Cross-Linking of Plasmalemmal Cholesterol in Lymphocytes Induces Capping, Membrane Shedding, and Endocytosis through Coated Pits
By use of a nicked and biotinylated perfringolysin O (BCθ), which binds to cholesterol specifically, we studied consequences of cross-linking cholesterol in lymphocytes. When bound with BCθ and then with labeled avidin or streptavidin, capping occurred in most cells within 30 min at 37°C. It was inh...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1999-07, Vol.260 (2), p.516-521 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Hagiwara, Haruo Kogure, Shin-ya Nakamura, Megumi Shimada, Yukiko Ohno-Iwashita, Yoshiko Fujimoto, Toyoshi |
| description | By use of a nicked and biotinylated perfringolysin O (BCθ), which binds to cholesterol specifically, we studied consequences of cross-linking cholesterol in lymphocytes. When bound with BCθ and then with labeled avidin or streptavidin, capping occurred in most cells within 30 min at 37°C. It was inhibited by cytochalasin D or NaN3, but not by nocodazole. When BCθ-cholesterol was capped, Thy-1 and transferrin receptor, a GPI-anchored protein and a transmembrane protein, respectively, remained evenly distributed. By fluorescence and electron microscopy, a cluster of small vesicles bound with BCθ were observed in the cap. They were then shed in the medium or internalized through coated pits. The result indicates that cross-linking of cholesterol in lymphocytes induces capping, but does not affect distribution of membrane proteins, and that the capped cholesterol molecules are either shed as vesicles or endocytosed. |
| doi_str_mv | 10.1006/bbrc.1999.0879 |
| format | Article |
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When bound with BCθ and then with labeled avidin or streptavidin, capping occurred in most cells within 30 min at 37°C. It was inhibited by cytochalasin D or NaN3, but not by nocodazole. When BCθ-cholesterol was capped, Thy-1 and transferrin receptor, a GPI-anchored protein and a transmembrane protein, respectively, remained evenly distributed. By fluorescence and electron microscopy, a cluster of small vesicles bound with BCθ were observed in the cap. They were then shed in the medium or internalized through coated pits. 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When bound with BCθ and then with labeled avidin or streptavidin, capping occurred in most cells within 30 min at 37°C. It was inhibited by cytochalasin D or NaN3, but not by nocodazole. When BCθ-cholesterol was capped, Thy-1 and transferrin receptor, a GPI-anchored protein and a transmembrane protein, respectively, remained evenly distributed. By fluorescence and electron microscopy, a cluster of small vesicles bound with BCθ were observed in the cap. They were then shed in the medium or internalized through coated pits. The result indicates that cross-linking of cholesterol in lymphocytes induces capping, but does not affect distribution of membrane proteins, and that the capped cholesterol molecules are either shed as vesicles or endocytosed.</description><subject>Animals</subject><subject>capping</subject><subject>Cell Membrane - metabolism</subject><subject>Cells, Cultured</subject><subject>cholesterol</subject><subject>Cholesterol - chemistry</subject><subject>Cholesterol - metabolism</subject><subject>coated pit</subject><subject>Coated Pits, Cell-Membrane - metabolism</subject><subject>Endocytosis</subject><subject>Humans</subject><subject>Jurkat Cells</subject><subject>lymphocyte</subject><subject>Lymphocytes - drug effects</subject><subject>Lymphocytes - metabolism</subject><subject>Lymphocytes - ultrastructure</subject><subject>Mice</subject><subject>Microscopy, Electron</subject><subject>shedding</subject><subject>Spectrometry, Fluorescence</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1v1DAQhi0EotvCtUfkE6dmGWfzYR9R1C9pq1YCJG6WY48blyQOdoK0N356nW4PXLh4pPHzjmYeQs4ZbBlA9aVtg94yIcQWeC3ekA0DAVnOoHhLNpCILBfs5wk5jfEJgLGiEu_JSfqGXS3Ehvxtgo8x27vxlxsfqbf0oVdxUD0O6aFN53uMMwbfUzfS_WGYOq8PM0Z6O5pFp9qoaUrRC3qHQxvUiPRbh8a8tNRo6OVo1oSPLtK5C3557Gjj1YyGPrg5fiDvrOojfnytZ-TH1eX35ibb31_fNl_3md4VMGcsF1DyFm3JK83zygrguQKrQVVlgXVpW6h5UQhVJxBKW9nSWlUVNaYGb3dn5PNx7hT87yXdJAcXNfZ92tgvUVaCiwIES-D2COrVTEArp-AGFQ6SgVydy9W5XJ3L1XkKfHqdvLQDmn_wo-QE8COA6b4_DoOM2uGo0biAepbGu__NfgbmEpG8</recordid><startdate>19990705</startdate><enddate>19990705</enddate><creator>Hagiwara, Haruo</creator><creator>Kogure, Shin-ya</creator><creator>Nakamura, Megumi</creator><creator>Shimada, Yukiko</creator><creator>Ohno-Iwashita, Yoshiko</creator><creator>Fujimoto, Toyoshi</creator><general>Elsevier Inc</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>7X8</scope></search><sort><creationdate>19990705</creationdate><title>Cross-Linking of Plasmalemmal Cholesterol in Lymphocytes Induces Capping, Membrane Shedding, and Endocytosis through Coated Pits</title><author>Hagiwara, Haruo ; Kogure, Shin-ya ; Nakamura, Megumi ; Shimada, Yukiko ; Ohno-Iwashita, Yoshiko ; Fujimoto, Toyoshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c340t-129058bef586c826f9082a0fc0a654e75fb078449a790505f6f5ffa647e7908b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Animals</topic><topic>capping</topic><topic>Cell Membrane - metabolism</topic><topic>Cells, Cultured</topic><topic>cholesterol</topic><topic>Cholesterol - chemistry</topic><topic>Cholesterol - metabolism</topic><topic>coated pit</topic><topic>Coated Pits, Cell-Membrane - metabolism</topic><topic>Endocytosis</topic><topic>Humans</topic><topic>Jurkat Cells</topic><topic>lymphocyte</topic><topic>Lymphocytes - drug effects</topic><topic>Lymphocytes - metabolism</topic><topic>Lymphocytes - ultrastructure</topic><topic>Mice</topic><topic>Microscopy, Electron</topic><topic>shedding</topic><topic>Spectrometry, Fluorescence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hagiwara, Haruo</creatorcontrib><creatorcontrib>Kogure, Shin-ya</creatorcontrib><creatorcontrib>Nakamura, Megumi</creatorcontrib><creatorcontrib>Shimada, Yukiko</creatorcontrib><creatorcontrib>Ohno-Iwashita, Yoshiko</creatorcontrib><creatorcontrib>Fujimoto, Toyoshi</creatorcontrib><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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hagiwara, Haruo</au><au>Kogure, Shin-ya</au><au>Nakamura, Megumi</au><au>Shimada, Yukiko</au><au>Ohno-Iwashita, Yoshiko</au><au>Fujimoto, Toyoshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cross-Linking of Plasmalemmal Cholesterol in Lymphocytes Induces Capping, Membrane Shedding, and Endocytosis through Coated Pits</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1999-07-05</date><risdate>1999</risdate><volume>260</volume><issue>2</issue><spage>516</spage><epage>521</epage><pages>516-521</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>By use of a nicked and biotinylated perfringolysin O (BCθ), which binds to cholesterol specifically, we studied consequences of cross-linking cholesterol in lymphocytes. When bound with BCθ and then with labeled avidin or streptavidin, capping occurred in most cells within 30 min at 37°C. It was inhibited by cytochalasin D or NaN3, but not by nocodazole. When BCθ-cholesterol was capped, Thy-1 and transferrin receptor, a GPI-anchored protein and a transmembrane protein, respectively, remained evenly distributed. By fluorescence and electron microscopy, a cluster of small vesicles bound with BCθ were observed in the cap. They were then shed in the medium or internalized through coated pits. The result indicates that cross-linking of cholesterol in lymphocytes induces capping, but does not affect distribution of membrane proteins, and that the capped cholesterol molecules are either shed as vesicles or endocytosed.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10403799</pmid><doi>10.1006/bbrc.1999.0879</doi><tpages>6</tpages></addata></record> |
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| subjects | Animals capping Cell Membrane - metabolism Cells, Cultured cholesterol Cholesterol - chemistry Cholesterol - metabolism coated pit Coated Pits, Cell-Membrane - metabolism Endocytosis Humans Jurkat Cells lymphocyte Lymphocytes - drug effects Lymphocytes - metabolism Lymphocytes - ultrastructure Mice Microscopy, Electron shedding Spectrometry, Fluorescence |
| title | Cross-Linking of Plasmalemmal Cholesterol in Lymphocytes Induces Capping, Membrane Shedding, and Endocytosis through Coated Pits |
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