D-Glutamate is metabolized in the heart mitochondria
D -Amino acids are enantiomers of L-amino acids and have recently been recognized as biomarkers and bioactive substances in mammals, including humans. In the present study, we investigated functions of the novel mammalian mitochondrial protein 9030617O03Rik and showed decreased expression under cond...
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| Veröffentlicht in: | Scientific reports 2017-03, Vol.7 (1), p.43911-43911, Article 43911 |
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| creator | Ariyoshi, Makoto Katane, Masumi Hamase, Kenji Miyoshi, Yurika Nakane, Maiko Hoshino, Atsushi Okawa, Yoshifumi Mita, Yuichiro Kaimoto, Satoshi Uchihashi, Motoki Fukai, Kuniyoshi Ono, Kazunori Tateishi, Syuhei Hato, Daichi Yamanaka, Ryoetsu Honda, Sakiko Fushimura, Yohei Iwai-Kanai, Eri Ishihara, Naotada Mita, Masashi Homma, Hiroshi Matoba, Satoaki |
| description | D
-Amino acids are enantiomers of L-amino acids and have recently been recognized as biomarkers and bioactive substances in mammals, including humans. In the present study, we investigated functions of the novel mammalian mitochondrial protein 9030617O03Rik and showed decreased expression under conditions of heart failure. Genomic sequence analyses showed partial homology with a bacterial aspartate/glutamate/hydantoin racemase. Subsequent determinations of all free amino acid concentrations in 9030617O03Rik-deficient mice showed high accumulations of D-glutamate in heart tissues. This is the first time that a significant amount of D-glutamate was detected in mammalian tissue. Further analysis of D-glutamate metabolism indicated that 9030617O03Rik is a D-glutamate cyclase that converts D-glutamate to 5-oxo-D-proline. Hence, this protein is the first identified enzyme responsible for mammalian D-glutamate metabolism, as confirmed in cloning analyses. These findings suggest that D-glutamate and 5-oxo-D-proline have bioactivities in mammals through the metabolism by D-glutamate cyclase. |
| doi_str_mv | 10.1038/srep43911 |
| format | Article |
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-Amino acids are enantiomers of L-amino acids and have recently been recognized as biomarkers and bioactive substances in mammals, including humans. In the present study, we investigated functions of the novel mammalian mitochondrial protein 9030617O03Rik and showed decreased expression under conditions of heart failure. Genomic sequence analyses showed partial homology with a bacterial aspartate/glutamate/hydantoin racemase. Subsequent determinations of all free amino acid concentrations in 9030617O03Rik-deficient mice showed high accumulations of D-glutamate in heart tissues. This is the first time that a significant amount of D-glutamate was detected in mammalian tissue. Further analysis of D-glutamate metabolism indicated that 9030617O03Rik is a D-glutamate cyclase that converts D-glutamate to 5-oxo-D-proline. Hence, this protein is the first identified enzyme responsible for mammalian D-glutamate metabolism, as confirmed in cloning analyses. These findings suggest that D-glutamate and 5-oxo-D-proline have bioactivities in mammals through the metabolism by D-glutamate cyclase.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep43911</identifier><identifier>PMID: 28266638</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/45/607/275 ; 64/60 ; 692/4019/592/75/230 ; 82/80 ; Amino acids ; Animals ; Cloning ; D-Glutamate cyclase ; Enantiomers ; Glutamic Acid - metabolism ; Heart diseases ; Homology ; Humanities and Social Sciences ; Hydro-Lyases - genetics ; Hydro-Lyases - metabolism ; Mammals ; Metabolism ; Mice ; Mice, Knockout ; Mitochondria ; Mitochondria, Heart - metabolism ; Mitochondrial Proteins - deficiency ; Mitochondrial Proteins - metabolism ; multidisciplinary ; Proline ; Pyrrolidonecarboxylic Acid - metabolism ; Rodents ; Science</subject><ispartof>Scientific reports, 2017-03, Vol.7 (1), p.43911-43911, Article 43911</ispartof><rights>The Author(s) 2017</rights><rights>Copyright Nature Publishing Group Mar 2017</rights><rights>Copyright © 2017, The Author(s) 2017 The Author(s)</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c588t-f11bff6cbcfa8f61a3f1003aeadb12630a7288ba15cdc5c87cf3f155f04379b43</citedby><cites>FETCH-LOGICAL-c588t-f11bff6cbcfa8f61a3f1003aeadb12630a7288ba15cdc5c87cf3f155f04379b43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5339696/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5339696/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,865,886,27929,27930,41125,42194,51581,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28266638$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ariyoshi, Makoto</creatorcontrib><creatorcontrib>Katane, Masumi</creatorcontrib><creatorcontrib>Hamase, Kenji</creatorcontrib><creatorcontrib>Miyoshi, Yurika</creatorcontrib><creatorcontrib>Nakane, Maiko</creatorcontrib><creatorcontrib>Hoshino, Atsushi</creatorcontrib><creatorcontrib>Okawa, Yoshifumi</creatorcontrib><creatorcontrib>Mita, Yuichiro</creatorcontrib><creatorcontrib>Kaimoto, Satoshi</creatorcontrib><creatorcontrib>Uchihashi, Motoki</creatorcontrib><creatorcontrib>Fukai, Kuniyoshi</creatorcontrib><creatorcontrib>Ono, Kazunori</creatorcontrib><creatorcontrib>Tateishi, Syuhei</creatorcontrib><creatorcontrib>Hato, Daichi</creatorcontrib><creatorcontrib>Yamanaka, Ryoetsu</creatorcontrib><creatorcontrib>Honda, Sakiko</creatorcontrib><creatorcontrib>Fushimura, Yohei</creatorcontrib><creatorcontrib>Iwai-Kanai, Eri</creatorcontrib><creatorcontrib>Ishihara, Naotada</creatorcontrib><creatorcontrib>Mita, Masashi</creatorcontrib><creatorcontrib>Homma, Hiroshi</creatorcontrib><creatorcontrib>Matoba, Satoaki</creatorcontrib><title>D-Glutamate is metabolized in the heart mitochondria</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>D
-Amino acids are enantiomers of L-amino acids and have recently been recognized as biomarkers and bioactive substances in mammals, including humans. In the present study, we investigated functions of the novel mammalian mitochondrial protein 9030617O03Rik and showed decreased expression under conditions of heart failure. Genomic sequence analyses showed partial homology with a bacterial aspartate/glutamate/hydantoin racemase. Subsequent determinations of all free amino acid concentrations in 9030617O03Rik-deficient mice showed high accumulations of D-glutamate in heart tissues. This is the first time that a significant amount of D-glutamate was detected in mammalian tissue. Further analysis of D-glutamate metabolism indicated that 9030617O03Rik is a D-glutamate cyclase that converts D-glutamate to 5-oxo-D-proline. Hence, this protein is the first identified enzyme responsible for mammalian D-glutamate metabolism, as confirmed in cloning analyses. These findings suggest that D-glutamate and 5-oxo-D-proline have bioactivities in mammals through the metabolism by D-glutamate cyclase.</description><subject>631/45/607/275</subject><subject>64/60</subject><subject>692/4019/592/75/230</subject><subject>82/80</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Cloning</subject><subject>D-Glutamate cyclase</subject><subject>Enantiomers</subject><subject>Glutamic Acid - metabolism</subject><subject>Heart diseases</subject><subject>Homology</subject><subject>Humanities and Social Sciences</subject><subject>Hydro-Lyases - genetics</subject><subject>Hydro-Lyases - metabolism</subject><subject>Mammals</subject><subject>Metabolism</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Mitochondria</subject><subject>Mitochondria, Heart - metabolism</subject><subject>Mitochondrial Proteins - deficiency</subject><subject>Mitochondrial Proteins - metabolism</subject><subject>multidisciplinary</subject><subject>Proline</subject><subject>Pyrrolidonecarboxylic Acid - 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Academic</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>Ariyoshi, Makoto</au><au>Katane, Masumi</au><au>Hamase, Kenji</au><au>Miyoshi, Yurika</au><au>Nakane, Maiko</au><au>Hoshino, Atsushi</au><au>Okawa, Yoshifumi</au><au>Mita, Yuichiro</au><au>Kaimoto, Satoshi</au><au>Uchihashi, Motoki</au><au>Fukai, Kuniyoshi</au><au>Ono, Kazunori</au><au>Tateishi, Syuhei</au><au>Hato, Daichi</au><au>Yamanaka, Ryoetsu</au><au>Honda, Sakiko</au><au>Fushimura, Yohei</au><au>Iwai-Kanai, Eri</au><au>Ishihara, Naotada</au><au>Mita, Masashi</au><au>Homma, Hiroshi</au><au>Matoba, Satoaki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>D-Glutamate is metabolized in the heart mitochondria</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2017-03-07</date><risdate>2017</risdate><volume>7</volume><issue>1</issue><spage>43911</spage><epage>43911</epage><pages>43911-43911</pages><artnum>43911</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>D
-Amino acids are enantiomers of L-amino acids and have recently been recognized as biomarkers and bioactive substances in mammals, including humans. In the present study, we investigated functions of the novel mammalian mitochondrial protein 9030617O03Rik and showed decreased expression under conditions of heart failure. Genomic sequence analyses showed partial homology with a bacterial aspartate/glutamate/hydantoin racemase. Subsequent determinations of all free amino acid concentrations in 9030617O03Rik-deficient mice showed high accumulations of D-glutamate in heart tissues. This is the first time that a significant amount of D-glutamate was detected in mammalian tissue. Further analysis of D-glutamate metabolism indicated that 9030617O03Rik is a D-glutamate cyclase that converts D-glutamate to 5-oxo-D-proline. Hence, this protein is the first identified enzyme responsible for mammalian D-glutamate metabolism, as confirmed in cloning analyses. These findings suggest that D-glutamate and 5-oxo-D-proline have bioactivities in mammals through the metabolism by D-glutamate cyclase.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>28266638</pmid><doi>10.1038/srep43911</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| source | Nature Open Access; MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Springer Nature OA/Free Journals; Free Full-Text Journals in Chemistry |
| subjects | 631/45/607/275 64/60 692/4019/592/75/230 82/80 Amino acids Animals Cloning D-Glutamate cyclase Enantiomers Glutamic Acid - metabolism Heart diseases Homology Humanities and Social Sciences Hydro-Lyases - genetics Hydro-Lyases - metabolism Mammals Metabolism Mice Mice, Knockout Mitochondria Mitochondria, Heart - metabolism Mitochondrial Proteins - deficiency Mitochondrial Proteins - metabolism multidisciplinary Proline Pyrrolidonecarboxylic Acid - metabolism Rodents Science |
| title | D-Glutamate is metabolized in the heart mitochondria |
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