Characterization and ultrastructural localization of annexin VI from mitochondria
Annexin VI, a member of a family of related intracellular proteins that associate reversibly with membrane phospholipids in a Ca 2+-dependent manner, has been purified from bovine liver mitochondria and characterized. Moreover, biochemical and immunocytochemical lines of evidence are presented which...
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Veröffentlicht in: | FEBS letters 1995-02, Vol.360 (1), p.80-84 |
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creator | Rainteau, Dominique Mansuelle, Pascal Rochat, Hervé Weinman, Serge |
description | Annexin VI, a member of a family of related intracellular proteins that associate reversibly with membrane phospholipids in a Ca
2+-dependent manner, has been purified from bovine liver mitochondria and characterized. Moreover, biochemical and immunocytochemical lines of evidence are presented which strongly suggest that annexin VI is closely associated with the cristae in the inner membrane of mitochondria. These findings are consistent with a calcium channel activity of annexin VI in mitochondria. |
doi_str_mv | 10.1016/0014-5793(95)00087-P |
format | Article |
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2+-dependent manner, has been purified from bovine liver mitochondria and characterized. Moreover, biochemical and immunocytochemical lines of evidence are presented which strongly suggest that annexin VI is closely associated with the cristae in the inner membrane of mitochondria. These findings are consistent with a calcium channel activity of annexin VI in mitochondria.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(95)00087-P</identifier><identifier>PMID: 7875306</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Animals ; Annexin A6 - metabolism ; Annexin VI ; Calcium Channels - metabolism ; Cattle ; Chemical Sciences ; Hydrolysis ; Microscopy, Immunoelectron ; Mitochondria ; Mitochondria, Liver - metabolism ; Mitochondria, Liver - ultrastructure ; Molecular Sequence Data ; Organic chemistry ; Rats ; Sequence Homology, Amino Acid</subject><ispartof>FEBS letters, 1995-02, Vol.360 (1), p.80-84</ispartof><rights>1995</rights><rights>FEBS Letters 360 (1995) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c531P-5e0d5c8a810dcf1e84c3a4b3698d10230167765e3739d4407d5dfc0b4c3d7d173</citedby><cites>FETCH-LOGICAL-c531P-5e0d5c8a810dcf1e84c3a4b3698d10230167765e3739d4407d5dfc0b4c3d7d173</cites><orcidid>0000-0001-8571-5045</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(95)00087-P$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7875306$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00815412$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Rainteau, Dominique</creatorcontrib><creatorcontrib>Mansuelle, Pascal</creatorcontrib><creatorcontrib>Rochat, Hervé</creatorcontrib><creatorcontrib>Weinman, Serge</creatorcontrib><title>Characterization and ultrastructural localization of annexin VI from mitochondria</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Annexin VI, a member of a family of related intracellular proteins that associate reversibly with membrane phospholipids in a Ca
2+-dependent manner, has been purified from bovine liver mitochondria and characterized. Moreover, biochemical and immunocytochemical lines of evidence are presented which strongly suggest that annexin VI is closely associated with the cristae in the inner membrane of mitochondria. These findings are consistent with a calcium channel activity of annexin VI in mitochondria.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Annexin A6 - metabolism</subject><subject>Annexin VI</subject><subject>Calcium Channels - metabolism</subject><subject>Cattle</subject><subject>Chemical Sciences</subject><subject>Hydrolysis</subject><subject>Microscopy, Immunoelectron</subject><subject>Mitochondria</subject><subject>Mitochondria, Liver - metabolism</subject><subject>Mitochondria, Liver - ultrastructure</subject><subject>Molecular Sequence Data</subject><subject>Organic chemistry</subject><subject>Rats</subject><subject>Sequence Homology, Amino Acid</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUFv1DAQhS0EKtvCPwApJ0QPAc86zjgXpHbVpZVWYpGAq-W1Ha2RExc7KZRfX6dZ9gicLL355nlmHiGvgL4DCvV7SqEqOTbsbcPPKaUCy-0TsgCBrGRVLZ6SxRF5Tk5T-p4hENCckBMUyBmtF-Tzaq-i0oON7rcaXOgL1Zti9ENUaYijHsaofOGDVv4PENrM9PaX64tvN0UbQ1d0bgh6H3oTnXpBnrXKJ_vy8J6Rr-urL6vrcvPp483qYlNqzmBbcksN10IJoEa3YEWlmap2rG6EAbpkeUPEmluGrDFVRdFw02q6y5hBA8jOyPnsu1de3kbXqXgvg3Ly-mIjJy1fBHgFyzvI7JuZvY3hx2jTIDuXtPVe9TaMSSIC5yjoP0FAyrBGlsFqBnUMKUXbHkcAKqd45HR7Od1eNlw-xiO3ue31wX_cddYcmw555Pp6rv903t7_l6dcX10up8KkN_xRnT76MBvZHMGds1Em7WyvrXHR6kGa4P4-6QM3zbGt</recordid><startdate>19950220</startdate><enddate>19950220</enddate><creator>Rainteau, Dominique</creator><creator>Mansuelle, Pascal</creator><creator>Rochat, Hervé</creator><creator>Weinman, Serge</creator><general>Elsevier B.V</general><general>Wiley</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>7QP</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0001-8571-5045</orcidid></search><sort><creationdate>19950220</creationdate><title>Characterization and ultrastructural localization of annexin VI from mitochondria</title><author>Rainteau, Dominique ; Mansuelle, Pascal ; Rochat, Hervé ; Weinman, Serge</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c531P-5e0d5c8a810dcf1e84c3a4b3698d10230167765e3739d4407d5dfc0b4c3d7d173</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Annexin A6 - metabolism</topic><topic>Annexin VI</topic><topic>Calcium Channels - metabolism</topic><topic>Cattle</topic><topic>Chemical Sciences</topic><topic>Hydrolysis</topic><topic>Microscopy, Immunoelectron</topic><topic>Mitochondria</topic><topic>Mitochondria, Liver - metabolism</topic><topic>Mitochondria, Liver - ultrastructure</topic><topic>Molecular Sequence Data</topic><topic>Organic chemistry</topic><topic>Rats</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rainteau, Dominique</creatorcontrib><creatorcontrib>Mansuelle, Pascal</creatorcontrib><creatorcontrib>Rochat, Hervé</creatorcontrib><creatorcontrib>Weinman, Serge</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>Calcium & Calcified Tissue Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rainteau, Dominique</au><au>Mansuelle, Pascal</au><au>Rochat, Hervé</au><au>Weinman, Serge</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization and ultrastructural localization of annexin VI from mitochondria</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1995-02-20</date><risdate>1995</risdate><volume>360</volume><issue>1</issue><spage>80</spage><epage>84</epage><pages>80-84</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Annexin VI, a member of a family of related intracellular proteins that associate reversibly with membrane phospholipids in a Ca
2+-dependent manner, has been purified from bovine liver mitochondria and characterized. Moreover, biochemical and immunocytochemical lines of evidence are presented which strongly suggest that annexin VI is closely associated with the cristae in the inner membrane of mitochondria. These findings are consistent with a calcium channel activity of annexin VI in mitochondria.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>7875306</pmid><doi>10.1016/0014-5793(95)00087-P</doi><tpages>5</tpages><orcidid>https://orcid.org/0000-0001-8571-5045</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Animals Annexin A6 - metabolism Annexin VI Calcium Channels - metabolism Cattle Chemical Sciences Hydrolysis Microscopy, Immunoelectron Mitochondria Mitochondria, Liver - metabolism Mitochondria, Liver - ultrastructure Molecular Sequence Data Organic chemistry Rats Sequence Homology, Amino Acid |
title | Characterization and ultrastructural localization of annexin VI from mitochondria |
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