ABO blood group A transferase and its codon 69 substitution enzymes synthesize FORS1 antigen of FORS blood group system
Human histo-blood group A transferase (AT) catalyzes the biosynthesis of oligosaccharide A antigen important in blood transfusion and cell/tissue/organ transplantation. This enzyme may synthesize Forssman antigen (FORS1) of the FORS blood group system when exon 3 or 4 of the AT mRNA is deleted and/o...
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| description | Human histo-blood group A transferase (AT) catalyzes the biosynthesis of oligosaccharide A antigen important in blood transfusion and cell/tissue/organ transplantation. This enzyme may synthesize Forssman antigen (FORS1) of the FORS blood group system when exon 3 or 4 of the AT mRNA is deleted and/or the LeuGlyGly tripeptide at codons 266–268 of AT is replaced by GlyGlyAla. The Met69Ser/Thr substitutions also confer weak Forssman glycolipid synthase (FS) activity. In this study, we prepared the human AT derivative constructs containing any of the 20 amino acids at codon 69 with and without the GlyGlyAla substitution, transfected DNA to newly generated COS1(B3GALNT1 + A4GALT) cells expressing an enhanced level of globoside (Gb4), the FS acceptor substrate, and immunologically examined the FORS1 expression. Our results showed that all those substitution constructs at codon 69 exhibited FS activity. The combination with GlyGlyAla significantly increased the activity. The conserved methionine residue in the
ABO
, but not
GBGT1
, gene-encoded proteins may implicate its contribution to the separation of these genes in genetic evolution. Surprisingly, with increased Gb4 availability, the original human AT with the methionine residue at codon 69 was also demonstrated to synthesize FORS1, providing another molecular mechanism of FORS1 appearance in cancer of ordinary FORS1-negative individuals. |
| doi_str_mv | 10.1038/s41598-019-46029-7 |
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ABO
, but not
GBGT1
, gene-encoded proteins may implicate its contribution to the separation of these genes in genetic evolution. Surprisingly, with increased Gb4 availability, the original human AT with the methionine residue at codon 69 was also demonstrated to synthesize FORS1, providing another molecular mechanism of FORS1 appearance in cancer of ordinary FORS1-negative individuals.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/s41598-019-46029-7</identifier><identifier>PMID: 31273262</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>13 ; 13/1 ; 13/31 ; 13/51 ; 38 ; 38/109 ; 42 ; 42/35 ; 45 ; 631/208/248 ; 631/250/248 ; 631/45/221 ; 631/45/881 ; 631/80/221 ; 96/106 ; ABO Blood-Group System - genetics ; ABO Blood-Group System - metabolism ; ABO system ; Amino Acid Substitution ; Amino acids ; Antigens ; Antigens, Surface - genetics ; Antigens, Surface - metabolism ; Biosynthesis ; Blood group A ; Blood Group Antigens - genetics ; Blood Group Antigens - metabolism ; Blood groups ; Blood transfusion ; Codon ; Codons ; Evolution & development ; Evolutionary genetics ; Forssman antigen ; HeLa Cells ; Humanities and Social Sciences ; Humans ; Methionine ; mRNA ; multidisciplinary ; N-Acetylgalactosaminyltransferases - genetics ; N-Acetylgalactosaminyltransferases - metabolism ; Oligosaccharides ; Science ; Science (multidisciplinary) ; Transferases - genetics ; Transferases - metabolism ; Transplantation</subject><ispartof>Scientific reports, 2019-07, Vol.9 (1), p.9717-11, Article 9717</ispartof><rights>The Author(s) 2019</rights><rights>2019. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c511t-44f3545d03390b93d6b61034dd3f17da119ad6ffcfa9e0200fcc3e984ee240243</citedby><cites>FETCH-LOGICAL-c511t-44f3545d03390b93d6b61034dd3f17da119ad6ffcfa9e0200fcc3e984ee240243</cites><orcidid>0000-0001-9690-7034 ; 0000-0001-9516-1402 ; 0000-0002-5025-352X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6609624/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6609624/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27901,27902,41096,42165,51551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31273262$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yamamoto, Miyako</creatorcontrib><creatorcontrib>Tarasco, Maria Cristina</creatorcontrib><creatorcontrib>Cid, Emili</creatorcontrib><creatorcontrib>Kobayashi, Hidetomo</creatorcontrib><creatorcontrib>Yamamoto, Fumiichiro</creatorcontrib><title>ABO blood group A transferase and its codon 69 substitution enzymes synthesize FORS1 antigen of FORS blood group system</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Human histo-blood group A transferase (AT) catalyzes the biosynthesis of oligosaccharide A antigen important in blood transfusion and cell/tissue/organ transplantation. This enzyme may synthesize Forssman antigen (FORS1) of the FORS blood group system when exon 3 or 4 of the AT mRNA is deleted and/or the LeuGlyGly tripeptide at codons 266–268 of AT is replaced by GlyGlyAla. The Met69Ser/Thr substitutions also confer weak Forssman glycolipid synthase (FS) activity. In this study, we prepared the human AT derivative constructs containing any of the 20 amino acids at codon 69 with and without the GlyGlyAla substitution, transfected DNA to newly generated COS1(B3GALNT1 + A4GALT) cells expressing an enhanced level of globoside (Gb4), the FS acceptor substrate, and immunologically examined the FORS1 expression. Our results showed that all those substitution constructs at codon 69 exhibited FS activity. The combination with GlyGlyAla significantly increased the activity. The conserved methionine residue in the
ABO
, but not
GBGT1
, gene-encoded proteins may implicate its contribution to the separation of these genes in genetic evolution. Surprisingly, with increased Gb4 availability, the original human AT with the methionine residue at codon 69 was also demonstrated to synthesize FORS1, providing another molecular mechanism of FORS1 appearance in cancer of ordinary FORS1-negative individuals.</description><subject>13</subject><subject>13/1</subject><subject>13/31</subject><subject>13/51</subject><subject>38</subject><subject>38/109</subject><subject>42</subject><subject>42/35</subject><subject>45</subject><subject>631/208/248</subject><subject>631/250/248</subject><subject>631/45/221</subject><subject>631/45/881</subject><subject>631/80/221</subject><subject>96/106</subject><subject>ABO Blood-Group System - genetics</subject><subject>ABO Blood-Group System - metabolism</subject><subject>ABO system</subject><subject>Amino Acid Substitution</subject><subject>Amino acids</subject><subject>Antigens</subject><subject>Antigens, Surface - genetics</subject><subject>Antigens, Surface - metabolism</subject><subject>Biosynthesis</subject><subject>Blood group A</subject><subject>Blood Group Antigens - 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genetics</topic><topic>ABO Blood-Group System - metabolism</topic><topic>ABO system</topic><topic>Amino Acid Substitution</topic><topic>Amino acids</topic><topic>Antigens</topic><topic>Antigens, Surface - genetics</topic><topic>Antigens, Surface - metabolism</topic><topic>Biosynthesis</topic><topic>Blood group A</topic><topic>Blood Group Antigens - genetics</topic><topic>Blood Group Antigens - metabolism</topic><topic>Blood groups</topic><topic>Blood transfusion</topic><topic>Codon</topic><topic>Codons</topic><topic>Evolution & development</topic><topic>Evolutionary genetics</topic><topic>Forssman antigen</topic><topic>HeLa Cells</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>Methionine</topic><topic>mRNA</topic><topic>multidisciplinary</topic><topic>N-Acetylgalactosaminyltransferases - genetics</topic><topic>N-Acetylgalactosaminyltransferases - metabolism</topic><topic>Oligosaccharides</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Transferases - genetics</topic><topic>Transferases - metabolism</topic><topic>Transplantation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yamamoto, Miyako</creatorcontrib><creatorcontrib>Tarasco, Maria Cristina</creatorcontrib><creatorcontrib>Cid, Emili</creatorcontrib><creatorcontrib>Kobayashi, Hidetomo</creatorcontrib><creatorcontrib>Yamamoto, Fumiichiro</creatorcontrib><collection>Springer Nature OA Free Journals</collection><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>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science 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 Edition)</collection><collection>ProQuest One Sustainability</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>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>Publicly Available Content 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 Basic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yamamoto, Miyako</au><au>Tarasco, Maria Cristina</au><au>Cid, Emili</au><au>Kobayashi, Hidetomo</au><au>Yamamoto, Fumiichiro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ABO blood group A transferase and its codon 69 substitution enzymes synthesize FORS1 antigen of FORS blood group system</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2019-07-04</date><risdate>2019</risdate><volume>9</volume><issue>1</issue><spage>9717</spage><epage>11</epage><pages>9717-11</pages><artnum>9717</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Human histo-blood group A transferase (AT) catalyzes the biosynthesis of oligosaccharide A antigen important in blood transfusion and cell/tissue/organ transplantation. This enzyme may synthesize Forssman antigen (FORS1) of the FORS blood group system when exon 3 or 4 of the AT mRNA is deleted and/or the LeuGlyGly tripeptide at codons 266–268 of AT is replaced by GlyGlyAla. The Met69Ser/Thr substitutions also confer weak Forssman glycolipid synthase (FS) activity. In this study, we prepared the human AT derivative constructs containing any of the 20 amino acids at codon 69 with and without the GlyGlyAla substitution, transfected DNA to newly generated COS1(B3GALNT1 + A4GALT) cells expressing an enhanced level of globoside (Gb4), the FS acceptor substrate, and immunologically examined the FORS1 expression. Our results showed that all those substitution constructs at codon 69 exhibited FS activity. The combination with GlyGlyAla significantly increased the activity. The conserved methionine residue in the
ABO
, but not
GBGT1
, gene-encoded proteins may implicate its contribution to the separation of these genes in genetic evolution. Surprisingly, with increased Gb4 availability, the original human AT with the methionine residue at codon 69 was also demonstrated to synthesize FORS1, providing another molecular mechanism of FORS1 appearance in cancer of ordinary FORS1-negative individuals.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>31273262</pmid><doi>10.1038/s41598-019-46029-7</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0001-9690-7034</orcidid><orcidid>https://orcid.org/0000-0001-9516-1402</orcidid><orcidid>https://orcid.org/0000-0002-5025-352X</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 13 13/1 13/31 13/51 38 38/109 42 42/35 45 631/208/248 631/250/248 631/45/221 631/45/881 631/80/221 96/106 ABO Blood-Group System - genetics ABO Blood-Group System - metabolism ABO system Amino Acid Substitution Amino acids Antigens Antigens, Surface - genetics Antigens, Surface - metabolism Biosynthesis Blood group A Blood Group Antigens - genetics Blood Group Antigens - metabolism Blood groups Blood transfusion Codon Codons Evolution & development Evolutionary genetics Forssman antigen HeLa Cells Humanities and Social Sciences Humans Methionine mRNA multidisciplinary N-Acetylgalactosaminyltransferases - genetics N-Acetylgalactosaminyltransferases - metabolism Oligosaccharides Science Science (multidisciplinary) Transferases - genetics Transferases - metabolism Transplantation |
| title | ABO blood group A transferase and its codon 69 substitution enzymes synthesize FORS1 antigen of FORS blood group system |
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