Molecular Definition of Bovine Argininosuccinate Synthetase Deficiency
Citrullinemia is an inborn error of metabolism due to deficiency of the urea cycle enzyme, argininosuccinate synthetase [L-citrulline:L-aspartate ligase (AMP-forming), EC 6.3.4.5]. The disease was first described in humans but was recently reported in dairy cattle in Australia. Here we report the nu...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1989-10, Vol.86 (20), p.7947-7951 |
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| creator | Dennis, Julie A. Healy, Peter J. Beaudet, Arthur L. O'Brien, William E. |
| description | Citrullinemia is an inborn error of metabolism due to deficiency of the urea cycle enzyme, argininosuccinate synthetase [L-citrulline:L-aspartate ligase (AMP-forming), EC 6.3.4.5]. The disease was first described in humans but was recently reported in dairy cattle in Australia. Here we report the nucleotide sequence of the normal bovine cDNA for argininosuccinate synthetase and the mutation present in animals with citrullinemia. Analysis of DNA from affected animals by Southern blotting did not readily identify the mutation in the bovine gene. RNA (Northern) blotting revealed a major reduction in the steady-state amount of mRNA in the liver of affected animals to |
| doi_str_mv | 10.1073/pnas.86.20.7947 |
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The disease was first described in humans but was recently reported in dairy cattle in Australia. Here we report the nucleotide sequence of the normal bovine cDNA for argininosuccinate synthetase and the mutation present in animals with citrullinemia. Analysis of DNA from affected animals by Southern blotting did not readily identify the mutation in the bovine gene. RNA (Northern) blotting revealed a major reduction in the steady-state amount of mRNA in the liver of affected animals to <5% of controls. The bovine cDNA was cloned and sequenced and revealed 96% identity with the deduced human sequence at the amino acid level. Starting with mutant bovine liver, the mRNA was reverse-transcribed; the cDNA product was amplified with the polymerase chain reaction, cloned, and sequenced. The sequence revealed a C → T transition converting arginine-86 (CGA) to a nonsense codon (TGA). A second C → T transition represented a polymorphism in proline-175 (CCC → CCT). The mutation and the polymorphism were confirmed by amplification of genomic DNA and demonstration with restriction endonuclease enzymes of both the loss of an Ava II site in DNA from mutant animals at codon 86 and the presence or absence of a Dde I site at codon 175. The loss of the Ava II site can be used for rapid, economical, nonradioactive detection of heterozygotes for bovine citrullinemia.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.86.20.7947</identifier><identifier>PMID: 2813370</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Amino Acid Metabolism, Inborn Errors - genetics ; Amino Acid Metabolism, Inborn Errors - veterinary ; Amino Acid Sequence ; Amino acids ; Animals ; Argininosuccinate Synthase - deficiency ; Argininosuccinate Synthase - genetics ; Base Sequence ; Cattle ; Cattle Diseases - genetics ; Citrulline - blood ; Citrullinemia ; Cloning, Molecular ; Codons ; Complementary DNA ; DNA ; DNA - blood ; DNA - genetics ; Generally accepted auditing standards ; Genetic mutation ; Humans ; Ligases - genetics ; Liver ; Molecular Sequence Data ; Monocytes - enzymology ; Mutation ; Polymerase Chain Reaction ; Sequence Homology, Nucleic Acid ; Ungulates</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1989-10, Vol.86 (20), p.7947-7951</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c492t-f16cf786161ea1f6ec27b203e2057f4e6e2c79fd58c13095407ea36ba74dfff3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/86/20.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/35200$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/35200$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53769,53771,57995,58228</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2813370$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dennis, Julie A.</creatorcontrib><creatorcontrib>Healy, Peter J.</creatorcontrib><creatorcontrib>Beaudet, Arthur L.</creatorcontrib><creatorcontrib>O'Brien, William E.</creatorcontrib><title>Molecular Definition of Bovine Argininosuccinate Synthetase Deficiency</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Citrullinemia is an inborn error of metabolism due to deficiency of the urea cycle enzyme, argininosuccinate synthetase [L-citrulline:L-aspartate ligase (AMP-forming), EC 6.3.4.5]. The disease was first described in humans but was recently reported in dairy cattle in Australia. Here we report the nucleotide sequence of the normal bovine cDNA for argininosuccinate synthetase and the mutation present in animals with citrullinemia. Analysis of DNA from affected animals by Southern blotting did not readily identify the mutation in the bovine gene. RNA (Northern) blotting revealed a major reduction in the steady-state amount of mRNA in the liver of affected animals to <5% of controls. The bovine cDNA was cloned and sequenced and revealed 96% identity with the deduced human sequence at the amino acid level. Starting with mutant bovine liver, the mRNA was reverse-transcribed; the cDNA product was amplified with the polymerase chain reaction, cloned, and sequenced. The sequence revealed a C → T transition converting arginine-86 (CGA) to a nonsense codon (TGA). A second C → T transition represented a polymorphism in proline-175 (CCC → CCT). The mutation and the polymorphism were confirmed by amplification of genomic DNA and demonstration with restriction endonuclease enzymes of both the loss of an Ava II site in DNA from mutant animals at codon 86 and the presence or absence of a Dde I site at codon 175. The loss of the Ava II site can be used for rapid, economical, nonradioactive detection of heterozygotes for bovine citrullinemia.</description><subject>Amino Acid Metabolism, Inborn Errors - genetics</subject><subject>Amino Acid Metabolism, Inborn Errors - veterinary</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Argininosuccinate Synthase - deficiency</subject><subject>Argininosuccinate Synthase - genetics</subject><subject>Base Sequence</subject><subject>Cattle</subject><subject>Cattle Diseases - genetics</subject><subject>Citrulline - blood</subject><subject>Citrullinemia</subject><subject>Cloning, Molecular</subject><subject>Codons</subject><subject>Complementary DNA</subject><subject>DNA</subject><subject>DNA - blood</subject><subject>DNA - genetics</subject><subject>Generally accepted auditing standards</subject><subject>Genetic mutation</subject><subject>Humans</subject><subject>Ligases - genetics</subject><subject>Liver</subject><subject>Molecular Sequence Data</subject><subject>Monocytes - enzymology</subject><subject>Mutation</subject><subject>Polymerase Chain Reaction</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Ungulates</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1vEzEQhi0EKqFwRkIC7YmeNh1_rL0-9FBKC0hFHOjdcpxx62pjB9tbkX_PhoSIXuBkye_zjGb0EvKawpyC4qfraMu8l3MGc6WFekJmFDRtpdDwlMwAmGp7wcRz8qKUewDQXQ9H5Ij1lHMFM3L1NQ3oxsHm5iP6EEMNKTbJNx_SQ4jYnOfb6TOmMjoXoq3YfN_EeofVFvxtuIDRbV6SZ94OBV_t32Nyc3V5c_G5vf726cvF-XXrhGa19VQ6r3pJJUVLvUTH1IIBRwad8gIlMqe0X3a9o3zaVYBCy-XCKrH03vNjcrYbux4XK1w6jDXbwaxzWNm8MckG8ziJ4c7cpgfDdE97Pfnv935OP0Ys1axCcTgMNmIai1GaQ0e5-C9IO64mTk3g6Q50OZWS0R-WoWC2DZltQ6aXhoHZNjQZb_--4cDvK5nyd_t8K_5JHw04-Sdg_DgMFX_WiXyzI-9LTfmA8o4B8F9d7q94</recordid><startdate>19891001</startdate><enddate>19891001</enddate><creator>Dennis, Julie A.</creator><creator>Healy, Peter J.</creator><creator>Beaudet, Arthur L.</creator><creator>O'Brien, William E.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19891001</creationdate><title>Molecular Definition of Bovine Argininosuccinate Synthetase Deficiency</title><author>Dennis, Julie A. ; Healy, Peter J. ; Beaudet, Arthur L. ; O'Brien, William E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c492t-f16cf786161ea1f6ec27b203e2057f4e6e2c79fd58c13095407ea36ba74dfff3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Amino Acid Metabolism, Inborn Errors - genetics</topic><topic>Amino Acid Metabolism, Inborn Errors - veterinary</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Argininosuccinate Synthase - deficiency</topic><topic>Argininosuccinate Synthase - genetics</topic><topic>Base Sequence</topic><topic>Cattle</topic><topic>Cattle Diseases - genetics</topic><topic>Citrulline - blood</topic><topic>Citrullinemia</topic><topic>Cloning, Molecular</topic><topic>Codons</topic><topic>Complementary DNA</topic><topic>DNA</topic><topic>DNA - blood</topic><topic>DNA - genetics</topic><topic>Generally accepted auditing standards</topic><topic>Genetic mutation</topic><topic>Humans</topic><topic>Ligases - genetics</topic><topic>Liver</topic><topic>Molecular Sequence Data</topic><topic>Monocytes - enzymology</topic><topic>Mutation</topic><topic>Polymerase Chain Reaction</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Ungulates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dennis, Julie A.</creatorcontrib><creatorcontrib>Healy, Peter J.</creatorcontrib><creatorcontrib>Beaudet, Arthur L.</creatorcontrib><creatorcontrib>O'Brien, William E.</creatorcontrib><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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dennis, Julie A.</au><au>Healy, Peter J.</au><au>Beaudet, Arthur L.</au><au>O'Brien, William E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular Definition of Bovine Argininosuccinate Synthetase Deficiency</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1989-10-01</date><risdate>1989</risdate><volume>86</volume><issue>20</issue><spage>7947</spage><epage>7951</epage><pages>7947-7951</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Citrullinemia is an inborn error of metabolism due to deficiency of the urea cycle enzyme, argininosuccinate synthetase [L-citrulline:L-aspartate ligase (AMP-forming), EC 6.3.4.5]. The disease was first described in humans but was recently reported in dairy cattle in Australia. Here we report the nucleotide sequence of the normal bovine cDNA for argininosuccinate synthetase and the mutation present in animals with citrullinemia. Analysis of DNA from affected animals by Southern blotting did not readily identify the mutation in the bovine gene. RNA (Northern) blotting revealed a major reduction in the steady-state amount of mRNA in the liver of affected animals to <5% of controls. The bovine cDNA was cloned and sequenced and revealed 96% identity with the deduced human sequence at the amino acid level. Starting with mutant bovine liver, the mRNA was reverse-transcribed; the cDNA product was amplified with the polymerase chain reaction, cloned, and sequenced. The sequence revealed a C → T transition converting arginine-86 (CGA) to a nonsense codon (TGA). A second C → T transition represented a polymorphism in proline-175 (CCC → CCT). The mutation and the polymorphism were confirmed by amplification of genomic DNA and demonstration with restriction endonuclease enzymes of both the loss of an Ava II site in DNA from mutant animals at codon 86 and the presence or absence of a Dde I site at codon 175. The loss of the Ava II site can be used for rapid, economical, nonradioactive detection of heterozygotes for bovine citrullinemia.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>2813370</pmid><doi>10.1073/pnas.86.20.7947</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1989-10, Vol.86 (20), p.7947-7951 |
| issn | 0027-8424 1091-6490 |
| language | eng |
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| source | Jstor Complete Legacy; MEDLINE; Full-Text Journals in Chemistry (Open access); PubMed Central; Alma/SFX Local Collection |
| subjects | Amino Acid Metabolism, Inborn Errors - genetics Amino Acid Metabolism, Inborn Errors - veterinary Amino Acid Sequence Amino acids Animals Argininosuccinate Synthase - deficiency Argininosuccinate Synthase - genetics Base Sequence Cattle Cattle Diseases - genetics Citrulline - blood Citrullinemia Cloning, Molecular Codons Complementary DNA DNA DNA - blood DNA - genetics Generally accepted auditing standards Genetic mutation Humans Ligases - genetics Liver Molecular Sequence Data Monocytes - enzymology Mutation Polymerase Chain Reaction Sequence Homology, Nucleic Acid Ungulates |
| title | Molecular Definition of Bovine Argininosuccinate Synthetase Deficiency |
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