Analysis of biochemical features of ST8 α-N-acetyl-neuraminide α2,8-sialyltransferase (St8sia) 5 isoforms
Gangliosides are important components of the membrane and are involved in many biological activities. St8sia5 is an α2,8-sialyltransferase involved in ganglioside synthesis, and has three isoforms. In this study, we analyzed the features of three isoforms, St8sia5-S, -M, and -L that had not been ana...
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| Veröffentlicht in: | Glycoconjugate journal 2022-04, Vol.39 (2), p.291-302 |
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| container_title | Glycoconjugate journal |
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| creator | Araki, Erino Hane, Masaya Hatanaka, Rina Kimura, Ryota Tsuda, Kana Konishi, Miku Komura, Naoko Ando, Hiromune Kitajima, Ken Sato, Chihiro |
| description | Gangliosides are important components of the membrane and are involved in many biological activities. St8sia5 is an α2,8-sialyltransferase involved in ganglioside synthesis, and has three isoforms. In this study, we analyzed the features of three isoforms, St8sia5-S, -M, and -L that had not been analyzed, and found that only St8sia5-L was localized in the Golgi, while the majority of St8sia5-M and -S were localized in the ER. The localization of Golgi of St8sia5 depended on the stem region. In addition, the incorporation of exogenous GD3 was upregulated only in St8sia5-L expressing cells. Taken together, the localization of St8sia5 is important for the activity of the enzyme. |
| doi_str_mv | 10.1007/s10719-021-10034-8 |
| format | Article |
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St8sia5 is an α2,8-sialyltransferase involved in ganglioside synthesis, and has three isoforms. In this study, we analyzed the features of three isoforms, St8sia5-S, -M, and -L that had not been analyzed, and found that only St8sia5-L was localized in the Golgi, while the majority of St8sia5-M and -S were localized in the ER. The localization of Golgi of St8sia5 depended on the stem region. In addition, the incorporation of exogenous GD3 was upregulated only in St8sia5-L expressing cells. Taken together, the localization of St8sia5 is important for the activity of the enzyme.</description><identifier>ISSN: 0282-0080</identifier><identifier>EISSN: 1573-4986</identifier><identifier>DOI: 10.1007/s10719-021-10034-8</identifier><identifier>PMID: 34982351</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Animals ; Biochemistry ; Biomedical and Life Sciences ; Gangliosides ; Gangliosides - metabolism ; Golgi apparatus ; Golgi Apparatus - metabolism ; Isoforms ; Life Sciences ; Localization ; Mice ; Original Article ; Pathology ; Protein Isoforms - genetics ; Sialyltransferases - genetics ; Sialyltransferases - metabolism ; Tribute to Professor Sen-itiroh Hakomori</subject><ispartof>Glycoconjugate journal, 2022-04, Vol.39 (2), p.291-302</ispartof><rights>The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2021</rights><rights>2021. 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Taken together, the localization of St8sia5 is important for the activity of the enzyme.</description><subject>Animals</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Gangliosides</subject><subject>Gangliosides - metabolism</subject><subject>Golgi apparatus</subject><subject>Golgi Apparatus - metabolism</subject><subject>Isoforms</subject><subject>Life Sciences</subject><subject>Localization</subject><subject>Mice</subject><subject>Original Article</subject><subject>Pathology</subject><subject>Protein Isoforms - genetics</subject><subject>Sialyltransferases - genetics</subject><subject>Sialyltransferases - metabolism</subject><subject>Tribute to Professor Sen-itiroh Hakomori</subject><issn>0282-0080</issn><issn>1573-4986</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp9kctuFDEQRS0EIkPgB1iglrIJUgxlux_2chTlJUWwmGFtud1l4tCPxNW9mM_iR_gmnEwIEgtWpbo-91qqy9h7AZ8EQPOZBDTCcJCC512VXL9gK1E1ipdG1y_ZCqSWHEDDAXtDdAvZVEr9mh2oDEhViRX7sR5dv6NIxRSKNk7-BofoXV8EdPOS8FHfbHXx6yf_wp3HedfzEZfkhjjGDrMuTzSnmFP6ObmRAiZHWBxvZp3Vj0VVRJrClAZ6y14F1xO-e5qH7Nv52fb0kl9_vbg6XV9zLw1oXobOCO-gkZUxZSNlCEIrpSAEha1zSphGa5Det62Roq7Qtx0GXdadqGow6pAd73Pv0nS_IM12iOSx792I00JW1tlkKgN1Ro_-QW-nJeWTPFBlY8raaJEpuad8mogSBnuX4uDSzgqwD1XYfRU2V2Efq7A6mz48RS_tgN2z5c_tM6D2AOWn8Tumv3__J_Y3hnKTyg</recordid><startdate>20220401</startdate><enddate>20220401</enddate><creator>Araki, Erino</creator><creator>Hane, Masaya</creator><creator>Hatanaka, Rina</creator><creator>Kimura, Ryota</creator><creator>Tsuda, Kana</creator><creator>Konishi, Miku</creator><creator>Komura, Naoko</creator><creator>Ando, Hiromune</creator><creator>Kitajima, Ken</creator><creator>Sato, Chihiro</creator><general>Springer US</general><general>Springer Nature B.V</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>7T5</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</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>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20220401</creationdate><title>Analysis of biochemical features of ST8 α-N-acetyl-neuraminide α2,8-sialyltransferase (St8sia) 5 isoforms</title><author>Araki, Erino ; Hane, Masaya ; Hatanaka, Rina ; Kimura, Ryota ; Tsuda, Kana ; Konishi, Miku ; Komura, Naoko ; Ando, Hiromune ; Kitajima, Ken ; Sato, Chihiro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2908-4fd91ca0725994722ff183330ff3ebaa31978802ccbb92165ecbdef846d156093</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Animals</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Gangliosides</topic><topic>Gangliosides - metabolism</topic><topic>Golgi apparatus</topic><topic>Golgi Apparatus - metabolism</topic><topic>Isoforms</topic><topic>Life Sciences</topic><topic>Localization</topic><topic>Mice</topic><topic>Original Article</topic><topic>Pathology</topic><topic>Protein Isoforms - genetics</topic><topic>Sialyltransferases - genetics</topic><topic>Sialyltransferases - metabolism</topic><topic>Tribute to Professor Sen-itiroh Hakomori</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Araki, Erino</creatorcontrib><creatorcontrib>Hane, Masaya</creatorcontrib><creatorcontrib>Hatanaka, Rina</creatorcontrib><creatorcontrib>Kimura, Ryota</creatorcontrib><creatorcontrib>Tsuda, Kana</creatorcontrib><creatorcontrib>Konishi, Miku</creatorcontrib><creatorcontrib>Komura, Naoko</creatorcontrib><creatorcontrib>Ando, Hiromune</creatorcontrib><creatorcontrib>Kitajima, Ken</creatorcontrib><creatorcontrib>Sato, Chihiro</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>Immunology Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</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 Edition)</collection><collection>ProQuest Central UK/Ireland</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>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science 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>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Glycoconjugate journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Araki, Erino</au><au>Hane, Masaya</au><au>Hatanaka, Rina</au><au>Kimura, Ryota</au><au>Tsuda, Kana</au><au>Konishi, Miku</au><au>Komura, Naoko</au><au>Ando, Hiromune</au><au>Kitajima, Ken</au><au>Sato, Chihiro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of biochemical features of ST8 α-N-acetyl-neuraminide α2,8-sialyltransferase (St8sia) 5 isoforms</atitle><jtitle>Glycoconjugate journal</jtitle><stitle>Glycoconj J</stitle><addtitle>Glycoconj J</addtitle><date>2022-04-01</date><risdate>2022</risdate><volume>39</volume><issue>2</issue><spage>291</spage><epage>302</epage><pages>291-302</pages><issn>0282-0080</issn><eissn>1573-4986</eissn><abstract>Gangliosides are important components of the membrane and are involved in many biological activities. St8sia5 is an α2,8-sialyltransferase involved in ganglioside synthesis, and has three isoforms. In this study, we analyzed the features of three isoforms, St8sia5-S, -M, and -L that had not been analyzed, and found that only St8sia5-L was localized in the Golgi, while the majority of St8sia5-M and -S were localized in the ER. The localization of Golgi of St8sia5 depended on the stem region. In addition, the incorporation of exogenous GD3 was upregulated only in St8sia5-L expressing cells. Taken together, the localization of St8sia5 is important for the activity of the enzyme.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>34982351</pmid><doi>10.1007/s10719-021-10034-8</doi><tpages>12</tpages></addata></record> |
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| subjects | Animals Biochemistry Biomedical and Life Sciences Gangliosides Gangliosides - metabolism Golgi apparatus Golgi Apparatus - metabolism Isoforms Life Sciences Localization Mice Original Article Pathology Protein Isoforms - genetics Sialyltransferases - genetics Sialyltransferases - metabolism Tribute to Professor Sen-itiroh Hakomori |
| title | Analysis of biochemical features of ST8 α-N-acetyl-neuraminide α2,8-sialyltransferase (St8sia) 5 isoforms |
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