Loading…
Molecular Characterization of Mammalian Dicarbonyl/l-Xylulose Reductase and Its Localization in Kidney
In this report, we first cloned a cDNA for a protein that is highly expressed in mouse kidney and then isolated its counterparts in human, rat hamster, and guinea pig by polymerase chain reaction-based cloning. The cDNAs of the five species encoded polypeptides of 244 amino acids, which shared more...
Saved in:
Published in: | The Journal of biological chemistry 2002-05, Vol.277 (20), p.17883-17891 |
---|---|
Main Authors: | , , , , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c475t-a1870f024217dbb906366cfce0c079a4c979663cfbf9bd65aed1b0da2bd017503 |
---|---|
cites | cdi_FETCH-LOGICAL-c475t-a1870f024217dbb906366cfce0c079a4c979663cfbf9bd65aed1b0da2bd017503 |
container_end_page | 17891 |
container_issue | 20 |
container_start_page | 17883 |
container_title | The Journal of biological chemistry |
container_volume | 277 |
creator | Nakagawa, Junichi Ishikura, Syuhei Asami, Jun Isaji, Tomoya Usami, Noriyuki Hara, Akira Sakurai, Takanobu Tsuritani, Katsuki Oda, Koji Takahashi, Masayoshi Yoshimoto, Makoto Otsuka, Noboru Kitamura, Kunihiro |
description | In this report, we first cloned a cDNA for a protein that is highly expressed in mouse kidney and then isolated its counterparts in human, rat hamster, and guinea pig by polymerase chain reaction-based cloning. The cDNAs of the five species encoded polypeptides of 244 amino acids, which shared more than 85% identity with each other and showed high identity with a human sperm 34-kDa protein, P34H, as well as a murine lung-specific carbonyl reductase of the short-chain dehydrogenase/reductase superfamily. In particular, the human protein is identical to P34H, except for one amino acid substitution. The purified recombinant proteins of the five species were about 100-kDa homotetramers with NADPH-linked reductase activity for α-dicarbonyl compounds, catalyzed the oxidoreduction between xylitol and l-xylulose, and were inhibited competitively by n-butyric acid. Therefore, the proteins are designated as dicarbonyl/l-xylulose reductases (DCXRs). The substrate specificity and kinetic constants of DCXRs for dicarbonyl compounds and sugars are similar to those of mammalian diacetyl reductase and l-xylulose reductase, respectively, and the identity of the DCXRs with these two enzymes was demonstrated by their co-purification from hamster and guinea pig livers and by protein sequencing of the hepatic enzymes. Both DCXR and its mRNA are highly expressed in kidney and liver of human and rodent tissues, and the protein was localized primarily to the inner membranes of the proximal renal tubules in murine kidneys. The results imply that P34H and diacetyl reductase (EC 1.1.1.5) are identical tol-xylulose reductase (EC 1.1.1.10), which is involved in the uronate cycle of glucose metabolism, and the unique localization of the enzyme in kidney suggests that it has a role other than in general carbohydrate metabolism. |
doi_str_mv | 10.1074/jbc.M110703200 |
format | article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_71678699</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0021925820852855</els_id><sourcerecordid>71678699</sourcerecordid><originalsourceid>FETCH-LOGICAL-c475t-a1870f024217dbb906366cfce0c079a4c979663cfbf9bd65aed1b0da2bd017503</originalsourceid><addsrcrecordid>eNp1kE1v1DAQhi0EotvClSPKAfWW7dhJbOeIFgoVu0KqitSb5Y8J68qJi52All-Pq12pJ-Yyc3jeV6OHkHcU1hREe_Vg7HpHywkNA3hBVhRkUzcdvX9JVgCM1j3r5Bk5z_kByrQ9fU3OKJWS8Q5WZNjFgHYJOlWbvU7azpj8Xz37OFVxqHZ6HHXweqo-eauTidMhXIX6_hCWEDNWt-gWO-ty6clVN3OuttGWwKnBT9U37yY8vCGvBh0yvj3tC_Lj-vPd5mu9_f7lZvNxW9tWdHOtqRQwAGsZFc6YHnjDuR0sggXR69b2oue8sYMZeuN4p9FRA04z44CKDpoLcnnsfUzx14J5VqPPFkPQE8YlK0G5kLzvC7g-gjbFnBMO6jH5UaeDoqCezKpiVj2bLYH3p-bFjOie8ZPKAnw4Anv_c__HJ1TGR7vHUTEhFCutQsqmYPKIYdHw22NS2XqcLLoSsbNy0f_vhX-sTZQS</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>71678699</pqid></control><display><type>article</type><title>Molecular Characterization of Mammalian Dicarbonyl/l-Xylulose Reductase and Its Localization in Kidney</title><source>ScienceDirect Additional Titles</source><creator>Nakagawa, Junichi ; Ishikura, Syuhei ; Asami, Jun ; Isaji, Tomoya ; Usami, Noriyuki ; Hara, Akira ; Sakurai, Takanobu ; Tsuritani, Katsuki ; Oda, Koji ; Takahashi, Masayoshi ; Yoshimoto, Makoto ; Otsuka, Noboru ; Kitamura, Kunihiro</creator><creatorcontrib>Nakagawa, Junichi ; Ishikura, Syuhei ; Asami, Jun ; Isaji, Tomoya ; Usami, Noriyuki ; Hara, Akira ; Sakurai, Takanobu ; Tsuritani, Katsuki ; Oda, Koji ; Takahashi, Masayoshi ; Yoshimoto, Makoto ; Otsuka, Noboru ; Kitamura, Kunihiro</creatorcontrib><description>In this report, we first cloned a cDNA for a protein that is highly expressed in mouse kidney and then isolated its counterparts in human, rat hamster, and guinea pig by polymerase chain reaction-based cloning. The cDNAs of the five species encoded polypeptides of 244 amino acids, which shared more than 85% identity with each other and showed high identity with a human sperm 34-kDa protein, P34H, as well as a murine lung-specific carbonyl reductase of the short-chain dehydrogenase/reductase superfamily. In particular, the human protein is identical to P34H, except for one amino acid substitution. The purified recombinant proteins of the five species were about 100-kDa homotetramers with NADPH-linked reductase activity for α-dicarbonyl compounds, catalyzed the oxidoreduction between xylitol and l-xylulose, and were inhibited competitively by n-butyric acid. Therefore, the proteins are designated as dicarbonyl/l-xylulose reductases (DCXRs). The substrate specificity and kinetic constants of DCXRs for dicarbonyl compounds and sugars are similar to those of mammalian diacetyl reductase and l-xylulose reductase, respectively, and the identity of the DCXRs with these two enzymes was demonstrated by their co-purification from hamster and guinea pig livers and by protein sequencing of the hepatic enzymes. Both DCXR and its mRNA are highly expressed in kidney and liver of human and rodent tissues, and the protein was localized primarily to the inner membranes of the proximal renal tubules in murine kidneys. The results imply that P34H and diacetyl reductase (EC 1.1.1.5) are identical tol-xylulose reductase (EC 1.1.1.10), which is involved in the uronate cycle of glucose metabolism, and the unique localization of the enzyme in kidney suggests that it has a role other than in general carbohydrate metabolism.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M110703200</identifier><identifier>PMID: 11882650</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Acetoin Dehydrogenase - metabolism ; Alcohol Oxidoreductases - chemistry ; Alcohol Oxidoreductases - metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Western ; Cloning, Molecular ; Cricetinae ; Electrophoresis, Polyacrylamide Gel ; Guinea Pigs ; Humans ; Kidney - enzymology ; Molecular Sequence Data ; Rats ; Sequence Alignment ; Sugar Alcohol Dehydrogenases - chemistry ; Sugar Alcohol Dehydrogenases - metabolism</subject><ispartof>The Journal of biological chemistry, 2002-05, Vol.277 (20), p.17883-17891</ispartof><rights>2002 © 2002 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c475t-a1870f024217dbb906366cfce0c079a4c979663cfbf9bd65aed1b0da2bd017503</citedby><cites>FETCH-LOGICAL-c475t-a1870f024217dbb906366cfce0c079a4c979663cfbf9bd65aed1b0da2bd017503</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0021925820852855$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3549,27924,27925,45780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11882650$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nakagawa, Junichi</creatorcontrib><creatorcontrib>Ishikura, Syuhei</creatorcontrib><creatorcontrib>Asami, Jun</creatorcontrib><creatorcontrib>Isaji, Tomoya</creatorcontrib><creatorcontrib>Usami, Noriyuki</creatorcontrib><creatorcontrib>Hara, Akira</creatorcontrib><creatorcontrib>Sakurai, Takanobu</creatorcontrib><creatorcontrib>Tsuritani, Katsuki</creatorcontrib><creatorcontrib>Oda, Koji</creatorcontrib><creatorcontrib>Takahashi, Masayoshi</creatorcontrib><creatorcontrib>Yoshimoto, Makoto</creatorcontrib><creatorcontrib>Otsuka, Noboru</creatorcontrib><creatorcontrib>Kitamura, Kunihiro</creatorcontrib><title>Molecular Characterization of Mammalian Dicarbonyl/l-Xylulose Reductase and Its Localization in Kidney</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>In this report, we first cloned a cDNA for a protein that is highly expressed in mouse kidney and then isolated its counterparts in human, rat hamster, and guinea pig by polymerase chain reaction-based cloning. The cDNAs of the five species encoded polypeptides of 244 amino acids, which shared more than 85% identity with each other and showed high identity with a human sperm 34-kDa protein, P34H, as well as a murine lung-specific carbonyl reductase of the short-chain dehydrogenase/reductase superfamily. In particular, the human protein is identical to P34H, except for one amino acid substitution. The purified recombinant proteins of the five species were about 100-kDa homotetramers with NADPH-linked reductase activity for α-dicarbonyl compounds, catalyzed the oxidoreduction between xylitol and l-xylulose, and were inhibited competitively by n-butyric acid. Therefore, the proteins are designated as dicarbonyl/l-xylulose reductases (DCXRs). The substrate specificity and kinetic constants of DCXRs for dicarbonyl compounds and sugars are similar to those of mammalian diacetyl reductase and l-xylulose reductase, respectively, and the identity of the DCXRs with these two enzymes was demonstrated by their co-purification from hamster and guinea pig livers and by protein sequencing of the hepatic enzymes. Both DCXR and its mRNA are highly expressed in kidney and liver of human and rodent tissues, and the protein was localized primarily to the inner membranes of the proximal renal tubules in murine kidneys. The results imply that P34H and diacetyl reductase (EC 1.1.1.5) are identical tol-xylulose reductase (EC 1.1.1.10), which is involved in the uronate cycle of glucose metabolism, and the unique localization of the enzyme in kidney suggests that it has a role other than in general carbohydrate metabolism.</description><subject>Acetoin Dehydrogenase - metabolism</subject><subject>Alcohol Oxidoreductases - chemistry</subject><subject>Alcohol Oxidoreductases - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Blotting, Western</subject><subject>Cloning, Molecular</subject><subject>Cricetinae</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Guinea Pigs</subject><subject>Humans</subject><subject>Kidney - enzymology</subject><subject>Molecular Sequence Data</subject><subject>Rats</subject><subject>Sequence Alignment</subject><subject>Sugar Alcohol Dehydrogenases - chemistry</subject><subject>Sugar Alcohol Dehydrogenases - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><recordid>eNp1kE1v1DAQhi0EotvClSPKAfWW7dhJbOeIFgoVu0KqitSb5Y8J68qJi52All-Pq12pJ-Yyc3jeV6OHkHcU1hREe_Vg7HpHywkNA3hBVhRkUzcdvX9JVgCM1j3r5Bk5z_kByrQ9fU3OKJWS8Q5WZNjFgHYJOlWbvU7azpj8Xz37OFVxqHZ6HHXweqo-eauTidMhXIX6_hCWEDNWt-gWO-ty6clVN3OuttGWwKnBT9U37yY8vCGvBh0yvj3tC_Lj-vPd5mu9_f7lZvNxW9tWdHOtqRQwAGsZFc6YHnjDuR0sggXR69b2oue8sYMZeuN4p9FRA04z44CKDpoLcnnsfUzx14J5VqPPFkPQE8YlK0G5kLzvC7g-gjbFnBMO6jH5UaeDoqCezKpiVj2bLYH3p-bFjOie8ZPKAnw4Anv_c__HJ1TGR7vHUTEhFCutQsqmYPKIYdHw22NS2XqcLLoSsbNy0f_vhX-sTZQS</recordid><startdate>20020517</startdate><enddate>20020517</enddate><creator>Nakagawa, Junichi</creator><creator>Ishikura, Syuhei</creator><creator>Asami, Jun</creator><creator>Isaji, Tomoya</creator><creator>Usami, Noriyuki</creator><creator>Hara, Akira</creator><creator>Sakurai, Takanobu</creator><creator>Tsuritani, Katsuki</creator><creator>Oda, Koji</creator><creator>Takahashi, Masayoshi</creator><creator>Yoshimoto, Makoto</creator><creator>Otsuka, Noboru</creator><creator>Kitamura, Kunihiro</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</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>7X8</scope></search><sort><creationdate>20020517</creationdate><title>Molecular Characterization of Mammalian Dicarbonyl/l-Xylulose Reductase and Its Localization in Kidney</title><author>Nakagawa, Junichi ; Ishikura, Syuhei ; Asami, Jun ; Isaji, Tomoya ; Usami, Noriyuki ; Hara, Akira ; Sakurai, Takanobu ; Tsuritani, Katsuki ; Oda, Koji ; Takahashi, Masayoshi ; Yoshimoto, Makoto ; Otsuka, Noboru ; Kitamura, Kunihiro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c475t-a1870f024217dbb906366cfce0c079a4c979663cfbf9bd65aed1b0da2bd017503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Acetoin Dehydrogenase - metabolism</topic><topic>Alcohol Oxidoreductases - chemistry</topic><topic>Alcohol Oxidoreductases - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Blotting, Western</topic><topic>Cloning, Molecular</topic><topic>Cricetinae</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Guinea Pigs</topic><topic>Humans</topic><topic>Kidney - enzymology</topic><topic>Molecular Sequence Data</topic><topic>Rats</topic><topic>Sequence Alignment</topic><topic>Sugar Alcohol Dehydrogenases - chemistry</topic><topic>Sugar Alcohol Dehydrogenases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nakagawa, Junichi</creatorcontrib><creatorcontrib>Ishikura, Syuhei</creatorcontrib><creatorcontrib>Asami, Jun</creatorcontrib><creatorcontrib>Isaji, Tomoya</creatorcontrib><creatorcontrib>Usami, Noriyuki</creatorcontrib><creatorcontrib>Hara, Akira</creatorcontrib><creatorcontrib>Sakurai, Takanobu</creatorcontrib><creatorcontrib>Tsuritani, Katsuki</creatorcontrib><creatorcontrib>Oda, Koji</creatorcontrib><creatorcontrib>Takahashi, Masayoshi</creatorcontrib><creatorcontrib>Yoshimoto, Makoto</creatorcontrib><creatorcontrib>Otsuka, Noboru</creatorcontrib><creatorcontrib>Kitamura, Kunihiro</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>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nakagawa, Junichi</au><au>Ishikura, Syuhei</au><au>Asami, Jun</au><au>Isaji, Tomoya</au><au>Usami, Noriyuki</au><au>Hara, Akira</au><au>Sakurai, Takanobu</au><au>Tsuritani, Katsuki</au><au>Oda, Koji</au><au>Takahashi, Masayoshi</au><au>Yoshimoto, Makoto</au><au>Otsuka, Noboru</au><au>Kitamura, Kunihiro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular Characterization of Mammalian Dicarbonyl/l-Xylulose Reductase and Its Localization in Kidney</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2002-05-17</date><risdate>2002</risdate><volume>277</volume><issue>20</issue><spage>17883</spage><epage>17891</epage><pages>17883-17891</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>In this report, we first cloned a cDNA for a protein that is highly expressed in mouse kidney and then isolated its counterparts in human, rat hamster, and guinea pig by polymerase chain reaction-based cloning. The cDNAs of the five species encoded polypeptides of 244 amino acids, which shared more than 85% identity with each other and showed high identity with a human sperm 34-kDa protein, P34H, as well as a murine lung-specific carbonyl reductase of the short-chain dehydrogenase/reductase superfamily. In particular, the human protein is identical to P34H, except for one amino acid substitution. The purified recombinant proteins of the five species were about 100-kDa homotetramers with NADPH-linked reductase activity for α-dicarbonyl compounds, catalyzed the oxidoreduction between xylitol and l-xylulose, and were inhibited competitively by n-butyric acid. Therefore, the proteins are designated as dicarbonyl/l-xylulose reductases (DCXRs). The substrate specificity and kinetic constants of DCXRs for dicarbonyl compounds and sugars are similar to those of mammalian diacetyl reductase and l-xylulose reductase, respectively, and the identity of the DCXRs with these two enzymes was demonstrated by their co-purification from hamster and guinea pig livers and by protein sequencing of the hepatic enzymes. Both DCXR and its mRNA are highly expressed in kidney and liver of human and rodent tissues, and the protein was localized primarily to the inner membranes of the proximal renal tubules in murine kidneys. The results imply that P34H and diacetyl reductase (EC 1.1.1.5) are identical tol-xylulose reductase (EC 1.1.1.10), which is involved in the uronate cycle of glucose metabolism, and the unique localization of the enzyme in kidney suggests that it has a role other than in general carbohydrate metabolism.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11882650</pmid><doi>10.1074/jbc.M110703200</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0021-9258 |
ispartof | The Journal of biological chemistry, 2002-05, Vol.277 (20), p.17883-17891 |
issn | 0021-9258 1083-351X |
language | eng |
recordid | cdi_proquest_miscellaneous_71678699 |
source | ScienceDirect Additional Titles |
subjects | Acetoin Dehydrogenase - metabolism Alcohol Oxidoreductases - chemistry Alcohol Oxidoreductases - metabolism Amino Acid Sequence Animals Base Sequence Blotting, Western Cloning, Molecular Cricetinae Electrophoresis, Polyacrylamide Gel Guinea Pigs Humans Kidney - enzymology Molecular Sequence Data Rats Sequence Alignment Sugar Alcohol Dehydrogenases - chemistry Sugar Alcohol Dehydrogenases - metabolism |
title | Molecular Characterization of Mammalian Dicarbonyl/l-Xylulose Reductase and Its Localization in Kidney |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T17%3A13%3A39IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Molecular%20Characterization%20of%20Mammalian%20Dicarbonyl/l-Xylulose%20Reductase%20and%20Its%20Localization%20in%20Kidney&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Nakagawa,%20Junichi&rft.date=2002-05-17&rft.volume=277&rft.issue=20&rft.spage=17883&rft.epage=17891&rft.pages=17883-17891&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1074/jbc.M110703200&rft_dat=%3Cproquest_cross%3E71678699%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c475t-a1870f024217dbb906366cfce0c079a4c979663cfbf9bd65aed1b0da2bd017503%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=71678699&rft_id=info:pmid/11882650&rfr_iscdi=true |