CD69 molecule in human neutrophils: Its expression and role in signal-transducing mechanisms
The CD69 glycoprotein is an early activation antigen of T and B lymphocytes and it is constitutively expressed on thymocytes and platelets. Here we report its presence on neutrophils and on bone marrow-derived myeloid precursors. Indeed, promyelocytic cells are CD69 + on the cell membrane, while in...
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Veröffentlicht in: | Cellular immunology 1992-06, Vol.142 (1), p.186-196 |
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description | The CD69 glycoprotein is an early activation antigen of T and B lymphocytes and it is constitutively expressed on thymocytes and platelets. Here we report its presence on neutrophils and on bone marrow-derived myeloid precursors. Indeed, promyelocytic cells are CD69
+ on the cell membrane, while in resting neutrophils this molecule is located inside the cell. However, intracellular CD69 molecules are rapidly mobilized to the cell surface upon activation by PMA or fMLP. This translocation is independent on a new protein synthesis, as it is not inhibited by cycloheximide; furthermore, CD69 molecules are likely stored in a
trans-Golgi structure since their expression is not affected by brefeldin A, a drug that blocks molecular trafficking from ER to Golgi vescicles. Immunoprecipitation of CD69 molecules either from activated neutrophils or from bone marrow cells showed that this protein has the same molecular size (28–34 kDa) as observed in platelets, T and B lymphocytes, and thymocytes. This similarity is reflected also in the functional role played by this molecule: in neutrophils as well as in lymphocytes and platelets, CD69 stimulation induced Ca
2+ influx through cellular membrane; furthermore, the perturbation of the CD69 antigen on PMA-activated neutrophils enhances the lysozyme release, suggesting a role of this molecule in the regulation of granule exocytosis, probably through a Ca
2+-dependent mechanism. |
doi_str_mv | 10.1016/0008-8749(92)90279-X |
format | Article |
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+ on the cell membrane, while in resting neutrophils this molecule is located inside the cell. However, intracellular CD69 molecules are rapidly mobilized to the cell surface upon activation by PMA or fMLP. This translocation is independent on a new protein synthesis, as it is not inhibited by cycloheximide; furthermore, CD69 molecules are likely stored in a
trans-Golgi structure since their expression is not affected by brefeldin A, a drug that blocks molecular trafficking from ER to Golgi vescicles. Immunoprecipitation of CD69 molecules either from activated neutrophils or from bone marrow cells showed that this protein has the same molecular size (28–34 kDa) as observed in platelets, T and B lymphocytes, and thymocytes. This similarity is reflected also in the functional role played by this molecule: in neutrophils as well as in lymphocytes and platelets, CD69 stimulation induced Ca
2+ influx through cellular membrane; furthermore, the perturbation of the CD69 antigen on PMA-activated neutrophils enhances the lysozyme release, suggesting a role of this molecule in the regulation of granule exocytosis, probably through a Ca
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+ on the cell membrane, while in resting neutrophils this molecule is located inside the cell. However, intracellular CD69 molecules are rapidly mobilized to the cell surface upon activation by PMA or fMLP. This translocation is independent on a new protein synthesis, as it is not inhibited by cycloheximide; furthermore, CD69 molecules are likely stored in a
trans-Golgi structure since their expression is not affected by brefeldin A, a drug that blocks molecular trafficking from ER to Golgi vescicles. Immunoprecipitation of CD69 molecules either from activated neutrophils or from bone marrow cells showed that this protein has the same molecular size (28–34 kDa) as observed in platelets, T and B lymphocytes, and thymocytes. This similarity is reflected also in the functional role played by this molecule: in neutrophils as well as in lymphocytes and platelets, CD69 stimulation induced Ca
2+ influx through cellular membrane; furthermore, the perturbation of the CD69 antigen on PMA-activated neutrophils enhances the lysozyme release, suggesting a role of this molecule in the regulation of granule exocytosis, probably through a Ca
2+-dependent mechanism.</description><subject>Antigens, CD - analysis</subject><subject>Antigens, CD - physiology</subject><subject>Antigens, Differentiation, T-Lymphocyte - analysis</subject><subject>Antigens, Differentiation, T-Lymphocyte - physiology</subject><subject>Biological and medical sciences</subject><subject>Bone Marrow Cells</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Humans</subject><subject>Immunobiology</subject><subject>Lectins, C-Type</subject><subject>Lysosomes - metabolism</subject><subject>Myeloid cells: ontogeny, maturation, markers, receptors</subject><subject>N-Formylmethionine Leucyl-Phenylalanine</subject><subject>Neutrophils - immunology</subject><subject>Neutrophils - metabolism</subject><subject>Phytohemagglutinins</subject><subject>Polynuclears</subject><subject>Signal Transduction</subject><issn>0008-8749</issn><issn>1090-2163</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1v1DAQhi1EVZbCPwDJB4TgEPB3Yg5IaIFSqRIXkHpAshx70jVKnK0nQeXfkyWr9ganOczzvpp5CHnG2RvOuHnLGGuqplb2lRWvLRO1ra4ekA1nllWCG_mQbO6QR-Qx4k_GOFeWnZJTrhtjtd6QH9uPxtJh7CHMPdCU6W4efKYZ5qmM-13q8R29mJDC7b4AYhoz9TnSMq40puvs-2oqPmOcQ8rXdICw8znhgE_ISed7hKfHeUa-f_70bfuluvx6frH9cFkFLdVUtVoz72UUDWjZMKsj1zwG1qoggzYSamGMrLtOKBWZ0raVbct5VLKLujVanpGXa---jDcz4OSGhAH63mcYZ3S1sKYWTPwXXKwJo7lcQLWCoYyIBTq3L2nw5bfjzB3su4Nad1DrrHB_7burJfb82D-3A8T70Kp72b847j0G33eLtZDwDtNq-b7mC_Z-xWCR9itBcRgS5AAxFQiTi2P69x1_AAXRoGI</recordid><startdate>19920601</startdate><enddate>19920601</enddate><creator>Gavioli, Riccardo</creator><creator>Risso, Angela</creator><creator>Smilovich, Daniela</creator><creator>Baldissarro, Isabella</creator><creator>Capra, M.Cristina</creator><creator>Bargellesi, Antonio</creator><creator>Cosulich, M.Elisabetta</creator><general>Elsevier Inc</general><general>Elsevier</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>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19920601</creationdate><title>CD69 molecule in human neutrophils: Its expression and role in signal-transducing mechanisms</title><author>Gavioli, Riccardo ; Risso, Angela ; Smilovich, Daniela ; Baldissarro, Isabella ; Capra, M.Cristina ; Bargellesi, Antonio ; Cosulich, M.Elisabetta</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c534t-b550aa3d28e538095d151dc0b4c3c563e726637ff244d0459b3bb11d43fd5b653</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Antigens, CD - analysis</topic><topic>Antigens, CD - physiology</topic><topic>Antigens, Differentiation, T-Lymphocyte - analysis</topic><topic>Antigens, Differentiation, T-Lymphocyte - physiology</topic><topic>Biological and medical sciences</topic><topic>Bone Marrow Cells</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Humans</topic><topic>Immunobiology</topic><topic>Lectins, C-Type</topic><topic>Lysosomes - metabolism</topic><topic>Myeloid cells: ontogeny, maturation, markers, receptors</topic><topic>N-Formylmethionine Leucyl-Phenylalanine</topic><topic>Neutrophils - immunology</topic><topic>Neutrophils - metabolism</topic><topic>Phytohemagglutinins</topic><topic>Polynuclears</topic><topic>Signal Transduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gavioli, Riccardo</creatorcontrib><creatorcontrib>Risso, Angela</creatorcontrib><creatorcontrib>Smilovich, Daniela</creatorcontrib><creatorcontrib>Baldissarro, Isabella</creatorcontrib><creatorcontrib>Capra, M.Cristina</creatorcontrib><creatorcontrib>Bargellesi, Antonio</creatorcontrib><creatorcontrib>Cosulich, M.Elisabetta</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>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cellular immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gavioli, Riccardo</au><au>Risso, Angela</au><au>Smilovich, Daniela</au><au>Baldissarro, Isabella</au><au>Capra, M.Cristina</au><au>Bargellesi, Antonio</au><au>Cosulich, M.Elisabetta</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>CD69 molecule in human neutrophils: Its expression and role in signal-transducing mechanisms</atitle><jtitle>Cellular immunology</jtitle><addtitle>Cell Immunol</addtitle><date>1992-06-01</date><risdate>1992</risdate><volume>142</volume><issue>1</issue><spage>186</spage><epage>196</epage><pages>186-196</pages><issn>0008-8749</issn><eissn>1090-2163</eissn><coden>CLIMB8</coden><abstract>The CD69 glycoprotein is an early activation antigen of T and B lymphocytes and it is constitutively expressed on thymocytes and platelets. Here we report its presence on neutrophils and on bone marrow-derived myeloid precursors. Indeed, promyelocytic cells are CD69
+ on the cell membrane, while in resting neutrophils this molecule is located inside the cell. However, intracellular CD69 molecules are rapidly mobilized to the cell surface upon activation by PMA or fMLP. This translocation is independent on a new protein synthesis, as it is not inhibited by cycloheximide; furthermore, CD69 molecules are likely stored in a
trans-Golgi structure since their expression is not affected by brefeldin A, a drug that blocks molecular trafficking from ER to Golgi vescicles. Immunoprecipitation of CD69 molecules either from activated neutrophils or from bone marrow cells showed that this protein has the same molecular size (28–34 kDa) as observed in platelets, T and B lymphocytes, and thymocytes. This similarity is reflected also in the functional role played by this molecule: in neutrophils as well as in lymphocytes and platelets, CD69 stimulation induced Ca
2+ influx through cellular membrane; furthermore, the perturbation of the CD69 antigen on PMA-activated neutrophils enhances the lysozyme release, suggesting a role of this molecule in the regulation of granule exocytosis, probably through a Ca
2+-dependent mechanism.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>1586955</pmid><doi>10.1016/0008-8749(92)90279-X</doi><tpages>11</tpages></addata></record> |
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subjects | Antigens, CD - analysis Antigens, CD - physiology Antigens, Differentiation, T-Lymphocyte - analysis Antigens, Differentiation, T-Lymphocyte - physiology Biological and medical sciences Bone Marrow Cells Fundamental and applied biological sciences. Psychology Fundamental immunology Humans Immunobiology Lectins, C-Type Lysosomes - metabolism Myeloid cells: ontogeny, maturation, markers, receptors N-Formylmethionine Leucyl-Phenylalanine Neutrophils - immunology Neutrophils - metabolism Phytohemagglutinins Polynuclears Signal Transduction |
title | CD69 molecule in human neutrophils: Its expression and role in signal-transducing mechanisms |
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