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Evidence for the binding of a biologically active interleukin-2 to human alpha 2-macroglobulin
Human alpha 2-macroglobulin (alpha 2M), which irreversibly entraps proteinases through a drastic conformational change, has also been reported to bind various cytokines. The meaning of cytokine binding to native and/or transformed alpha 2M molecules is, however, not understood. In an attempt to eluc...
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Published in: | The Journal of biological chemistry 1995-04, Vol.270 (15), p.8381-8384 |
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creator | Legrès, L G Pochon, F Barray, M Gay, F Chouaib, S Delain, E |
description | Human alpha 2-macroglobulin (alpha 2M), which irreversibly entraps proteinases through a drastic conformational change, has also been reported to bind various cytokines. The meaning of cytokine binding to native and/or transformed alpha 2M molecules is, however, not understood. In an attempt to elucidate this question, we have studied the interaction of radioiodinated recombinant human interleukin-2 (125I-rhIL-2) with native and chymotrypsin (alpha 2M-C)- or methylamine-transformed (alpha 2M-MA) alpha 2M. Our results show that native and alpha 2M-MA are able to bind 125I-rhIL-2, with binding occurring only with the latter in a covalent manner, whereas the labeled cytokine is proteolyzed when incubated with alpha 2M-entrapped chymotrypsin. The degradation of uncomplexed 125I-rhIL-2 has also been observed in the presence of trypsin, whereas 125I-rhIL-2 bound to alpha 2M-MA is protected. Moreover, the proliferative activity of this cytokine on responsive cells is still maintained either with native alpha 2M- or alpha 2M-MA-complexed rhIL-2 in comparison with that observed with the cytokine alone. Our results, which lead us to consider alpha 2M molecules as IL-2-binding proteins, emphasize the possible role of these molecules as immune response regulators. |
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The meaning of cytokine binding to native and/or transformed alpha 2M molecules is, however, not understood. In an attempt to elucidate this question, we have studied the interaction of radioiodinated recombinant human interleukin-2 (125I-rhIL-2) with native and chymotrypsin (alpha 2M-C)- or methylamine-transformed (alpha 2M-MA) alpha 2M. Our results show that native and alpha 2M-MA are able to bind 125I-rhIL-2, with binding occurring only with the latter in a covalent manner, whereas the labeled cytokine is proteolyzed when incubated with alpha 2M-entrapped chymotrypsin. The degradation of uncomplexed 125I-rhIL-2 has also been observed in the presence of trypsin, whereas 125I-rhIL-2 bound to alpha 2M-MA is protected. Moreover, the proliferative activity of this cytokine on responsive cells is still maintained either with native alpha 2M- or alpha 2M-MA-complexed rhIL-2 in comparison with that observed with the cytokine alone. Our results, which lead us to consider alpha 2M molecules as IL-2-binding proteins, emphasize the possible role of these molecules as immune response regulators.</description><identifier>ISSN: 0021-9258</identifier><identifier>PMID: 7536736</identifier><language>eng</language><publisher>United States</publisher><subject>alpha-Macroglobulins - chemistry ; alpha-Macroglobulins - metabolism ; Cells, Cultured ; Electrophoresis, Polyacrylamide Gel ; Humans ; Hydrolysis ; Interleukin-2 - metabolism ; Protein Binding ; Protein Conformation ; Recombinant Proteins - metabolism</subject><ispartof>The Journal of biological chemistry, 1995-04, Vol.270 (15), p.8381-8384</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7536736$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Legrès, L G</creatorcontrib><creatorcontrib>Pochon, F</creatorcontrib><creatorcontrib>Barray, M</creatorcontrib><creatorcontrib>Gay, F</creatorcontrib><creatorcontrib>Chouaib, S</creatorcontrib><creatorcontrib>Delain, E</creatorcontrib><title>Evidence for the binding of a biologically active interleukin-2 to human alpha 2-macroglobulin</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Human alpha 2-macroglobulin (alpha 2M), which irreversibly entraps proteinases through a drastic conformational change, has also been reported to bind various cytokines. The meaning of cytokine binding to native and/or transformed alpha 2M molecules is, however, not understood. In an attempt to elucidate this question, we have studied the interaction of radioiodinated recombinant human interleukin-2 (125I-rhIL-2) with native and chymotrypsin (alpha 2M-C)- or methylamine-transformed (alpha 2M-MA) alpha 2M. Our results show that native and alpha 2M-MA are able to bind 125I-rhIL-2, with binding occurring only with the latter in a covalent manner, whereas the labeled cytokine is proteolyzed when incubated with alpha 2M-entrapped chymotrypsin. The degradation of uncomplexed 125I-rhIL-2 has also been observed in the presence of trypsin, whereas 125I-rhIL-2 bound to alpha 2M-MA is protected. Moreover, the proliferative activity of this cytokine on responsive cells is still maintained either with native alpha 2M- or alpha 2M-MA-complexed rhIL-2 in comparison with that observed with the cytokine alone. Our results, which lead us to consider alpha 2M molecules as IL-2-binding proteins, emphasize the possible role of these molecules as immune response regulators.</description><subject>alpha-Macroglobulins - chemistry</subject><subject>alpha-Macroglobulins - metabolism</subject><subject>Cells, Cultured</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Humans</subject><subject>Hydrolysis</subject><subject>Interleukin-2 - metabolism</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Recombinant Proteins - metabolism</subject><issn>0021-9258</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><recordid>eNotkMtqwzAURLVoSdO0n1DQqjuDJFuStSwhfUCgm6xr5KtrW60suX4E8vc1NLMZBg7DMDdky5jgmRGyvCP30_TNVhWGb8hGy1zpXG3J1-HsHUZA2qSRzh3S2kfnY0tTQ-0aUkitBxvChVqY_RmpjzOOAZcfHzNB50S7pbeR2jB0loqstzCmNqR6CT4-kNvGhgkfr74jp9fDaf-eHT_fPvYvx2xYh2TONFIxdCVzhQFtysKCMegAdJ0zkCBKLQyWRirJgOdacWc4V9YKKFxj8h15_q8dxvS74DRXvZ8AQ7AR0zJVWgtRcKlW8OkKLnWPrhpG39vxUl3_yP8ACjpbPA</recordid><startdate>19950414</startdate><enddate>19950414</enddate><creator>Legrès, L G</creator><creator>Pochon, F</creator><creator>Barray, M</creator><creator>Gay, F</creator><creator>Chouaib, S</creator><creator>Delain, E</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19950414</creationdate><title>Evidence for the binding of a biologically active interleukin-2 to human alpha 2-macroglobulin</title><author>Legrès, L G ; Pochon, F ; Barray, M ; Gay, F ; Chouaib, S ; Delain, E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p536-d9f560ed80d49c7984ac99edcc7b30c5c28729e895650c13761d9116aa2c4df93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>alpha-Macroglobulins - chemistry</topic><topic>alpha-Macroglobulins - metabolism</topic><topic>Cells, Cultured</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Humans</topic><topic>Hydrolysis</topic><topic>Interleukin-2 - metabolism</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Recombinant Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Legrès, L G</creatorcontrib><creatorcontrib>Pochon, F</creatorcontrib><creatorcontrib>Barray, M</creatorcontrib><creatorcontrib>Gay, F</creatorcontrib><creatorcontrib>Chouaib, S</creatorcontrib><creatorcontrib>Delain, E</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</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>Legrès, L G</au><au>Pochon, F</au><au>Barray, M</au><au>Gay, F</au><au>Chouaib, S</au><au>Delain, E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence for the binding of a biologically active interleukin-2 to human alpha 2-macroglobulin</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1995-04-14</date><risdate>1995</risdate><volume>270</volume><issue>15</issue><spage>8381</spage><epage>8384</epage><pages>8381-8384</pages><issn>0021-9258</issn><abstract>Human alpha 2-macroglobulin (alpha 2M), which irreversibly entraps proteinases through a drastic conformational change, has also been reported to bind various cytokines. The meaning of cytokine binding to native and/or transformed alpha 2M molecules is, however, not understood. In an attempt to elucidate this question, we have studied the interaction of radioiodinated recombinant human interleukin-2 (125I-rhIL-2) with native and chymotrypsin (alpha 2M-C)- or methylamine-transformed (alpha 2M-MA) alpha 2M. Our results show that native and alpha 2M-MA are able to bind 125I-rhIL-2, with binding occurring only with the latter in a covalent manner, whereas the labeled cytokine is proteolyzed when incubated with alpha 2M-entrapped chymotrypsin. The degradation of uncomplexed 125I-rhIL-2 has also been observed in the presence of trypsin, whereas 125I-rhIL-2 bound to alpha 2M-MA is protected. Moreover, the proliferative activity of this cytokine on responsive cells is still maintained either with native alpha 2M- or alpha 2M-MA-complexed rhIL-2 in comparison with that observed with the cytokine alone. Our results, which lead us to consider alpha 2M molecules as IL-2-binding proteins, emphasize the possible role of these molecules as immune response regulators.</abstract><cop>United States</cop><pmid>7536736</pmid><tpages>4</tpages></addata></record> |
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subjects | alpha-Macroglobulins - chemistry alpha-Macroglobulins - metabolism Cells, Cultured Electrophoresis, Polyacrylamide Gel Humans Hydrolysis Interleukin-2 - metabolism Protein Binding Protein Conformation Recombinant Proteins - metabolism |
title | Evidence for the binding of a biologically active interleukin-2 to human alpha 2-macroglobulin |
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