Endobrevin/VAMP8 mediates exocytotic release of hexosaminidase from rat basophilic leukaemia cells
Mast cells are important players in innate immunity and mediate allergic responses. Upon stimulation, they release biologically active mediators including histamine, cytokines and lysosomal hydrolases. We used permeabilized rat basophilic leukaemia cells as model to identify R-SNAREs (soluble NSF (N...
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| Veröffentlicht in: | FEBS letters 2007-07, Vol.581 (18), p.3479-3484 |
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| creator | Lippert, Undine Ferrari, David M. Jahn, Reinhard |
| description | Mast cells are important players in innate immunity and mediate allergic responses. Upon stimulation, they release biologically active mediators including histamine, cytokines and lysosomal hydrolases. We used permeabilized rat basophilic leukaemia cells as model to identify R-SNAREs (soluble NSF (N-ethylmaleimide-sensitive fusion protein)) mediating exocytosis of hexosaminidase from mast cells. Of a complete set of recombinant mammalian R-SNAREs, only vesicle associated membrane protein (VAMP8)/endobrevin consistently blocked hexosaminidase release, which was also insensitive to treatment with clostridial neurotoxins. Thus, VAMP8, which also mediates fusion of late endosomes and lysosomes, plays a major role in hexosaminidase release, strengthening the view that mast cell granules share properties of both secretory granules and lysosomes. |
| doi_str_mv | 10.1016/j.febslet.2007.06.057 |
| format | Article |
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Upon stimulation, they release biologically active mediators including histamine, cytokines and lysosomal hydrolases. We used permeabilized rat basophilic leukaemia cells as model to identify R-SNAREs (soluble NSF (N-ethylmaleimide-sensitive fusion protein)) mediating exocytosis of hexosaminidase from mast cells. Of a complete set of recombinant mammalian R-SNAREs, only vesicle associated membrane protein (VAMP8)/endobrevin consistently blocked hexosaminidase release, which was also insensitive to treatment with clostridial neurotoxins. Thus, VAMP8, which also mediates fusion of late endosomes and lysosomes, plays a major role in hexosaminidase release, strengthening the view that mast cell granules share properties of both secretory granules and lysosomes.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2007.06.057</identifier><identifier>PMID: 17618625</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Bacterial Proteins - pharmacology ; Basophils - drug effects ; Basophils - metabolism ; BoNT/D ; botulinum neurotoxin D ; Calcium - pharmacology ; Cell Line, Tumor ; Cell Membrane Permeability - drug effects ; Endobrevin ; Exocytosis ; Exocytosis - drug effects ; Hexosaminidase ; Hexosaminidases - metabolism ; Hexosaminidases - secretion ; Leukemia - genetics ; Leukemia - metabolism ; Mast cell ; R-SNARE ; R-SNARE Proteins - genetics ; R-SNARE Proteins - metabolism ; rat basophilic leukaemia ; Rats ; RBL ; SLO ; SNARE ; soluble NSF (N-ethylmaleimide-sensitive fusion protein) attachment protein receptor ; streptolysin O ; Streptolysins - pharmacology ; TeNT ; tetanus neurotoxin ; VAMP ; VAMP8 ; vesicle associated membrane protein ; Vesicle-Associated Membrane Protein 2 - metabolism ; Vesicle-Associated Membrane Protein 3 - metabolism</subject><ispartof>FEBS letters, 2007-07, Vol.581 (18), p.3479-3484</ispartof><rights>2007 Federation of European Biochemical Societies</rights><rights>FEBS Letters 581 (2007) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5060-6b87a2bb90f22ffbf2faf40fa9835e45747c130cc6978d2ba75c3fa9b6ff734b3</citedby><cites>FETCH-LOGICAL-c5060-6b87a2bb90f22ffbf2faf40fa9835e45747c130cc6978d2ba75c3fa9b6ff734b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2007.06.057$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2007.06.057$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,778,782,1414,1430,3539,27907,27908,45557,45558,45978,46392,46816</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17618625$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lippert, Undine</creatorcontrib><creatorcontrib>Ferrari, David M.</creatorcontrib><creatorcontrib>Jahn, Reinhard</creatorcontrib><title>Endobrevin/VAMP8 mediates exocytotic release of hexosaminidase from rat basophilic leukaemia cells</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Mast cells are important players in innate immunity and mediate allergic responses. Upon stimulation, they release biologically active mediators including histamine, cytokines and lysosomal hydrolases. We used permeabilized rat basophilic leukaemia cells as model to identify R-SNAREs (soluble NSF (N-ethylmaleimide-sensitive fusion protein)) mediating exocytosis of hexosaminidase from mast cells. Of a complete set of recombinant mammalian R-SNAREs, only vesicle associated membrane protein (VAMP8)/endobrevin consistently blocked hexosaminidase release, which was also insensitive to treatment with clostridial neurotoxins. Thus, VAMP8, which also mediates fusion of late endosomes and lysosomes, plays a major role in hexosaminidase release, strengthening the view that mast cell granules share properties of both secretory granules and lysosomes.</description><subject>Animals</subject><subject>Bacterial Proteins - pharmacology</subject><subject>Basophils - drug effects</subject><subject>Basophils - metabolism</subject><subject>BoNT/D</subject><subject>botulinum neurotoxin D</subject><subject>Calcium - pharmacology</subject><subject>Cell Line, Tumor</subject><subject>Cell Membrane Permeability - drug effects</subject><subject>Endobrevin</subject><subject>Exocytosis</subject><subject>Exocytosis - drug effects</subject><subject>Hexosaminidase</subject><subject>Hexosaminidases - metabolism</subject><subject>Hexosaminidases - secretion</subject><subject>Leukemia - genetics</subject><subject>Leukemia - metabolism</subject><subject>Mast cell</subject><subject>R-SNARE</subject><subject>R-SNARE Proteins - genetics</subject><subject>R-SNARE Proteins - metabolism</subject><subject>rat basophilic leukaemia</subject><subject>Rats</subject><subject>RBL</subject><subject>SLO</subject><subject>SNARE</subject><subject>soluble NSF (N-ethylmaleimide-sensitive fusion protein) attachment protein receptor</subject><subject>streptolysin O</subject><subject>Streptolysins - pharmacology</subject><subject>TeNT</subject><subject>tetanus neurotoxin</subject><subject>VAMP</subject><subject>VAMP8</subject><subject>vesicle associated membrane protein</subject><subject>Vesicle-Associated Membrane Protein 2 - metabolism</subject><subject>Vesicle-Associated Membrane Protein 3 - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU9P3DAQxS1UVBbaj0CVU28JYyexkxOiaPkjUYFE26tlO2PhbRJv7Sxlvz2OdiWOcLI88-Z5_HuEnFIoKFB-tios6tjjVDAAUQAvoBYHZEEbUeZlxZtPZAFAq7wWbXlEjmNcQbo3tP1MjqjgtOGsXhC9HDuvAz678ezPxc-HJhuwc2rCmOGLN9vJT85kAXtUETNvs6dUjmpwo-vmig1-yIKaMq2iXz-5Pql73PxVODiVGez7-IUcWtVH_Lo_T8jvq-Wvy5v87v769vLiLjc1cMi5boRiWrdgGbNWW2aVrcCqtilrrGpRCUNLMIa3oumYVqI2Zepqbq0oK12ekO8733Xw_zYYJzm4OG-gRvSbKBlU6c-UJWG9E5rgYwxo5Tq4QYWtpCBnuHIl93DlDFcClwlumvu2f2CjE6W3qT3NJLjZCf67Hrcfc5VXyx_scU5qDgpE6lAGyep8Z4WJ2LPDIKNxOJoUTkAzyc67d7Z9Bf7ipPo</recordid><startdate>20070724</startdate><enddate>20070724</enddate><creator>Lippert, Undine</creator><creator>Ferrari, David M.</creator><creator>Jahn, Reinhard</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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></search><sort><creationdate>20070724</creationdate><title>Endobrevin/VAMP8 mediates exocytotic release of hexosaminidase from rat basophilic leukaemia cells</title><author>Lippert, Undine ; Ferrari, David M. ; Jahn, Reinhard</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5060-6b87a2bb90f22ffbf2faf40fa9835e45747c130cc6978d2ba75c3fa9b6ff734b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Animals</topic><topic>Bacterial Proteins - pharmacology</topic><topic>Basophils - drug effects</topic><topic>Basophils - metabolism</topic><topic>BoNT/D</topic><topic>botulinum neurotoxin D</topic><topic>Calcium - pharmacology</topic><topic>Cell Line, Tumor</topic><topic>Cell Membrane Permeability - drug effects</topic><topic>Endobrevin</topic><topic>Exocytosis</topic><topic>Exocytosis - drug effects</topic><topic>Hexosaminidase</topic><topic>Hexosaminidases - metabolism</topic><topic>Hexosaminidases - secretion</topic><topic>Leukemia - genetics</topic><topic>Leukemia - metabolism</topic><topic>Mast cell</topic><topic>R-SNARE</topic><topic>R-SNARE Proteins - genetics</topic><topic>R-SNARE Proteins - metabolism</topic><topic>rat basophilic leukaemia</topic><topic>Rats</topic><topic>RBL</topic><topic>SLO</topic><topic>SNARE</topic><topic>soluble NSF (N-ethylmaleimide-sensitive fusion protein) attachment protein receptor</topic><topic>streptolysin O</topic><topic>Streptolysins - pharmacology</topic><topic>TeNT</topic><topic>tetanus neurotoxin</topic><topic>VAMP</topic><topic>VAMP8</topic><topic>vesicle associated membrane protein</topic><topic>Vesicle-Associated Membrane Protein 2 - metabolism</topic><topic>Vesicle-Associated Membrane Protein 3 - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lippert, Undine</creatorcontrib><creatorcontrib>Ferrari, David M.</creatorcontrib><creatorcontrib>Jahn, Reinhard</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lippert, Undine</au><au>Ferrari, David M.</au><au>Jahn, Reinhard</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Endobrevin/VAMP8 mediates exocytotic release of hexosaminidase from rat basophilic leukaemia cells</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2007-07-24</date><risdate>2007</risdate><volume>581</volume><issue>18</issue><spage>3479</spage><epage>3484</epage><pages>3479-3484</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Mast cells are important players in innate immunity and mediate allergic responses. Upon stimulation, they release biologically active mediators including histamine, cytokines and lysosomal hydrolases. We used permeabilized rat basophilic leukaemia cells as model to identify R-SNAREs (soluble NSF (N-ethylmaleimide-sensitive fusion protein)) mediating exocytosis of hexosaminidase from mast cells. Of a complete set of recombinant mammalian R-SNAREs, only vesicle associated membrane protein (VAMP8)/endobrevin consistently blocked hexosaminidase release, which was also insensitive to treatment with clostridial neurotoxins. Thus, VAMP8, which also mediates fusion of late endosomes and lysosomes, plays a major role in hexosaminidase release, strengthening the view that mast cell granules share properties of both secretory granules and lysosomes.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>17618625</pmid><doi>10.1016/j.febslet.2007.06.057</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Wiley Online Library Free Content; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals Bacterial Proteins - pharmacology Basophils - drug effects Basophils - metabolism BoNT/D botulinum neurotoxin D Calcium - pharmacology Cell Line, Tumor Cell Membrane Permeability - drug effects Endobrevin Exocytosis Exocytosis - drug effects Hexosaminidase Hexosaminidases - metabolism Hexosaminidases - secretion Leukemia - genetics Leukemia - metabolism Mast cell R-SNARE R-SNARE Proteins - genetics R-SNARE Proteins - metabolism rat basophilic leukaemia Rats RBL SLO SNARE soluble NSF (N-ethylmaleimide-sensitive fusion protein) attachment protein receptor streptolysin O Streptolysins - pharmacology TeNT tetanus neurotoxin VAMP VAMP8 vesicle associated membrane protein Vesicle-Associated Membrane Protein 2 - metabolism Vesicle-Associated Membrane Protein 3 - metabolism |
| title | Endobrevin/VAMP8 mediates exocytotic release of hexosaminidase from rat basophilic leukaemia cells |
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