Tumor Necrosis Factor Induces Phosphorylation of a 28-kDa mRNA Cap-Binding Protein in Human Cervical Carcinoma Cells
Tumor necrosis factor α (TNF-α ) stimulated the phosphorylation of a 28-kDa protein (p28) in the ME-180 line of human cervical carcinoma cells. The effect of TNF-α on the phosphorylation state of p28 was rapid (4-fold increase within 15 min) and persistent, remaining above the basal level for at lea...
Gespeichert in:
| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1989-11, Vol.86 (21), p.8417-8421 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 8421 |
|---|---|
| container_issue | 21 |
| container_start_page | 8417 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 86 |
| creator | Marino, Michael W. Pfeffer, Lawrence M. Guidon, Peter T. Donner, David B. |
| description | Tumor necrosis factor α (TNF-α ) stimulated the phosphorylation of a 28-kDa protein (p28) in the ME-180 line of human cervical carcinoma cells. The effect of TNF-α on the phosphorylation state of p28 was rapid (4-fold increase within 15 min) and persistent, remaining above the basal level for at least 2 hr. The specific binding of 125I-labeled TNF-α to cell-surface binding sites, the stimulation of p28 phosphorylation by TNF-α , and the inhibition of cell proliferation by TNF-α occurred with nearly identical dose-response relationships. Two-dimensional SDS/PAGE resolved p28 into two isoforms having pI values of 6.2 and 6.1. A phosphorylated cap-binding protein was substantially enriched from lysates of control or TNF-α -treated ME-180 cells by affinity chromatography with 7-methylguanosine 5′-triphosphate-Sepharose. The phosphoprotein recovered from this procedure was the substrate for TNF-α -promoted phosphorylation, p28. Thus, TNF-α stimulates the phosphorylation of this mRNA cap-binding protein, which may be involved in the transduction of TNF-α -receptor binding into cellular responses. |
| doi_str_mv | 10.1073/pnas.86.21.8417 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmed_primary_2813400</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>34882</jstor_id><sourcerecordid>34882</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4637-cfebbea2e40ae3e3907af7ed9de9c9d061dc42c7598a0feb42a6a7dfa9dc39943</originalsourceid><addsrcrecordid>eNqFkt1rFDEUxQdR6lp9FgQliOjTbPO1-Xjwoa7WFkotUp_D3UymmzqTbJOZYv97M-y62BeFQEjO756by0lVvSR4TrBkR5sAea7EnJK54kQ-qmYEa1ILrvHjaoYxlbXilD-tnuV8gzHWC4UPqgOqCOMYz6rhauxjQhfOpph9Ridgh3I-C81oXUaX65g365juOxh8DCi2CBBV9c_PgPrvF8doCZv6kw-ND9foMsXB-YDKOh17CGjp0p230BUqWR9iD-Wq6_Lz6kkLXXYvdvth9ePky9XytD7_9vVseXxeWy6YrG3rVisH1HEMjjmmsYRWukY3TlvdYEEay6mVC60AF5ZTECCbFnRjmdacHVYft76bcdW7xrowJOjMJvke0r2J4M1DJfi1uY53hmpFNSv1b7f1MQ_eZOsHZ9c2huDsYCQRC8EXBXq_a5Li7ejyYHqfbRkTgotjNlIzjDml_wXJggml6eR4tAWnTHJy7f7FBJspdTOlbpQwlJgp9VLx-u9B9_wu5qK_2-mQSx5tgmB93mNCKibENO-bHTb5_1Ef9PnwT8C0Y9cN7tdQyFdb8iaX_7RHGVeKst_FyNfN</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15368925</pqid></control><display><type>article</type><title>Tumor Necrosis Factor Induces Phosphorylation of a 28-kDa mRNA Cap-Binding Protein in Human Cervical Carcinoma Cells</title><source>Jstor Complete Legacy</source><source>MEDLINE</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Marino, Michael W. ; Pfeffer, Lawrence M. ; Guidon, Peter T. ; Donner, David B.</creator><creatorcontrib>Marino, Michael W. ; Pfeffer, Lawrence M. ; Guidon, Peter T. ; Donner, David B.</creatorcontrib><description>Tumor necrosis factor α (TNF-α ) stimulated the phosphorylation of a 28-kDa protein (p28) in the ME-180 line of human cervical carcinoma cells. The effect of TNF-α on the phosphorylation state of p28 was rapid (4-fold increase within 15 min) and persistent, remaining above the basal level for at least 2 hr. The specific binding of 125I-labeled TNF-α to cell-surface binding sites, the stimulation of p28 phosphorylation by TNF-α , and the inhibition of cell proliferation by TNF-α occurred with nearly identical dose-response relationships. Two-dimensional SDS/PAGE resolved p28 into two isoforms having pI values of 6.2 and 6.1. A phosphorylated cap-binding protein was substantially enriched from lysates of control or TNF-α -treated ME-180 cells by affinity chromatography with 7-methylguanosine 5′-triphosphate-Sepharose. The phosphoprotein recovered from this procedure was the substrate for TNF-α -promoted phosphorylation, p28. Thus, TNF-α stimulates the phosphorylation of this mRNA cap-binding protein, which may be involved in the transduction of TNF-α -receptor binding into cellular responses.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.86.21.8417</identifier><identifier>PMID: 2813400</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>550201 - Biochemistry- Tracer Techniques ; ANIMAL CELLS ; ANIMALS ; AUTORADIOGRAPHY ; BASIC BIOLOGICAL SCIENCES ; BETA DECAY RADIOISOTOPES ; BETA-MINUS DECAY RADIOISOTOPES ; Biological and medical sciences ; CARCINOMAS ; Carrier Proteins - metabolism ; Cell Division - drug effects ; Cell growth ; Cell Line ; Cell lines ; Cell physiology ; CELL PROLIFERATION ; Cells ; CHEMICAL REACTIONS ; Chromatography ; CONNECTIVE TISSUE CELLS ; DAYS LIVING RADIOISOTOPES ; DISEASES ; ELECTRON CAPTURE RADIOISOTOPES ; ELECTROPHORESIS ; Electrophoresis, Gel, Two-Dimensional ; Electrophoresis, Polyacrylamide Gel ; Elution ; Female ; Fundamental and applied biological sciences. Psychology ; Gels ; GROWTH FACTORS ; HeLa cells ; Humans ; INTERMEDIATE MASS NUCLEI ; IODINE 125 ; IODINE ISOTOPES ; ISOTOPES ; Kinetics ; LIGHT NUCLEI ; MACROPHAGES ; MAMMALS ; MAN ; ME-180 cells ; MEMBRANE PROTEINS ; MESSENGER-RNA ; MITOGENS ; Molecular and cellular biology ; Molecular Weight ; mRNA cap-binding protein ; NECROSIS ; NEOPLASMS ; NUCLEI ; NUCLEIC ACIDS ; ODD-EVEN NUCLEI ; ODD-ODD NUCLEI ; ORGANIC COMPOUNDS ; PATHOLOGICAL CHANGES ; PHAGOCYTES ; Phosphoproteins ; Phosphoproteins - biosynthesis ; Phosphoproteins - isolation & purification ; PHOSPHORUS 32 ; PHOSPHORUS ISOTOPES ; PHOSPHORYLATION ; PRIMATES ; PROTEINS ; RADIOISOTOPES ; RECEPTORS ; Responses to growth factors, tumor promotors, other factors ; RNA ; RNA Cap-Binding Proteins ; RNA Caps - metabolism ; SOMATIC CELLS ; TUMOR CELLS ; Tumor Cells, Cultured - cytology ; Tumor Cells, Cultured - drug effects ; Tumor Cells, Cultured - metabolism ; Tumor Necrosis Factor-alpha - pharmacology ; Uterine Cervical Neoplasms ; VERTEBRATES</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1989-11, Vol.86 (21), p.8417-8421</ispartof><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4637-cfebbea2e40ae3e3907af7ed9de9c9d061dc42c7598a0feb42a6a7dfa9dc39943</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/86/21.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/34882$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/34882$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53769,53771,57995,58228</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6783663$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2813400$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/7165645$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Marino, Michael W.</creatorcontrib><creatorcontrib>Pfeffer, Lawrence M.</creatorcontrib><creatorcontrib>Guidon, Peter T.</creatorcontrib><creatorcontrib>Donner, David B.</creatorcontrib><title>Tumor Necrosis Factor Induces Phosphorylation of a 28-kDa mRNA Cap-Binding Protein in Human Cervical Carcinoma Cells</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Tumor necrosis factor α (TNF-α ) stimulated the phosphorylation of a 28-kDa protein (p28) in the ME-180 line of human cervical carcinoma cells. The effect of TNF-α on the phosphorylation state of p28 was rapid (4-fold increase within 15 min) and persistent, remaining above the basal level for at least 2 hr. The specific binding of 125I-labeled TNF-α to cell-surface binding sites, the stimulation of p28 phosphorylation by TNF-α , and the inhibition of cell proliferation by TNF-α occurred with nearly identical dose-response relationships. Two-dimensional SDS/PAGE resolved p28 into two isoforms having pI values of 6.2 and 6.1. A phosphorylated cap-binding protein was substantially enriched from lysates of control or TNF-α -treated ME-180 cells by affinity chromatography with 7-methylguanosine 5′-triphosphate-Sepharose. The phosphoprotein recovered from this procedure was the substrate for TNF-α -promoted phosphorylation, p28. Thus, TNF-α stimulates the phosphorylation of this mRNA cap-binding protein, which may be involved in the transduction of TNF-α -receptor binding into cellular responses.</description><subject>550201 - Biochemistry- Tracer Techniques</subject><subject>ANIMAL CELLS</subject><subject>ANIMALS</subject><subject>AUTORADIOGRAPHY</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>BETA DECAY RADIOISOTOPES</subject><subject>BETA-MINUS DECAY RADIOISOTOPES</subject><subject>Biological and medical sciences</subject><subject>CARCINOMAS</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Division - drug effects</subject><subject>Cell growth</subject><subject>Cell Line</subject><subject>Cell lines</subject><subject>Cell physiology</subject><subject>CELL PROLIFERATION</subject><subject>Cells</subject><subject>CHEMICAL REACTIONS</subject><subject>Chromatography</subject><subject>CONNECTIVE TISSUE CELLS</subject><subject>DAYS LIVING RADIOISOTOPES</subject><subject>DISEASES</subject><subject>ELECTRON CAPTURE RADIOISOTOPES</subject><subject>ELECTROPHORESIS</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Elution</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>GROWTH FACTORS</subject><subject>HeLa cells</subject><subject>Humans</subject><subject>INTERMEDIATE MASS NUCLEI</subject><subject>IODINE 125</subject><subject>IODINE ISOTOPES</subject><subject>ISOTOPES</subject><subject>Kinetics</subject><subject>LIGHT NUCLEI</subject><subject>MACROPHAGES</subject><subject>MAMMALS</subject><subject>MAN</subject><subject>ME-180 cells</subject><subject>MEMBRANE PROTEINS</subject><subject>MESSENGER-RNA</subject><subject>MITOGENS</subject><subject>Molecular and cellular biology</subject><subject>Molecular Weight</subject><subject>mRNA cap-binding protein</subject><subject>NECROSIS</subject><subject>NEOPLASMS</subject><subject>NUCLEI</subject><subject>NUCLEIC ACIDS</subject><subject>ODD-EVEN NUCLEI</subject><subject>ODD-ODD NUCLEI</subject><subject>ORGANIC COMPOUNDS</subject><subject>PATHOLOGICAL CHANGES</subject><subject>PHAGOCYTES</subject><subject>Phosphoproteins</subject><subject>Phosphoproteins - biosynthesis</subject><subject>Phosphoproteins - isolation & purification</subject><subject>PHOSPHORUS 32</subject><subject>PHOSPHORUS ISOTOPES</subject><subject>PHOSPHORYLATION</subject><subject>PRIMATES</subject><subject>PROTEINS</subject><subject>RADIOISOTOPES</subject><subject>RECEPTORS</subject><subject>Responses to growth factors, tumor promotors, other factors</subject><subject>RNA</subject><subject>RNA Cap-Binding Proteins</subject><subject>RNA Caps - metabolism</subject><subject>SOMATIC CELLS</subject><subject>TUMOR CELLS</subject><subject>Tumor Cells, Cultured - cytology</subject><subject>Tumor Cells, Cultured - drug effects</subject><subject>Tumor Cells, Cultured - metabolism</subject><subject>Tumor Necrosis Factor-alpha - pharmacology</subject><subject>Uterine Cervical Neoplasms</subject><subject>VERTEBRATES</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkt1rFDEUxQdR6lp9FgQliOjTbPO1-Xjwoa7WFkotUp_D3UymmzqTbJOZYv97M-y62BeFQEjO756by0lVvSR4TrBkR5sAea7EnJK54kQ-qmYEa1ILrvHjaoYxlbXilD-tnuV8gzHWC4UPqgOqCOMYz6rhauxjQhfOpph9Ridgh3I-C81oXUaX65g365juOxh8DCi2CBBV9c_PgPrvF8doCZv6kw-ND9foMsXB-YDKOh17CGjp0p230BUqWR9iD-Wq6_Lz6kkLXXYvdvth9ePky9XytD7_9vVseXxeWy6YrG3rVisH1HEMjjmmsYRWukY3TlvdYEEay6mVC60AF5ZTECCbFnRjmdacHVYft76bcdW7xrowJOjMJvke0r2J4M1DJfi1uY53hmpFNSv1b7f1MQ_eZOsHZ9c2huDsYCQRC8EXBXq_a5Li7ejyYHqfbRkTgotjNlIzjDml_wXJggml6eR4tAWnTHJy7f7FBJspdTOlbpQwlJgp9VLx-u9B9_wu5qK_2-mQSx5tgmB93mNCKibENO-bHTb5_1Ef9PnwT8C0Y9cN7tdQyFdb8iaX_7RHGVeKst_FyNfN</recordid><startdate>19891101</startdate><enddate>19891101</enddate><creator>Marino, Michael W.</creator><creator>Pfeffer, Lawrence M.</creator><creator>Guidon, Peter T.</creator><creator>Donner, David B.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>19891101</creationdate><title>Tumor Necrosis Factor Induces Phosphorylation of a 28-kDa mRNA Cap-Binding Protein in Human Cervical Carcinoma Cells</title><author>Marino, Michael W. ; Pfeffer, Lawrence M. ; Guidon, Peter T. ; Donner, David B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4637-cfebbea2e40ae3e3907af7ed9de9c9d061dc42c7598a0feb42a6a7dfa9dc39943</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>550201 - Biochemistry- Tracer Techniques</topic><topic>ANIMAL CELLS</topic><topic>ANIMALS</topic><topic>AUTORADIOGRAPHY</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>BETA DECAY RADIOISOTOPES</topic><topic>BETA-MINUS DECAY RADIOISOTOPES</topic><topic>Biological and medical sciences</topic><topic>CARCINOMAS</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Division - drug effects</topic><topic>Cell growth</topic><topic>Cell Line</topic><topic>Cell lines</topic><topic>Cell physiology</topic><topic>CELL PROLIFERATION</topic><topic>Cells</topic><topic>CHEMICAL REACTIONS</topic><topic>Chromatography</topic><topic>CONNECTIVE TISSUE CELLS</topic><topic>DAYS LIVING RADIOISOTOPES</topic><topic>DISEASES</topic><topic>ELECTRON CAPTURE RADIOISOTOPES</topic><topic>ELECTROPHORESIS</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Elution</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>GROWTH FACTORS</topic><topic>HeLa cells</topic><topic>Humans</topic><topic>INTERMEDIATE MASS NUCLEI</topic><topic>IODINE 125</topic><topic>IODINE ISOTOPES</topic><topic>ISOTOPES</topic><topic>Kinetics</topic><topic>LIGHT NUCLEI</topic><topic>MACROPHAGES</topic><topic>MAMMALS</topic><topic>MAN</topic><topic>ME-180 cells</topic><topic>MEMBRANE PROTEINS</topic><topic>MESSENGER-RNA</topic><topic>MITOGENS</topic><topic>Molecular and cellular biology</topic><topic>Molecular Weight</topic><topic>mRNA cap-binding protein</topic><topic>NECROSIS</topic><topic>NEOPLASMS</topic><topic>NUCLEI</topic><topic>NUCLEIC ACIDS</topic><topic>ODD-EVEN NUCLEI</topic><topic>ODD-ODD NUCLEI</topic><topic>ORGANIC COMPOUNDS</topic><topic>PATHOLOGICAL CHANGES</topic><topic>PHAGOCYTES</topic><topic>Phosphoproteins</topic><topic>Phosphoproteins - biosynthesis</topic><topic>Phosphoproteins - isolation & purification</topic><topic>PHOSPHORUS 32</topic><topic>PHOSPHORUS ISOTOPES</topic><topic>PHOSPHORYLATION</topic><topic>PRIMATES</topic><topic>PROTEINS</topic><topic>RADIOISOTOPES</topic><topic>RECEPTORS</topic><topic>Responses to growth factors, tumor promotors, other factors</topic><topic>RNA</topic><topic>RNA Cap-Binding Proteins</topic><topic>RNA Caps - metabolism</topic><topic>SOMATIC CELLS</topic><topic>TUMOR CELLS</topic><topic>Tumor Cells, Cultured - cytology</topic><topic>Tumor Cells, Cultured - drug effects</topic><topic>Tumor Cells, Cultured - metabolism</topic><topic>Tumor Necrosis Factor-alpha - pharmacology</topic><topic>Uterine Cervical Neoplasms</topic><topic>VERTEBRATES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Marino, Michael W.</creatorcontrib><creatorcontrib>Pfeffer, Lawrence M.</creatorcontrib><creatorcontrib>Guidon, Peter T.</creatorcontrib><creatorcontrib>Donner, David B.</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Marino, Michael W.</au><au>Pfeffer, Lawrence M.</au><au>Guidon, Peter T.</au><au>Donner, David B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tumor Necrosis Factor Induces Phosphorylation of a 28-kDa mRNA Cap-Binding Protein in Human Cervical Carcinoma Cells</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1989-11-01</date><risdate>1989</risdate><volume>86</volume><issue>21</issue><spage>8417</spage><epage>8421</epage><pages>8417-8421</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>Tumor necrosis factor α (TNF-α ) stimulated the phosphorylation of a 28-kDa protein (p28) in the ME-180 line of human cervical carcinoma cells. The effect of TNF-α on the phosphorylation state of p28 was rapid (4-fold increase within 15 min) and persistent, remaining above the basal level for at least 2 hr. The specific binding of 125I-labeled TNF-α to cell-surface binding sites, the stimulation of p28 phosphorylation by TNF-α , and the inhibition of cell proliferation by TNF-α occurred with nearly identical dose-response relationships. Two-dimensional SDS/PAGE resolved p28 into two isoforms having pI values of 6.2 and 6.1. A phosphorylated cap-binding protein was substantially enriched from lysates of control or TNF-α -treated ME-180 cells by affinity chromatography with 7-methylguanosine 5′-triphosphate-Sepharose. The phosphoprotein recovered from this procedure was the substrate for TNF-α -promoted phosphorylation, p28. Thus, TNF-α stimulates the phosphorylation of this mRNA cap-binding protein, which may be involved in the transduction of TNF-α -receptor binding into cellular responses.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>2813400</pmid><doi>10.1073/pnas.86.21.8417</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1989-11, Vol.86 (21), p.8417-8421 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pubmed_primary_2813400 |
| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | 550201 - Biochemistry- Tracer Techniques ANIMAL CELLS ANIMALS AUTORADIOGRAPHY BASIC BIOLOGICAL SCIENCES BETA DECAY RADIOISOTOPES BETA-MINUS DECAY RADIOISOTOPES Biological and medical sciences CARCINOMAS Carrier Proteins - metabolism Cell Division - drug effects Cell growth Cell Line Cell lines Cell physiology CELL PROLIFERATION Cells CHEMICAL REACTIONS Chromatography CONNECTIVE TISSUE CELLS DAYS LIVING RADIOISOTOPES DISEASES ELECTRON CAPTURE RADIOISOTOPES ELECTROPHORESIS Electrophoresis, Gel, Two-Dimensional Electrophoresis, Polyacrylamide Gel Elution Female Fundamental and applied biological sciences. Psychology Gels GROWTH FACTORS HeLa cells Humans INTERMEDIATE MASS NUCLEI IODINE 125 IODINE ISOTOPES ISOTOPES Kinetics LIGHT NUCLEI MACROPHAGES MAMMALS MAN ME-180 cells MEMBRANE PROTEINS MESSENGER-RNA MITOGENS Molecular and cellular biology Molecular Weight mRNA cap-binding protein NECROSIS NEOPLASMS NUCLEI NUCLEIC ACIDS ODD-EVEN NUCLEI ODD-ODD NUCLEI ORGANIC COMPOUNDS PATHOLOGICAL CHANGES PHAGOCYTES Phosphoproteins Phosphoproteins - biosynthesis Phosphoproteins - isolation & purification PHOSPHORUS 32 PHOSPHORUS ISOTOPES PHOSPHORYLATION PRIMATES PROTEINS RADIOISOTOPES RECEPTORS Responses to growth factors, tumor promotors, other factors RNA RNA Cap-Binding Proteins RNA Caps - metabolism SOMATIC CELLS TUMOR CELLS Tumor Cells, Cultured - cytology Tumor Cells, Cultured - drug effects Tumor Cells, Cultured - metabolism Tumor Necrosis Factor-alpha - pharmacology Uterine Cervical Neoplasms VERTEBRATES |
| title | Tumor Necrosis Factor Induces Phosphorylation of a 28-kDa mRNA Cap-Binding Protein in Human Cervical Carcinoma Cells |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-28T02%3A11%3A10IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Tumor%20Necrosis%20Factor%20Induces%20Phosphorylation%20of%20a%2028-kDa%20mRNA%20Cap-Binding%20Protein%20in%20Human%20Cervical%20Carcinoma%20Cells&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Marino,%20Michael%20W.&rft.date=1989-11-01&rft.volume=86&rft.issue=21&rft.spage=8417&rft.epage=8421&rft.pages=8417-8421&rft.issn=0027-8424&rft.eissn=1091-6490&rft.coden=PNASA6&rft_id=info:doi/10.1073/pnas.86.21.8417&rft_dat=%3Cjstor_pubme%3E34882%3C/jstor_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=15368925&rft_id=info:pmid/2813400&rft_jstor_id=34882&rfr_iscdi=true |