The expression of the abnormal human red cell anion transporter from South-East Asian ovalocytes (band 3 SAO) in Xenopus oocytes
South-East Asian ovalocytosis (SAO) is caused by the heterozygous presence of a variant form of the human erythrocyte anion transporter (band 3; AE1). The expression of band 3 SAO has been studied in Xenopus oocytes. Band 3 SAO is not functional as an anion transporter but is inserted stably into th...
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Veröffentlicht in: | FEBS letters 1993-09, Vol.330 (2), p.186-190 |
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description | South-East Asian ovalocytosis (SAO) is caused by the heterozygous presence of a variant form of the human erythrocyte anion transporter (band 3; AE1). The expression of band 3 SAO has been studied in
Xenopus oocytes. Band 3 SAO is not functional as an anion transporter but is inserted stably into the plasma membrane of oocytes. Band 3 SAO translocation to the cell surface does not require co-expression of normal band 3. Co-expression of glycophorin A (GPA) increases the rate of translocation of band 3 SAO to the oocyte membrane but is not essential for this process. We suggest that the increased tendency of band 3 SAO to form oligomers may facilitate its translocation to the cell surface. |
doi_str_mv | 10.1016/0014-5793(93)80270-5 |
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Xenopus oocytes. Band 3 SAO is not functional as an anion transporter but is inserted stably into the plasma membrane of oocytes. Band 3 SAO translocation to the cell surface does not require co-expression of normal band 3. Co-expression of glycophorin A (GPA) increases the rate of translocation of band 3 SAO to the oocyte membrane but is not essential for this process. We suggest that the increased tendency of band 3 SAO to form oligomers may facilitate its translocation to the cell surface.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(93)80270-5</identifier><identifier>PMID: 7689982</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Anemias. Hemoglobinopathies ; Animals ; Anion Exchange Protein 1, Erythrocyte - genetics ; Anion Exchange Protein 1, Erythrocyte - metabolism ; Anion transporter ; BADS, 4-benzamido-4'-aminostilbene-2,2'-disulphonate ; Band 3 ; Base Sequence ; Biological and medical sciences ; Biological Transport ; Cell Membrane - metabolism ; Cloning, Molecular ; DIDS, 4,4'-diisothiocyanato-2,2'-stilbene disulphonate ; Diseases of red blood cells ; DNA ; DNDS, 4,4'-dinitrostilbene-2,2'-disulphonate ; Elliptocytosis, Hereditary - genetics ; Freshwater ; Glycophorin - genetics ; Glycophorin - metabolism ; Glycophorin A ; GPA, glycophorin A ; Hematologic and hematopoietic diseases ; Hereditary ovalocytosis ; Humans ; Medical sciences ; Molecular Sequence Data ; Oocytes ; Precipitin Tests ; RNA - genetics ; RNA - metabolism ; RNA, Complementary ; SAO, South-East Asian hereditary ovalocytosis ; Sequence Deletion ; Xenopus ; Xenopus oocyte</subject><ispartof>FEBS letters, 1993-09, Vol.330 (2), p.186-190</ispartof><rights>1993</rights><rights>FEBS Letters 330 (1993) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6215-ea2b8fc36eb61fc177a4b92aa3836b2965d61287b64f83d4db203a0b247d0b2a3</citedby><cites>FETCH-LOGICAL-c6215-ea2b8fc36eb61fc177a4b92aa3836b2965d61287b64f83d4db203a0b247d0b2a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0014579393802705$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3755334$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7689982$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Groves, Jonathan D.</creatorcontrib><creatorcontrib>Ring, Susan M.</creatorcontrib><creatorcontrib>Schofield, Ann E.</creatorcontrib><creatorcontrib>Tanner, Michael J.A.</creatorcontrib><title>The expression of the abnormal human red cell anion transporter from South-East Asian ovalocytes (band 3 SAO) in Xenopus oocytes</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>South-East Asian ovalocytosis (SAO) is caused by the heterozygous presence of a variant form of the human erythrocyte anion transporter (band 3; AE1). The expression of band 3 SAO has been studied in
Xenopus oocytes. Band 3 SAO is not functional as an anion transporter but is inserted stably into the plasma membrane of oocytes. Band 3 SAO translocation to the cell surface does not require co-expression of normal band 3. Co-expression of glycophorin A (GPA) increases the rate of translocation of band 3 SAO to the oocyte membrane but is not essential for this process. We suggest that the increased tendency of band 3 SAO to form oligomers may facilitate its translocation to the cell surface.</description><subject>Anemias. Hemoglobinopathies</subject><subject>Animals</subject><subject>Anion Exchange Protein 1, Erythrocyte - genetics</subject><subject>Anion Exchange Protein 1, Erythrocyte - metabolism</subject><subject>Anion transporter</subject><subject>BADS, 4-benzamido-4'-aminostilbene-2,2'-disulphonate</subject><subject>Band 3</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biological Transport</subject><subject>Cell Membrane - metabolism</subject><subject>Cloning, Molecular</subject><subject>DIDS, 4,4'-diisothiocyanato-2,2'-stilbene disulphonate</subject><subject>Diseases of red blood cells</subject><subject>DNA</subject><subject>DNDS, 4,4'-dinitrostilbene-2,2'-disulphonate</subject><subject>Elliptocytosis, Hereditary - genetics</subject><subject>Freshwater</subject><subject>Glycophorin - genetics</subject><subject>Glycophorin - metabolism</subject><subject>Glycophorin A</subject><subject>GPA, glycophorin A</subject><subject>Hematologic and hematopoietic diseases</subject><subject>Hereditary ovalocytosis</subject><subject>Humans</subject><subject>Medical sciences</subject><subject>Molecular Sequence Data</subject><subject>Oocytes</subject><subject>Precipitin Tests</subject><subject>RNA - genetics</subject><subject>RNA - metabolism</subject><subject>RNA, Complementary</subject><subject>SAO, South-East Asian hereditary ovalocytosis</subject><subject>Sequence Deletion</subject><subject>Xenopus</subject><subject>Xenopus oocyte</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1v1DAQhi0EKkvhH4DkA0LtIeCv2M6l0lLtAlKlHlokbpbjTLRGib3YSWFv_HSSZrVHQLJsed5nZux3EHpNyXtKqPxACBVFqSp-UfFLTZgiRfkErahWvOBC6qdodUKeoxc5fyfTXdPqDJ0pqatKsxX6fb8DDL_2CXL2MeDY4mGK2DrE1NsO78beBpygwQ66DtswQ0OyIe9jGiDhNsUe38Vx2BUbmwe8zn5KiA-2i-4wQMYXtQ0N5vhufXuJfcDfIMT9mHFc9JfoWWu7DK-O5zn6ut3cX38ubm4_fble3xROMloWYFmtW8cl1JK2jiplRV0xa7nmsmaVLBtJmVa1FK3mjWhqRrglNROqmXbLz9G7pe4-xR8j5MH0Ps9_sgHimI0qK0GUkP8EqVSaEyImUCygSzHnBK3ZJ9_bdDCUmHlCZrbfzPabaT1OyJRT2ptj_bHuoTklHUcy6W-Pus3Odu3ktfP5hHFVlpzP3bcL9tN3cPiv1ma7-chmYY5X_DE6v-dqKQST-w8eksnOQ3DQ-ARuME30f__QH7M6v-I</recordid><startdate>19930913</startdate><enddate>19930913</enddate><creator>Groves, Jonathan D.</creator><creator>Ring, Susan M.</creator><creator>Schofield, Ann E.</creator><creator>Tanner, Michael J.A.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</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>7TM</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>19930913</creationdate><title>The expression of the abnormal human red cell anion transporter from South-East Asian ovalocytes (band 3 SAO) in Xenopus oocytes</title><author>Groves, Jonathan D. ; Ring, Susan M. ; Schofield, Ann E. ; Tanner, Michael J.A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6215-ea2b8fc36eb61fc177a4b92aa3836b2965d61287b64f83d4db203a0b247d0b2a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Anemias. Hemoglobinopathies</topic><topic>Animals</topic><topic>Anion Exchange Protein 1, Erythrocyte - genetics</topic><topic>Anion Exchange Protein 1, Erythrocyte - metabolism</topic><topic>Anion transporter</topic><topic>BADS, 4-benzamido-4'-aminostilbene-2,2'-disulphonate</topic><topic>Band 3</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biological Transport</topic><topic>Cell Membrane - metabolism</topic><topic>Cloning, Molecular</topic><topic>DIDS, 4,4'-diisothiocyanato-2,2'-stilbene disulphonate</topic><topic>Diseases of red blood cells</topic><topic>DNA</topic><topic>DNDS, 4,4'-dinitrostilbene-2,2'-disulphonate</topic><topic>Elliptocytosis, Hereditary - genetics</topic><topic>Freshwater</topic><topic>Glycophorin - genetics</topic><topic>Glycophorin - metabolism</topic><topic>Glycophorin A</topic><topic>GPA, glycophorin A</topic><topic>Hematologic and hematopoietic diseases</topic><topic>Hereditary ovalocytosis</topic><topic>Humans</topic><topic>Medical sciences</topic><topic>Molecular Sequence Data</topic><topic>Oocytes</topic><topic>Precipitin Tests</topic><topic>RNA - genetics</topic><topic>RNA - metabolism</topic><topic>RNA, Complementary</topic><topic>SAO, South-East Asian hereditary ovalocytosis</topic><topic>Sequence Deletion</topic><topic>Xenopus</topic><topic>Xenopus oocyte</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Groves, Jonathan D.</creatorcontrib><creatorcontrib>Ring, Susan M.</creatorcontrib><creatorcontrib>Schofield, Ann E.</creatorcontrib><creatorcontrib>Tanner, Michael J.A.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Groves, Jonathan D.</au><au>Ring, Susan M.</au><au>Schofield, Ann E.</au><au>Tanner, Michael J.A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The expression of the abnormal human red cell anion transporter from South-East Asian ovalocytes (band 3 SAO) in Xenopus oocytes</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1993-09-13</date><risdate>1993</risdate><volume>330</volume><issue>2</issue><spage>186</spage><epage>190</epage><pages>186-190</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>South-East Asian ovalocytosis (SAO) is caused by the heterozygous presence of a variant form of the human erythrocyte anion transporter (band 3; AE1). The expression of band 3 SAO has been studied in
Xenopus oocytes. Band 3 SAO is not functional as an anion transporter but is inserted stably into the plasma membrane of oocytes. Band 3 SAO translocation to the cell surface does not require co-expression of normal band 3. Co-expression of glycophorin A (GPA) increases the rate of translocation of band 3 SAO to the oocyte membrane but is not essential for this process. We suggest that the increased tendency of band 3 SAO to form oligomers may facilitate its translocation to the cell surface.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>7689982</pmid><doi>10.1016/0014-5793(93)80270-5</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Anemias. Hemoglobinopathies Animals Anion Exchange Protein 1, Erythrocyte - genetics Anion Exchange Protein 1, Erythrocyte - metabolism Anion transporter BADS, 4-benzamido-4'-aminostilbene-2,2'-disulphonate Band 3 Base Sequence Biological and medical sciences Biological Transport Cell Membrane - metabolism Cloning, Molecular DIDS, 4,4'-diisothiocyanato-2,2'-stilbene disulphonate Diseases of red blood cells DNA DNDS, 4,4'-dinitrostilbene-2,2'-disulphonate Elliptocytosis, Hereditary - genetics Freshwater Glycophorin - genetics Glycophorin - metabolism Glycophorin A GPA, glycophorin A Hematologic and hematopoietic diseases Hereditary ovalocytosis Humans Medical sciences Molecular Sequence Data Oocytes Precipitin Tests RNA - genetics RNA - metabolism RNA, Complementary SAO, South-East Asian hereditary ovalocytosis Sequence Deletion Xenopus Xenopus oocyte |
title | The expression of the abnormal human red cell anion transporter from South-East Asian ovalocytes (band 3 SAO) in Xenopus oocytes |
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