phosphatidylinositol-specific phospholipase C-pretreatment also inhibited this tyrosine phosphorylation. These data suggest that TNF-α stimulates U937 cell apoptosis by forming a high-affinity nanomeric (TNF-α)
3–(TNFR)
3–(GPI-anchored glycan)
3 complex. The GPI-anchored glycoprotein involved remains to be identified.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/j.abb.2004.02.028</identifier><identifier>PMID: 15158680</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Apoptosis ; Apoptosis - drug effects ; Apoptosis - physiology ; Cell Cycle Proteins - metabolism ; Dose-Response Relationship, Drug ; GPI anchor ; GPI-Linked Proteins ; Humans ; Mannosephosphates - metabolism ; Mannosephosphates - pharmacology ; Membrane Proteins - metabolism ; Neoplasm Proteins - metabolism ; Protein Binding ; Signal Transduction - drug effects ; Signal Transduction - physiology ; TNF-α ; Tumor Necrosis Factor-alpha - metabolism ; Tumor Necrosis Factor-alpha - pharmacology ; U937 Cells ; β- N-acetylglucosaminyl phosphate diester</subject><ispartof>Archives of biochemistry and biophysics, 2004-06, Vol.426 (2), p.298-305</ispartof><rights>2004 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c349t-5d8dcc3976da1e1c985519237d152e6ae9236cb26c88d1dfd3d988461455c57a3</citedby><cites>FETCH-LOGICAL-c349t-5d8dcc3976da1e1c985519237d152e6ae9236cb26c88d1dfd3d988461455c57a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,783,787,27938,27939</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15158680$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fukushima, Keiko</creatorcontrib><creatorcontrib>Ishiyama, Chikako</creatorcontrib><creatorcontrib>Yamashita, Katsuko</creatorcontrib><title>Recognition by TNF-α of the GPI-anchor glycan induces apoptosis of U937 cells</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Tumor necrosis factor-α (TNF-α) binds to TNF-α receptors (TNFR) to produce a hexameric (TNF-α)
3–(TNFR)
3 structure that stimulates apoptosis. We found by using ELISA that TNF-α binds to the glycosylphosphatidylinositol (GPI) anchor glycans of carcinoembryonic antigen, human placental alkaline phosphatase (hAP), and Tamm–Horsfall glycoprotein. These binding abilities were inhibited by 10
−6
M mannose-6-phosphate. Treatment of hAP with mild acid and phosphatase, which releases the
N-acetylglucosamine (GlcNAc) β1
→
phosphate
→
6 residue from the GPI-anchor glycan of hAP, abrogated the binding of TNF-α to hAP. Thus, TNF-α binds to the GlcNAcβ1
→
phosphate
→
6Man residue in GPI-anchor glycans. To investigate whether the carbohydrate-binding ability of TNF-α is related to its physiological functions, human lymphoma U937 cells were used. TNF-α stimulates U937 cell apoptosis in a dose-dependent manner and the presence of mannose-6-phosphate inhibited this. TNF-α-dependent tyrosine phosphorylation of several proteins in U937 cells was also diminished by mannose-6-phosphate. Phosphatidylinositol-specific phospholipase C-pretreatment also inhibited this tyrosine phosphorylation. These data suggest that TNF-α stimulates U937 cell apoptosis by forming a high-affinity nanomeric (TNF-α)
3–(TNFR)
3–(GPI-anchored glycan)
3 complex. The GPI-anchored glycoprotein involved remains to be identified.</description><subject>Apoptosis</subject><subject>Apoptosis - drug effects</subject><subject>Apoptosis - physiology</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Dose-Response Relationship, Drug</subject><subject>GPI anchor</subject><subject>GPI-Linked Proteins</subject><subject>Humans</subject><subject>Mannosephosphates - metabolism</subject><subject>Mannosephosphates - pharmacology</subject><subject>Membrane Proteins - metabolism</subject><subject>Neoplasm Proteins - metabolism</subject><subject>Protein Binding</subject><subject>Signal Transduction - drug effects</subject><subject>Signal Transduction - physiology</subject><subject>TNF-α</subject><subject>Tumor Necrosis Factor-alpha - metabolism</subject><subject>Tumor Necrosis Factor-alpha - pharmacology</subject><subject>U937 Cells</subject><subject>β- N-acetylglucosaminyl phosphate diester</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><recordid>eNp9kMFKAzEQhoMotlYfwIvk5G1rZneTTfAkxdaCVJH2HLLJtE1pN3WzFfpYvojP5JYWvAk_zBy-_2fmJ-QWWB8YiIdV35RlP2Us77O0lTwjXWBKJCyT-TnpMsayREkBHXIV44oxgFykl6QDHLgUknXJ5ANtWFS-8aGi5Z5OJ8Pk55uGOW2WSEfv48RUdhlquljvramor9zOYqRmG7ZNiD4e0JnKCmpxvY7X5GJu1hFvTrNHZsPn6eAleX0bjQdPr4nNctUk3ElnbaYK4QwgWCU5B5VmhQOeojDY7sKWqbBSOnBzlzklZS4g59zywmQ9cn_M3dbhc4ex0RsfDxeYCsMu6gKUyCXPWxCOoK1DjDXO9bb2G1PvNTB9KFGvdFuiPpSoWdpKtp67U_iu3KD7c5xaa4HHI4Dti18eax2tx8qi8zXaRrvg_4n_BblngIo</recordid><startdate>20040615</startdate><enddate>20040615</enddate><creator>Fukushima, Keiko</creator><creator>Ishiyama, Chikako</creator><creator>Yamashita, Katsuko</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>7X8</scope></search><sort><creationdate>20040615</creationdate><title>Recognition by TNF-α of the GPI-anchor glycan induces apoptosis of U937 cells</title><author>Fukushima, Keiko ; Ishiyama, Chikako ; Yamashita, Katsuko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c349t-5d8dcc3976da1e1c985519237d152e6ae9236cb26c88d1dfd3d988461455c57a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Apoptosis</topic><topic>Apoptosis - drug effects</topic><topic>Apoptosis - physiology</topic><topic>Cell Cycle Proteins - metabolism</topic><topic>Dose-Response Relationship, Drug</topic><topic>GPI anchor</topic><topic>GPI-Linked Proteins</topic><topic>Humans</topic><topic>Mannosephosphates - metabolism</topic><topic>Mannosephosphates - pharmacology</topic><topic>Membrane Proteins - metabolism</topic><topic>Neoplasm Proteins - metabolism</topic><topic>Protein Binding</topic><topic>Signal Transduction - drug effects</topic><topic>Signal Transduction - physiology</topic><topic>TNF-α</topic><topic>Tumor Necrosis Factor-alpha - metabolism</topic><topic>Tumor Necrosis Factor-alpha - pharmacology</topic><topic>U937 Cells</topic><topic>β- N-acetylglucosaminyl phosphate diester</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fukushima, Keiko</creatorcontrib><creatorcontrib>Ishiyama, Chikako</creatorcontrib><creatorcontrib>Yamashita, Katsuko</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fukushima, Keiko</au><au>Ishiyama, Chikako</au><au>Yamashita, Katsuko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Recognition by TNF-α of the GPI-anchor glycan induces apoptosis of U937 cells</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>2004-06-15</date><risdate>2004</risdate><volume>426</volume><issue>2</issue><spage>298</spage><epage>305</epage><pages>298-305</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>Tumor necrosis factor-α (TNF-α) binds to TNF-α receptors (TNFR) to produce a hexameric (TNF-α)
3–(TNFR)
3 structure that stimulates apoptosis. We found by using ELISA that TNF-α binds to the glycosylphosphatidylinositol (GPI) anchor glycans of carcinoembryonic antigen, human placental alkaline phosphatase (hAP), and Tamm–Horsfall glycoprotein. These binding abilities were inhibited by 10
−6
M mannose-6-phosphate. Treatment of hAP with mild acid and phosphatase, which releases the
N-acetylglucosamine (GlcNAc) β1
→
phosphate
→
6 residue from the GPI-anchor glycan of hAP, abrogated the binding of TNF-α to hAP. Thus, TNF-α binds to the GlcNAcβ1
→
phosphate
→
6Man residue in GPI-anchor glycans. To investigate whether the carbohydrate-binding ability of TNF-α is related to its physiological functions, human lymphoma U937 cells were used. TNF-α stimulates U937 cell apoptosis in a dose-dependent manner and the presence of mannose-6-phosphate inhibited this. TNF-α-dependent tyrosine phosphorylation of several proteins in U937 cells was also diminished by mannose-6-phosphate. Phosphatidylinositol-specific phospholipase C-pretreatment also inhibited this tyrosine phosphorylation. These data suggest that TNF-α stimulates U937 cell apoptosis by forming a high-affinity nanomeric (TNF-α)
3–(TNFR)
3–(GPI-anchored glycan)
3 complex. The GPI-anchored glycoprotein involved remains to be identified.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15158680</pmid><doi>10.1016/j.abb.2004.02.028</doi><tpages>8</tpages></addata></record> |
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| ispartof | Archives of biochemistry and biophysics, 2004-06, Vol.426 (2), p.298-305 |
| issn | 0003-9861 1096-0384 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_71964854 |
| source | Elsevier |
| subjects | Apoptosis Apoptosis - drug effects Apoptosis - physiology Cell Cycle Proteins - metabolism Dose-Response Relationship, Drug GPI anchor GPI-Linked Proteins Humans Mannosephosphates - metabolism Mannosephosphates - pharmacology Membrane Proteins - metabolism Neoplasm Proteins - metabolism Protein Binding Signal Transduction - drug effects Signal Transduction - physiology TNF-α Tumor Necrosis Factor-alpha - metabolism Tumor Necrosis Factor-alpha - pharmacology U937 Cells β- N-acetylglucosaminyl phosphate diester |
| title | Recognition by TNF-α of the GPI-anchor glycan induces apoptosis of U937 cells |
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