Insulin and interleukin-1 differentially regulate pp63, an acute phase phosphoprotein in hepatoma cell line
We have reported previously that the phosphoprotein pp63, an acute phase protein, which has been recently identified as the rat fetuin, was capable of blocking the mitogenic effect of insulin on the rat Fao hepatoma cell line, without affecting metabolic effects of the hormone. Only the phosphorylat...
Gespeichert in:
Veröffentlicht in: | The Journal of biological chemistry 1994-06, Vol.269 (22), p.15925-15930 |
---|---|
Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 15930 |
---|---|
container_issue | 22 |
container_start_page | 15925 |
container_title | The Journal of biological chemistry |
container_volume | 269 |
creator | Akhoundi, C Amiot, M Auberger, P Le Cam, A Rossi, B |
description | We have reported previously that the phosphoprotein pp63, an acute phase protein, which has been recently identified as the
rat fetuin, was capable of blocking the mitogenic effect of insulin on the rat Fao hepatoma cell line, without affecting metabolic
effects of the hormone. Only the phosphorylated form of the protein has been shown to exhibit both anti-tyrosine kinase and
growth inhibitory properties. In this study, we used the FTO-2B rat hepatoma cell line to analyze the mechanisms involved
in the control of synthesis and/or phosphorylation of pp63. For this purpose, we investigated the action of effectors known
to modulate hepatic functions, such as cytokines (interleukin (IL)-1 beta and IL-6), which regulate the production of acute
phase proteins, and insulin, which elicits profound effects on hepatocyte metabolism. Here, we demonstrate that IL-1 beta
diminished markedly the pp63 production by affecting its mRNA transcription and that the cytokine was able to modify the N-glycosylation
process of the protein. In contrast, insulin did not affect the biosynthesis of pp63 but dramatically decreased its extent
of phosphorylation. |
doi_str_mv | 10.1016/S0021-9258(17)40769-1 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_76503970</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>76503970</sourcerecordid><originalsourceid>FETCH-LOGICAL-c411t-4074258215a73d4b585ccf3f11f25695a387c751ee7b46918b13d9e8a0d8e22e3</originalsourceid><addsrcrecordid>eNqFUctKxTAQDaLo9fEJQhciClYzSdM0S7n4AsGFCu5C2k5ttC-TFvHvTe-9uDXkQZgzZ87MIeQY6CVQSK-eKWUQKyayM5DnCZWpimGLLIBmPOYC3rbJ4g-yR_a9_6BhJQp2ya4UIGgqFuTzofNTY7vIdGVkuxFdg9On7WKISltV6LAbrWman8jh-9SYEaNhSPlFwEemmOZvbfx89z6cwfUjBrawaxzM2LcmKrBpolACD8lOZRqPR5v3gLze3rws7-PHp7uH5fVjXCQAYxxaSYJkBsJIXia5yERRVLwCqJhIlTA8k0VoAFHmSaogy4GXCjNDywwZQ35ATte8Qc3XhH7UrfWzCtNhP3ktU0G5kvRfIKRCSaZkAIo1sHC99w4rPTjbGvejgerZDb1yQ8-j1iD1yg0NIe94U2DKWyz_sjbjD_GTdby27_W3dahz2xc1tpqFfMY0iEDJfwEvyJE1</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16597297</pqid></control><display><type>article</type><title>Insulin and interleukin-1 differentially regulate pp63, an acute phase phosphoprotein in hepatoma cell line</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Akhoundi, C ; Amiot, M ; Auberger, P ; Le Cam, A ; Rossi, B</creator><creatorcontrib>Akhoundi, C ; Amiot, M ; Auberger, P ; Le Cam, A ; Rossi, B</creatorcontrib><description>We have reported previously that the phosphoprotein pp63, an acute phase protein, which has been recently identified as the
rat fetuin, was capable of blocking the mitogenic effect of insulin on the rat Fao hepatoma cell line, without affecting metabolic
effects of the hormone. Only the phosphorylated form of the protein has been shown to exhibit both anti-tyrosine kinase and
growth inhibitory properties. In this study, we used the FTO-2B rat hepatoma cell line to analyze the mechanisms involved
in the control of synthesis and/or phosphorylation of pp63. For this purpose, we investigated the action of effectors known
to modulate hepatic functions, such as cytokines (interleukin (IL)-1 beta and IL-6), which regulate the production of acute
phase proteins, and insulin, which elicits profound effects on hepatocyte metabolism. Here, we demonstrate that IL-1 beta
diminished markedly the pp63 production by affecting its mRNA transcription and that the cytokine was able to modify the N-glycosylation
process of the protein. In contrast, insulin did not affect the biosynthesis of pp63 but dramatically decreased its extent
of phosphorylation.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)40769-1</identifier><identifier>PMID: 7515065</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Acute-Phase Proteins - biosynthesis ; Acute-Phase Proteins - isolation & purification ; alpha-Fetoproteins - biosynthesis ; alpha-Fetoproteins - isolation & purification ; Animals ; Cell Line ; Cell Nucleus - metabolism ; Cells, Cultured ; Dexamethasone - pharmacology ; Electrophoresis, Polyacrylamide Gel ; Gene Expression Regulation, Neoplastic ; Glycosylation ; Humans ; Insulin - pharmacology ; Interleukin-1 - pharmacology ; Interleukin-6 - pharmacology ; Kinetics ; Liver - drug effects ; Liver - metabolism ; Liver Neoplasms, Experimental ; Male ; Phosphoproteins - biosynthesis ; Phosphoproteins - isolation & purification ; Phosphorylation ; Protein Processing, Post-Translational ; Rats ; Rats, Wistar ; Recombinant Proteins - pharmacology ; RNA, Messenger - biosynthesis ; RNA, Messenger - metabolism ; Transcription, Genetic ; Tumor Cells, Cultured</subject><ispartof>The Journal of biological chemistry, 1994-06, Vol.269 (22), p.15925-15930</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c411t-4074258215a73d4b585ccf3f11f25695a387c751ee7b46918b13d9e8a0d8e22e3</citedby><cites>FETCH-LOGICAL-c411t-4074258215a73d4b585ccf3f11f25695a387c751ee7b46918b13d9e8a0d8e22e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7515065$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Akhoundi, C</creatorcontrib><creatorcontrib>Amiot, M</creatorcontrib><creatorcontrib>Auberger, P</creatorcontrib><creatorcontrib>Le Cam, A</creatorcontrib><creatorcontrib>Rossi, B</creatorcontrib><title>Insulin and interleukin-1 differentially regulate pp63, an acute phase phosphoprotein in hepatoma cell line</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We have reported previously that the phosphoprotein pp63, an acute phase protein, which has been recently identified as the
rat fetuin, was capable of blocking the mitogenic effect of insulin on the rat Fao hepatoma cell line, without affecting metabolic
effects of the hormone. Only the phosphorylated form of the protein has been shown to exhibit both anti-tyrosine kinase and
growth inhibitory properties. In this study, we used the FTO-2B rat hepatoma cell line to analyze the mechanisms involved
in the control of synthesis and/or phosphorylation of pp63. For this purpose, we investigated the action of effectors known
to modulate hepatic functions, such as cytokines (interleukin (IL)-1 beta and IL-6), which regulate the production of acute
phase proteins, and insulin, which elicits profound effects on hepatocyte metabolism. Here, we demonstrate that IL-1 beta
diminished markedly the pp63 production by affecting its mRNA transcription and that the cytokine was able to modify the N-glycosylation
process of the protein. In contrast, insulin did not affect the biosynthesis of pp63 but dramatically decreased its extent
of phosphorylation.</description><subject>Acute-Phase Proteins - biosynthesis</subject><subject>Acute-Phase Proteins - isolation & purification</subject><subject>alpha-Fetoproteins - biosynthesis</subject><subject>alpha-Fetoproteins - isolation & purification</subject><subject>Animals</subject><subject>Cell Line</subject><subject>Cell Nucleus - metabolism</subject><subject>Cells, Cultured</subject><subject>Dexamethasone - pharmacology</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Gene Expression Regulation, Neoplastic</subject><subject>Glycosylation</subject><subject>Humans</subject><subject>Insulin - pharmacology</subject><subject>Interleukin-1 - pharmacology</subject><subject>Interleukin-6 - pharmacology</subject><subject>Kinetics</subject><subject>Liver - drug effects</subject><subject>Liver - metabolism</subject><subject>Liver Neoplasms, Experimental</subject><subject>Male</subject><subject>Phosphoproteins - biosynthesis</subject><subject>Phosphoproteins - isolation & purification</subject><subject>Phosphorylation</subject><subject>Protein Processing, Post-Translational</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Recombinant Proteins - pharmacology</subject><subject>RNA, Messenger - biosynthesis</subject><subject>RNA, Messenger - metabolism</subject><subject>Transcription, Genetic</subject><subject>Tumor Cells, Cultured</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUctKxTAQDaLo9fEJQhciClYzSdM0S7n4AsGFCu5C2k5ttC-TFvHvTe-9uDXkQZgzZ87MIeQY6CVQSK-eKWUQKyayM5DnCZWpimGLLIBmPOYC3rbJ4g-yR_a9_6BhJQp2ya4UIGgqFuTzofNTY7vIdGVkuxFdg9On7WKISltV6LAbrWman8jh-9SYEaNhSPlFwEemmOZvbfx89z6cwfUjBrawaxzM2LcmKrBpolACD8lOZRqPR5v3gLze3rws7-PHp7uH5fVjXCQAYxxaSYJkBsJIXia5yERRVLwCqJhIlTA8k0VoAFHmSaogy4GXCjNDywwZQ35ATte8Qc3XhH7UrfWzCtNhP3ktU0G5kvRfIKRCSaZkAIo1sHC99w4rPTjbGvejgerZDb1yQ8-j1iD1yg0NIe94U2DKWyz_sjbjD_GTdby27_W3dahz2xc1tpqFfMY0iEDJfwEvyJE1</recordid><startdate>19940603</startdate><enddate>19940603</enddate><creator>Akhoundi, C</creator><creator>Amiot, M</creator><creator>Auberger, P</creator><creator>Le Cam, A</creator><creator>Rossi, B</creator><general>American Society for Biochemistry and Molecular Biology</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>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19940603</creationdate><title>Insulin and interleukin-1 differentially regulate pp63, an acute phase phosphoprotein in hepatoma cell line</title><author>Akhoundi, C ; Amiot, M ; Auberger, P ; Le Cam, A ; Rossi, B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c411t-4074258215a73d4b585ccf3f11f25695a387c751ee7b46918b13d9e8a0d8e22e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Acute-Phase Proteins - biosynthesis</topic><topic>Acute-Phase Proteins - isolation & purification</topic><topic>alpha-Fetoproteins - biosynthesis</topic><topic>alpha-Fetoproteins - isolation & purification</topic><topic>Animals</topic><topic>Cell Line</topic><topic>Cell Nucleus - metabolism</topic><topic>Cells, Cultured</topic><topic>Dexamethasone - pharmacology</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Gene Expression Regulation, Neoplastic</topic><topic>Glycosylation</topic><topic>Humans</topic><topic>Insulin - pharmacology</topic><topic>Interleukin-1 - pharmacology</topic><topic>Interleukin-6 - pharmacology</topic><topic>Kinetics</topic><topic>Liver - drug effects</topic><topic>Liver - metabolism</topic><topic>Liver Neoplasms, Experimental</topic><topic>Male</topic><topic>Phosphoproteins - biosynthesis</topic><topic>Phosphoproteins - isolation & purification</topic><topic>Phosphorylation</topic><topic>Protein Processing, Post-Translational</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Recombinant Proteins - pharmacology</topic><topic>RNA, Messenger - biosynthesis</topic><topic>RNA, Messenger - metabolism</topic><topic>Transcription, Genetic</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Akhoundi, C</creatorcontrib><creatorcontrib>Amiot, M</creatorcontrib><creatorcontrib>Auberger, P</creatorcontrib><creatorcontrib>Le Cam, A</creatorcontrib><creatorcontrib>Rossi, B</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Akhoundi, C</au><au>Amiot, M</au><au>Auberger, P</au><au>Le Cam, A</au><au>Rossi, B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Insulin and interleukin-1 differentially regulate pp63, an acute phase phosphoprotein in hepatoma cell line</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-06-03</date><risdate>1994</risdate><volume>269</volume><issue>22</issue><spage>15925</spage><epage>15930</epage><pages>15925-15930</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>We have reported previously that the phosphoprotein pp63, an acute phase protein, which has been recently identified as the
rat fetuin, was capable of blocking the mitogenic effect of insulin on the rat Fao hepatoma cell line, without affecting metabolic
effects of the hormone. Only the phosphorylated form of the protein has been shown to exhibit both anti-tyrosine kinase and
growth inhibitory properties. In this study, we used the FTO-2B rat hepatoma cell line to analyze the mechanisms involved
in the control of synthesis and/or phosphorylation of pp63. For this purpose, we investigated the action of effectors known
to modulate hepatic functions, such as cytokines (interleukin (IL)-1 beta and IL-6), which regulate the production of acute
phase proteins, and insulin, which elicits profound effects on hepatocyte metabolism. Here, we demonstrate that IL-1 beta
diminished markedly the pp63 production by affecting its mRNA transcription and that the cytokine was able to modify the N-glycosylation
process of the protein. In contrast, insulin did not affect the biosynthesis of pp63 but dramatically decreased its extent
of phosphorylation.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>7515065</pmid><doi>10.1016/S0021-9258(17)40769-1</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0021-9258 |
ispartof | The Journal of biological chemistry, 1994-06, Vol.269 (22), p.15925-15930 |
issn | 0021-9258 1083-351X |
language | eng |
recordid | cdi_proquest_miscellaneous_76503970 |
source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
subjects | Acute-Phase Proteins - biosynthesis Acute-Phase Proteins - isolation & purification alpha-Fetoproteins - biosynthesis alpha-Fetoproteins - isolation & purification Animals Cell Line Cell Nucleus - metabolism Cells, Cultured Dexamethasone - pharmacology Electrophoresis, Polyacrylamide Gel Gene Expression Regulation, Neoplastic Glycosylation Humans Insulin - pharmacology Interleukin-1 - pharmacology Interleukin-6 - pharmacology Kinetics Liver - drug effects Liver - metabolism Liver Neoplasms, Experimental Male Phosphoproteins - biosynthesis Phosphoproteins - isolation & purification Phosphorylation Protein Processing, Post-Translational Rats Rats, Wistar Recombinant Proteins - pharmacology RNA, Messenger - biosynthesis RNA, Messenger - metabolism Transcription, Genetic Tumor Cells, Cultured |
title | Insulin and interleukin-1 differentially regulate pp63, an acute phase phosphoprotein in hepatoma cell line |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-18T04%3A50%3A13IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Insulin%20and%20interleukin-1%20differentially%20regulate%20pp63,%20an%20acute%20phase%20phosphoprotein%20in%20hepatoma%20cell%20line&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Akhoundi,%20C&rft.date=1994-06-03&rft.volume=269&rft.issue=22&rft.spage=15925&rft.epage=15930&rft.pages=15925-15930&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1016/S0021-9258(17)40769-1&rft_dat=%3Cproquest_cross%3E76503970%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=16597297&rft_id=info:pmid/7515065&rfr_iscdi=true |