Interleukin 2 is a lectin that associates its receptor with the T-cell receptor complex
To determine the nature of the mechanism by which the binding of interleukin-2 (IL-2) to its receptor (IL-2R beta) induces IL-2R beta phosphorylation by the tyrosine kinase p56lck associated with the T-cell receptor (TCR) complex, we investigated the possibility that this mechanism was due to the pu...
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| Veröffentlicht in: | Biochemical journal 1996-08, Vol.318 ( Pt 1) (1), p.49-53 |
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| container_title | Biochemical journal |
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| creator | Zanetta, J P Alonso, C Michalski, J C |
| description | To determine the nature of the mechanism by which the binding of interleukin-2 (IL-2) to its receptor (IL-2R beta) induces IL-2R beta phosphorylation by the tyrosine kinase p56lck associated with the T-cell receptor (TCR) complex, we investigated the possibility that this mechanism was due to the putative lectin activity of IL-2 ([Sherblom, Sathyamoorthy, Decker and Muchmore (1989) J. Immunol. 143, 939-944]. Here we demonstrate that IL-2 is a calcium-independent lectin specific for oligomannosidic N-glycans with five and six mannose residues. This lectin activity is preserved after binding of IL-2 to IL-2R beta. IL-2 behaves as a bifunctional molecule that associates IL-2R beta with specific glycoprotein ligands of the TCR complex including a glycosylated form of CD3. |
| doi_str_mv | 10.1042/bj3180049 |
| format | Article |
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Immunol. 143, 939-944]. Here we demonstrate that IL-2 is a calcium-independent lectin specific for oligomannosidic N-glycans with five and six mannose residues. This lectin activity is preserved after binding of IL-2 to IL-2R beta. IL-2 behaves as a bifunctional molecule that associates IL-2R beta with specific glycoprotein ligands of the TCR complex including a glycosylated form of CD3.</description><subject>Carbohydrate Sequence</subject><subject>Glycoproteins - metabolism</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>Interleukin-2 - metabolism</subject><subject>Interleukin-2 - pharmacology</subject><subject>Lectins - metabolism</subject><subject>Lectins - pharmacology</subject><subject>Lymphocyte Specific Protein Tyrosine Kinase p56(lck)</subject><subject>Lymphocytes - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Oligosaccharides - pharmacology</subject><subject>Phosphorylation</subject><subject>Polysaccharides - metabolism</subject><subject>Polysaccharides - pharmacology</subject><subject>Receptors, Antigen, T-Cell - metabolism</subject><subject>Receptors, Interleukin-2 - metabolism</subject><subject>Ribonucleases - metabolism</subject><subject>src-Family Kinases - metabolism</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1LAzEQhoMotVYP_gAhJ8HD6iSb3exeBCl-FApeKh5DNp21qftlkvrx793SUvXkYWYY5uHlHV5CThlcMhD8qljGLAMQ-R4ZMiEhyiTP9skQeCqiFDg7JEfeLwGYAAEDMshkykTChuR50gR0Fa5ebUM5tZ5qWqEJ_RYWOlDtfWusDuipDZ46NNiF1tEPGxY9gXQWGayqn4Np667Cz2NyUOrK48l2jsjT3e1s_BBNH-8n45tpZASwEKGQppjHDEuW5oUuBGjkItZSA6KeJ0UuMYnLOciir7I0fY9FYXQqmOmXeESuN7rdqqhxbrAJTleqc7bW7ku12qq_l8Yu1Ev7rhhnMslkL3C-FXDt2wp9ULX165d0g-3KK5lxyUXyP8iSPM4h4T14sQGNa713WO7cMFDruNQurp49-21_R27zib8BCBSSUA</recordid><startdate>19960815</startdate><enddate>19960815</enddate><creator>Zanetta, J P</creator><creator>Alonso, C</creator><creator>Michalski, J C</creator><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><scope>5PM</scope></search><sort><creationdate>19960815</creationdate><title>Interleukin 2 is a lectin that associates its receptor with the T-cell receptor complex</title><author>Zanetta, J P ; 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Immunol. 143, 939-944]. Here we demonstrate that IL-2 is a calcium-independent lectin specific for oligomannosidic N-glycans with five and six mannose residues. This lectin activity is preserved after binding of IL-2 to IL-2R beta. IL-2 behaves as a bifunctional molecule that associates IL-2R beta with specific glycoprotein ligands of the TCR complex including a glycosylated form of CD3.</abstract><cop>England</cop><pmid>8761451</pmid><doi>10.1042/bj3180049</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biochemical journal, 1996-08, Vol.318 ( Pt 1) (1), p.49-53 |
| issn | 0264-6021 1470-8728 |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Carbohydrate Sequence Glycoproteins - metabolism Humans Immunoblotting Interleukin-2 - metabolism Interleukin-2 - pharmacology Lectins - metabolism Lectins - pharmacology Lymphocyte Specific Protein Tyrosine Kinase p56(lck) Lymphocytes - metabolism Molecular Sequence Data Oligosaccharides - pharmacology Phosphorylation Polysaccharides - metabolism Polysaccharides - pharmacology Receptors, Antigen, T-Cell - metabolism Receptors, Interleukin-2 - metabolism Ribonucleases - metabolism src-Family Kinases - metabolism |
| title | Interleukin 2 is a lectin that associates its receptor with the T-cell receptor complex |
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