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Ultrastructural localization of highly variable 185/333 immune response proteins in the coelomocytes of the sea urchin, Heliocidaris erythrogramma
The 185/333 proteins of sea urchins represent a family of highly variable immune response molecules with unknown functions. In this study, we show that 185/333 proteins are expressed by three cell types: amoebocytes, colourless spherule cells and gut‐associated amoebocytes. A sub‐population of amoeb...
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Published in: | Immunology and cell biology 2011-11, Vol.89 (8), p.861-869 |
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description | The 185/333 proteins of sea urchins represent a family of highly variable immune response molecules with unknown functions. In this study, we show that 185/333 proteins are expressed by three cell types: amoebocytes, colourless spherule cells and gut‐associated amoebocytes. A sub‐population of amoebocytes express 185/333 proteins on the membranes of vesicles emanating from the trans‐Golgi and which later fuse with the plasma membranes of the cells. The previously uncharacterized gut‐associated amoebocytes also show a high level of 185/333 protein expression on their internal vesicles and plasma membranes. Colourless spherule cells contain 185/333 proteins within large spherules (specialized intracellular vesicles). In the presence of bacteria and yeast, the ultrastucture of colourless spherule cells changes and 185/333 proteins disappear. In contrast, 185/333 proteins were not found in the phagosomes of coelomocytes. The 185/333‐positive gut amoebocytes were often associated with anuclear bodies, which appeared to incorporate material of microbial origin that was surrounded by 185/333 proteins. The association between 185/333 proteins on gut amoebocytes and anuclear bodies suggests that these proteins may be involved in the phagocytosis of microbes in the gut epithelium. |
doi_str_mv | 10.1038/icb.2011.3 |
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In this study, we show that 185/333 proteins are expressed by three cell types: amoebocytes, colourless spherule cells and gut‐associated amoebocytes. A sub‐population of amoebocytes express 185/333 proteins on the membranes of vesicles emanating from the trans‐Golgi and which later fuse with the plasma membranes of the cells. The previously uncharacterized gut‐associated amoebocytes also show a high level of 185/333 protein expression on their internal vesicles and plasma membranes. Colourless spherule cells contain 185/333 proteins within large spherules (specialized intracellular vesicles). In the presence of bacteria and yeast, the ultrastucture of colourless spherule cells changes and 185/333 proteins disappear. In contrast, 185/333 proteins were not found in the phagosomes of coelomocytes. The 185/333‐positive gut amoebocytes were often associated with anuclear bodies, which appeared to incorporate material of microbial origin that was surrounded by 185/333 proteins. 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In this study, we show that 185/333 proteins are expressed by three cell types: amoebocytes, colourless spherule cells and gut‐associated amoebocytes. A sub‐population of amoebocytes express 185/333 proteins on the membranes of vesicles emanating from the trans‐Golgi and which later fuse with the plasma membranes of the cells. The previously uncharacterized gut‐associated amoebocytes also show a high level of 185/333 protein expression on their internal vesicles and plasma membranes. Colourless spherule cells contain 185/333 proteins within large spherules (specialized intracellular vesicles). In the presence of bacteria and yeast, the ultrastucture of colourless spherule cells changes and 185/333 proteins disappear. In contrast, 185/333 proteins were not found in the phagosomes of coelomocytes. The 185/333‐positive gut amoebocytes were often associated with anuclear bodies, which appeared to incorporate material of microbial origin that was surrounded by 185/333 proteins. The association between 185/333 proteins on gut amoebocytes and anuclear bodies suggests that these proteins may be involved in the phagocytosis of microbes in the gut epithelium.</description><subject>185/333 proteins</subject><subject>Animals</subject><subject>Anthocidaris - immunology</subject><subject>Anthocidaris - metabolism</subject><subject>Anthocidaris - ultrastructure</subject><subject>Cell Membrane - immunology</subject><subject>coelomocytes</subject><subject>Cytoplasmic Vesicles - immunology</subject><subject>Cytoplasmic Vesicles - ultrastructure</subject><subject>Digestive System - immunology</subject><subject>Digestive System - metabolism</subject><subject>Intestinal Mucosa - immunology</subject><subject>Intestinal Mucosa - ultrastructure</subject><subject>intestine</subject><subject>invertebrate immunity</subject><subject>Life Sciences</subject><subject>Membrane Proteins - immunology</subject><subject>Membrane Proteins - metabolism</subject><subject>Phagocytes - immunology</subject><subject>Phagocytes - metabolism</subject><subject>Phagocytosis</subject><subject>sea urchin</subject><subject>transmission electron microscopy</subject><issn>0818-9641</issn><issn>1440-1711</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><recordid>eNp9kc1u1DAURi0EokNhwwMgSywqEJn6ZyZ2lmUETKVBbOjaunFuGldOPNhJUXgMnhhHU7pgwcrWvUdH39VHyGvO1pxJfelsvRaM87V8QlZ8s2EFV5w_JSumuS6qcsPPyIuU7hhjSmj5nJwJvlVKSLEiv2_8GCGNcbLjFMFTHyx49wtGFwYaWtq5287P9B6ig9oj5Xp7KaWkru-nAWnEdAxDQnqMYUQ3JOoGOnZIbUAf-mDnEdPiWWYJgU7Rdm74QPfoXbCuyd5EMc5jF8NthL6Hl-RZCz7hq4f3nNx8_vR9ty8O375c764OhZUVk0XdirJpkW1l3ZZVqVsNrGK8KetKNEwozRrBAAQgb7FiqhbbvADAVlVQSZDn5N3J24E3x-h6iLMJ4Mz-6mCWGZNKVXwj7nlmL05sPvPHhGk0vUsWvYcBw5RMDlSWLMfI5Nt_yLswxSEfYrjSGeK6ZJl6f6JsDClFbB8DcGaWUk0u1SylGpnhNw_Kqe6xeUT_tpgBfgJ-Oo_zf1Tm-uvu4_KV8g-0la0k</recordid><startdate>201111</startdate><enddate>201111</enddate><creator>Dheilly, Nolwenn M</creator><creator>Birch, Debra</creator><creator>Nair, Sham V</creator><creator>Raftos, David A</creator><general>Nature Publishing Group</general><general>Blackwell Science Ltd</general><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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>1XC</scope></search><sort><creationdate>201111</creationdate><title>Ultrastructural localization of highly variable 185/333 immune response proteins in the coelomocytes of the sea urchin, Heliocidaris erythrogramma</title><author>Dheilly, Nolwenn M ; Birch, Debra ; Nair, Sham V ; Raftos, David A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3903-bf26dfe053bf6968f8a0901d6b92d02780d20aa2ae1fe907b2592daaef79a93a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>185/333 proteins</topic><topic>Animals</topic><topic>Anthocidaris - immunology</topic><topic>Anthocidaris - metabolism</topic><topic>Anthocidaris - ultrastructure</topic><topic>Cell Membrane - immunology</topic><topic>coelomocytes</topic><topic>Cytoplasmic Vesicles - immunology</topic><topic>Cytoplasmic Vesicles - ultrastructure</topic><topic>Digestive System - immunology</topic><topic>Digestive System - metabolism</topic><topic>Intestinal Mucosa - immunology</topic><topic>Intestinal Mucosa - ultrastructure</topic><topic>intestine</topic><topic>invertebrate immunity</topic><topic>Life Sciences</topic><topic>Membrane Proteins - immunology</topic><topic>Membrane Proteins - metabolism</topic><topic>Phagocytes - immunology</topic><topic>Phagocytes - metabolism</topic><topic>Phagocytosis</topic><topic>sea urchin</topic><topic>transmission electron microscopy</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dheilly, Nolwenn M</creatorcontrib><creatorcontrib>Birch, Debra</creatorcontrib><creatorcontrib>Nair, Sham V</creatorcontrib><creatorcontrib>Raftos, David A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Immunology and cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dheilly, Nolwenn M</au><au>Birch, Debra</au><au>Nair, Sham V</au><au>Raftos, David A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ultrastructural localization of highly variable 185/333 immune response proteins in the coelomocytes of the sea urchin, Heliocidaris erythrogramma</atitle><jtitle>Immunology and cell biology</jtitle><addtitle>Immunol Cell Biol</addtitle><date>2011-11</date><risdate>2011</risdate><volume>89</volume><issue>8</issue><spage>861</spage><epage>869</epage><pages>861-869</pages><issn>0818-9641</issn><eissn>1440-1711</eissn><abstract>The 185/333 proteins of sea urchins represent a family of highly variable immune response molecules with unknown functions. In this study, we show that 185/333 proteins are expressed by three cell types: amoebocytes, colourless spherule cells and gut‐associated amoebocytes. A sub‐population of amoebocytes express 185/333 proteins on the membranes of vesicles emanating from the trans‐Golgi and which later fuse with the plasma membranes of the cells. The previously uncharacterized gut‐associated amoebocytes also show a high level of 185/333 protein expression on their internal vesicles and plasma membranes. Colourless spherule cells contain 185/333 proteins within large spherules (specialized intracellular vesicles). In the presence of bacteria and yeast, the ultrastucture of colourless spherule cells changes and 185/333 proteins disappear. In contrast, 185/333 proteins were not found in the phagosomes of coelomocytes. The 185/333‐positive gut amoebocytes were often associated with anuclear bodies, which appeared to incorporate material of microbial origin that was surrounded by 185/333 proteins. The association between 185/333 proteins on gut amoebocytes and anuclear bodies suggests that these proteins may be involved in the phagocytosis of microbes in the gut epithelium.</abstract><cop>United States</cop><pub>Nature Publishing Group</pub><pmid>21577232</pmid><doi>10.1038/icb.2011.3</doi><tpages>9</tpages></addata></record> |
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subjects | 185/333 proteins Animals Anthocidaris - immunology Anthocidaris - metabolism Anthocidaris - ultrastructure Cell Membrane - immunology coelomocytes Cytoplasmic Vesicles - immunology Cytoplasmic Vesicles - ultrastructure Digestive System - immunology Digestive System - metabolism Intestinal Mucosa - immunology Intestinal Mucosa - ultrastructure intestine invertebrate immunity Life Sciences Membrane Proteins - immunology Membrane Proteins - metabolism Phagocytes - immunology Phagocytes - metabolism Phagocytosis sea urchin transmission electron microscopy |
title | Ultrastructural localization of highly variable 185/333 immune response proteins in the coelomocytes of the sea urchin, Heliocidaris erythrogramma |
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