Serglycin Is Essential for Maturation of Mast Cell Secretory Granule
To address the biological function of the scarcely studied intracellular proteoglycans, we targeted the gene for serglycin (SG), the only known committed intracellular proteoglycan. SG-/- mice developed normally and were fertile, but their mast cells (MCs) were severely affected. In peritoneum there...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 2004-09, Vol.279 (39), p.40897-40905 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 40905 |
|---|---|
| container_issue | 39 |
| container_start_page | 40897 |
| container_title | The Journal of biological chemistry |
| container_volume | 279 |
| creator | Åbrink, Magnus Grujic, Mirjana Pejler, Gunnar |
| description | To address the biological function of the scarcely studied intracellular proteoglycans, we targeted the gene for serglycin (SG), the only known committed intracellular proteoglycan. SG-/- mice developed normally and were fertile, but their mast cells (MCs) were severely affected. In peritoneum there was a complete absence of normal granulated MCs. Furthermore, peritoneal cells and ear tissue from SG-/- animals were devoid of the various MC-specific proteases. However, mRNA for the proteases was present in SG+/+, SG+/-, and SG-/- tissues, indicating that SG is essential for the storage, but not expression, of the MC proteases. Experiments, in which the differentiation of bone marrow stem cells into mature MCs was followed, showed that secretory granule maturation was compromised in SG-/- cells. Moreover, SG+/+ and SG+/- cells, but not SG-/- cells, synthesized proteoglycans of high anionic charge density. Taken together, we demonstrate a key role for SG proteoglycan in MC function. |
| doi_str_mv | 10.1074/jbc.M405856200 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_66894182</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0021925820771863</els_id><sourcerecordid>66894182</sourcerecordid><originalsourceid>FETCH-LOGICAL-c475t-1faa434a7a6e6eb5f9321a3728aa8c1075c97664fa84acd9899affba87b6eab03</originalsourceid><addsrcrecordid>eNp1kD1PwzAQhi0EoqWwMqIMiC3FTpzEHlH5qtSKoSCxWRf3TI3SuNgJqP8eo1bqxC2nk5473fsQcsnomNGK337WejzntBBFmVF6RIaMijzNC_Z-TIaUZiyVWSEG5CyETxqLS3ZKBqzIciYyNiT3C_QfzVbbNpmG5CEEbDsLTWKcT-bQ9R4669rEmTiFLplg0yQL1B4757fJk4e2b_CcnBhoAl7s-4i8PT68Tp7T2cvTdHI3SzWvii5lBoDnHCooscS6MDLPGORVJgCEjnEKLauy5AYEB72UQkowpgZR1SVCTfMRudnd3Xj31WPo1NoGHV-CFl0fVFkKyWOuCI53oPYuBI9Gbbxdg98qRtWfNxW9qYO3uHC1v9zXa1we8L2oCFzvgJX9WP1Yj6q2Tq9wrbJKqlwqToWsIiZ2GEYN3xa9Ctpiq3EZV3Snls7-98IvO9KHeg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>66894182</pqid></control><display><type>article</type><title>Serglycin Is Essential for Maturation of Mast Cell Secretory Granule</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Åbrink, Magnus ; Grujic, Mirjana ; Pejler, Gunnar</creator><creatorcontrib>Åbrink, Magnus ; Grujic, Mirjana ; Pejler, Gunnar</creatorcontrib><description>To address the biological function of the scarcely studied intracellular proteoglycans, we targeted the gene for serglycin (SG), the only known committed intracellular proteoglycan. SG-/- mice developed normally and were fertile, but their mast cells (MCs) were severely affected. In peritoneum there was a complete absence of normal granulated MCs. Furthermore, peritoneal cells and ear tissue from SG-/- animals were devoid of the various MC-specific proteases. However, mRNA for the proteases was present in SG+/+, SG+/-, and SG-/- tissues, indicating that SG is essential for the storage, but not expression, of the MC proteases. Experiments, in which the differentiation of bone marrow stem cells into mature MCs was followed, showed that secretory granule maturation was compromised in SG-/- cells. Moreover, SG+/+ and SG+/- cells, but not SG-/- cells, synthesized proteoglycans of high anionic charge density. Taken together, we demonstrate a key role for SG proteoglycan in MC function.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M405856200</identifier><identifier>PMID: 15231821</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Blotting, Northern ; Blotting, Western ; Bone Marrow Cells - metabolism ; Cells, Cultured ; Contig Mapping ; Cytoplasmic Granules - metabolism ; DNA - metabolism ; Endopeptidases - metabolism ; Exons ; Gene Targeting ; Genotype ; Glycosaminoglycans - metabolism ; Immunoblotting ; Immunohistochemistry ; Male ; Mast Cells - metabolism ; Mice ; Mice, Knockout ; Mice, Transgenic ; Models, Genetic ; Peritoneum - cytology ; Phenotype ; Proteoglycans - genetics ; Proteoglycans - metabolism ; Proteoglycans - physiology ; Proto-Oncogene Proteins c-kit - metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; RNA, Messenger - metabolism ; Secretory Vesicles - metabolism ; Serine Endopeptidases - metabolism ; Stem Cells - metabolism ; Vesicular Transport Proteins</subject><ispartof>The Journal of biological chemistry, 2004-09, Vol.279 (39), p.40897-40905</ispartof><rights>2004 © 2004 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>Copyright 2004 American Society for Biochemistry and Molecular Biology, Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c475t-1faa434a7a6e6eb5f9321a3728aa8c1075c97664fa84acd9899affba87b6eab03</citedby><cites>FETCH-LOGICAL-c475t-1faa434a7a6e6eb5f9321a3728aa8c1075c97664fa84acd9899affba87b6eab03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15231821$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Åbrink, Magnus</creatorcontrib><creatorcontrib>Grujic, Mirjana</creatorcontrib><creatorcontrib>Pejler, Gunnar</creatorcontrib><title>Serglycin Is Essential for Maturation of Mast Cell Secretory Granule</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>To address the biological function of the scarcely studied intracellular proteoglycans, we targeted the gene for serglycin (SG), the only known committed intracellular proteoglycan. SG-/- mice developed normally and were fertile, but their mast cells (MCs) were severely affected. In peritoneum there was a complete absence of normal granulated MCs. Furthermore, peritoneal cells and ear tissue from SG-/- animals were devoid of the various MC-specific proteases. However, mRNA for the proteases was present in SG+/+, SG+/-, and SG-/- tissues, indicating that SG is essential for the storage, but not expression, of the MC proteases. Experiments, in which the differentiation of bone marrow stem cells into mature MCs was followed, showed that secretory granule maturation was compromised in SG-/- cells. Moreover, SG+/+ and SG+/- cells, but not SG-/- cells, synthesized proteoglycans of high anionic charge density. Taken together, we demonstrate a key role for SG proteoglycan in MC function.</description><subject>Animals</subject><subject>Blotting, Northern</subject><subject>Blotting, Western</subject><subject>Bone Marrow Cells - metabolism</subject><subject>Cells, Cultured</subject><subject>Contig Mapping</subject><subject>Cytoplasmic Granules - metabolism</subject><subject>DNA - metabolism</subject><subject>Endopeptidases - metabolism</subject><subject>Exons</subject><subject>Gene Targeting</subject><subject>Genotype</subject><subject>Glycosaminoglycans - metabolism</subject><subject>Immunoblotting</subject><subject>Immunohistochemistry</subject><subject>Male</subject><subject>Mast Cells - metabolism</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Mice, Transgenic</subject><subject>Models, Genetic</subject><subject>Peritoneum - cytology</subject><subject>Phenotype</subject><subject>Proteoglycans - genetics</subject><subject>Proteoglycans - metabolism</subject><subject>Proteoglycans - physiology</subject><subject>Proto-Oncogene Proteins c-kit - metabolism</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RNA, Messenger - metabolism</subject><subject>Secretory Vesicles - metabolism</subject><subject>Serine Endopeptidases - metabolism</subject><subject>Stem Cells - metabolism</subject><subject>Vesicular Transport Proteins</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kD1PwzAQhi0EoqWwMqIMiC3FTpzEHlH5qtSKoSCxWRf3TI3SuNgJqP8eo1bqxC2nk5473fsQcsnomNGK337WejzntBBFmVF6RIaMijzNC_Z-TIaUZiyVWSEG5CyETxqLS3ZKBqzIciYyNiT3C_QfzVbbNpmG5CEEbDsLTWKcT-bQ9R4669rEmTiFLplg0yQL1B4757fJk4e2b_CcnBhoAl7s-4i8PT68Tp7T2cvTdHI3SzWvii5lBoDnHCooscS6MDLPGORVJgCEjnEKLauy5AYEB72UQkowpgZR1SVCTfMRudnd3Xj31WPo1NoGHV-CFl0fVFkKyWOuCI53oPYuBI9Gbbxdg98qRtWfNxW9qYO3uHC1v9zXa1we8L2oCFzvgJX9WP1Yj6q2Tq9wrbJKqlwqToWsIiZ2GEYN3xa9Ctpiq3EZV3Snls7-98IvO9KHeg</recordid><startdate>20040924</startdate><enddate>20040924</enddate><creator>Åbrink, Magnus</creator><creator>Grujic, Mirjana</creator><creator>Pejler, Gunnar</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</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>7X8</scope></search><sort><creationdate>20040924</creationdate><title>Serglycin Is Essential for Maturation of Mast Cell Secretory Granule</title><author>Åbrink, Magnus ; Grujic, Mirjana ; Pejler, Gunnar</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c475t-1faa434a7a6e6eb5f9321a3728aa8c1075c97664fa84acd9899affba87b6eab03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Animals</topic><topic>Blotting, Northern</topic><topic>Blotting, Western</topic><topic>Bone Marrow Cells - metabolism</topic><topic>Cells, Cultured</topic><topic>Contig Mapping</topic><topic>Cytoplasmic Granules - metabolism</topic><topic>DNA - metabolism</topic><topic>Endopeptidases - metabolism</topic><topic>Exons</topic><topic>Gene Targeting</topic><topic>Genotype</topic><topic>Glycosaminoglycans - metabolism</topic><topic>Immunoblotting</topic><topic>Immunohistochemistry</topic><topic>Male</topic><topic>Mast Cells - metabolism</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Mice, Transgenic</topic><topic>Models, Genetic</topic><topic>Peritoneum - cytology</topic><topic>Phenotype</topic><topic>Proteoglycans - genetics</topic><topic>Proteoglycans - metabolism</topic><topic>Proteoglycans - physiology</topic><topic>Proto-Oncogene Proteins c-kit - metabolism</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>RNA, Messenger - metabolism</topic><topic>Secretory Vesicles - metabolism</topic><topic>Serine Endopeptidases - metabolism</topic><topic>Stem Cells - metabolism</topic><topic>Vesicular Transport Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Åbrink, Magnus</creatorcontrib><creatorcontrib>Grujic, Mirjana</creatorcontrib><creatorcontrib>Pejler, Gunnar</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>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Åbrink, Magnus</au><au>Grujic, Mirjana</au><au>Pejler, Gunnar</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Serglycin Is Essential for Maturation of Mast Cell Secretory Granule</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2004-09-24</date><risdate>2004</risdate><volume>279</volume><issue>39</issue><spage>40897</spage><epage>40905</epage><pages>40897-40905</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>To address the biological function of the scarcely studied intracellular proteoglycans, we targeted the gene for serglycin (SG), the only known committed intracellular proteoglycan. SG-/- mice developed normally and were fertile, but their mast cells (MCs) were severely affected. In peritoneum there was a complete absence of normal granulated MCs. Furthermore, peritoneal cells and ear tissue from SG-/- animals were devoid of the various MC-specific proteases. However, mRNA for the proteases was present in SG+/+, SG+/-, and SG-/- tissues, indicating that SG is essential for the storage, but not expression, of the MC proteases. Experiments, in which the differentiation of bone marrow stem cells into mature MCs was followed, showed that secretory granule maturation was compromised in SG-/- cells. Moreover, SG+/+ and SG+/- cells, but not SG-/- cells, synthesized proteoglycans of high anionic charge density. Taken together, we demonstrate a key role for SG proteoglycan in MC function.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15231821</pmid><doi>10.1074/jbc.M405856200</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 2004-09, Vol.279 (39), p.40897-40905 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_66894182 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Blotting, Northern Blotting, Western Bone Marrow Cells - metabolism Cells, Cultured Contig Mapping Cytoplasmic Granules - metabolism DNA - metabolism Endopeptidases - metabolism Exons Gene Targeting Genotype Glycosaminoglycans - metabolism Immunoblotting Immunohistochemistry Male Mast Cells - metabolism Mice Mice, Knockout Mice, Transgenic Models, Genetic Peritoneum - cytology Phenotype Proteoglycans - genetics Proteoglycans - metabolism Proteoglycans - physiology Proto-Oncogene Proteins c-kit - metabolism Reverse Transcriptase Polymerase Chain Reaction RNA, Messenger - metabolism Secretory Vesicles - metabolism Serine Endopeptidases - metabolism Stem Cells - metabolism Vesicular Transport Proteins |
| title | Serglycin Is Essential for Maturation of Mast Cell Secretory Granule |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-12T16%3A40%3A35IST&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=Serglycin%20Is%20Essential%20for%20Maturation%20of%20Mast%20Cell%20Secretory%20Granule&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=%C3%85brink,%20Magnus&rft.date=2004-09-24&rft.volume=279&rft.issue=39&rft.spage=40897&rft.epage=40905&rft.pages=40897-40905&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1074/jbc.M405856200&rft_dat=%3Cproquest_cross%3E66894182%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=66894182&rft_id=info:pmid/15231821&rft_els_id=S0021925820771863&rfr_iscdi=true |