Cloning and Expression of Large Isoform of Glutamic Acid Decarboxylase from Human Pancreatic-Islet
Glutamic acid decarboxylase (GAD) catalyzes formation of γ-aminobutyric acid from glutamic acid and is a major autoantigen in insulin-dependent diabetes mellitus. Its two isoforms, GAD65 and GAD67, are encoded by two separate genes. We prepared human islet cDNA library and screened it with cDNA prob...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1993-05, Vol.192 (3), p.1353-1359 |
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| creator | Kawasaki, E. Moriuchi, R. Watanabe, M. Saitoh, K. Brunicardi, F.C. Watt, P.C. Yamaguchi, T. Mullen, Y. Akazawa, S. Miyamoto, T. Nagataki, S. |
| description | Glutamic acid decarboxylase (GAD) catalyzes formation of γ-aminobutyric acid from glutamic acid and is a major autoantigen in insulin-dependent diabetes mellitus. Its two isoforms, GAD65 and GAD67, are encoded by two separate genes. We prepared human islet cDNA library and screened it with cDNA probes of rat brain GAD67. We cloned the cDNA for GAD67, the large isoform of glutamic acid decarboxylase, and determined its nucleotide sequence. Sequencing of the resulting clone identified a 1,785 residue open-reading frame encoded a 594 amino acid polypeptide that showed a 99.4% similarity with GAD67 from human brain. The bacterially expressed human islet GAD67 protein was enzymatically active and immunoreactive. The isolation of cDNA for this additional islet GAD isoforms will be important in studying the etiology and pathogenesis of IDDM. |
| doi_str_mv | 10.1006/bbrc.1993.1565 |
| format | Article |
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Its two isoforms, GAD65 and GAD67, are encoded by two separate genes. We prepared human islet cDNA library and screened it with cDNA probes of rat brain GAD67. We cloned the cDNA for GAD67, the large isoform of glutamic acid decarboxylase, and determined its nucleotide sequence. Sequencing of the resulting clone identified a 1,785 residue open-reading frame encoded a 594 amino acid polypeptide that showed a 99.4% similarity with GAD67 from human brain. The bacterially expressed human islet GAD67 protein was enzymatically active and immunoreactive. The isolation of cDNA for this additional islet GAD isoforms will be important in studying the etiology and pathogenesis of IDDM.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.1993.1565</identifier><identifier>PMID: 8507203</identifier><identifier>CODEN: BBRCA9</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Base Sequence ; Biological and medical sciences ; Brain - enzymology ; Cloning, Molecular ; DNA Probes ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Gene Expression ; Gene Library ; Glutamate Decarboxylase - genetics ; Glutamate Decarboxylase - isolation & purification ; Glutamate Decarboxylase - metabolism ; Humans ; Islets of Langerhans - enzymology ; Isoenzymes - genetics ; Isoenzymes - isolation & purification ; Isoenzymes - metabolism ; Kinetics ; Lyases ; Molecular Sequence Data ; Oligonucleotide Probes ; Rats ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Sequence Homology, Amino Acid</subject><ispartof>Biochemical and biophysical research communications, 1993-05, Vol.192 (3), p.1353-1359</ispartof><rights>1993 Academic Press</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c434t-201c510f10d6f35b7a0dc09a69838f163c35633b51195cd016e958a84cc3c073</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/bbrc.1993.1565$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4882378$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8507203$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kawasaki, E.</creatorcontrib><creatorcontrib>Moriuchi, R.</creatorcontrib><creatorcontrib>Watanabe, M.</creatorcontrib><creatorcontrib>Saitoh, K.</creatorcontrib><creatorcontrib>Brunicardi, F.C.</creatorcontrib><creatorcontrib>Watt, P.C.</creatorcontrib><creatorcontrib>Yamaguchi, T.</creatorcontrib><creatorcontrib>Mullen, Y.</creatorcontrib><creatorcontrib>Akazawa, S.</creatorcontrib><creatorcontrib>Miyamoto, T.</creatorcontrib><creatorcontrib>Nagataki, S.</creatorcontrib><title>Cloning and Expression of Large Isoform of Glutamic Acid Decarboxylase from Human Pancreatic-Islet</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Glutamic acid decarboxylase (GAD) catalyzes formation of γ-aminobutyric acid from glutamic acid and is a major autoantigen in insulin-dependent diabetes mellitus. Its two isoforms, GAD65 and GAD67, are encoded by two separate genes. We prepared human islet cDNA library and screened it with cDNA probes of rat brain GAD67. We cloned the cDNA for GAD67, the large isoform of glutamic acid decarboxylase, and determined its nucleotide sequence. Sequencing of the resulting clone identified a 1,785 residue open-reading frame encoded a 594 amino acid polypeptide that showed a 99.4% similarity with GAD67 from human brain. The bacterially expressed human islet GAD67 protein was enzymatically active and immunoreactive. The isolation of cDNA for this additional islet GAD isoforms will be important in studying the etiology and pathogenesis of IDDM.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Brain - enzymology</subject><subject>Cloning, Molecular</subject><subject>DNA Probes</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression</subject><subject>Gene Library</subject><subject>Glutamate Decarboxylase - genetics</subject><subject>Glutamate Decarboxylase - isolation & purification</subject><subject>Glutamate Decarboxylase - metabolism</subject><subject>Humans</subject><subject>Islets of Langerhans - enzymology</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - isolation & purification</subject><subject>Isoenzymes - metabolism</subject><subject>Kinetics</subject><subject>Lyases</subject><subject>Molecular Sequence Data</subject><subject>Oligonucleotide Probes</subject><subject>Rats</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kEFr3DAQRkVpSTfbXnsr6FB683ZkWbZ0DNs0WVhoDzn0JuTxKKjY1layS_Lva7NLbjkMA_O9GYbH2CcBOwFQf2vbhDthjNwJVas3bCPAQFEKqN6yDSxEURrx-z27zvkPgBBVba7YlVbQlCA3rN33cQzjI3djx2-fTolyDnHk0fOjS4_EDzn6mIZ1cNfPkxsC8hsMHf9O6FIbn557l4n7FAd-Pw9u5L_ciIncFLA45J6mD-ydd32mj5e-ZQ8_bh_298Xx591hf3MssJLVVJQgUAnwArraS9U2DjoE42qjpfailihVLWWrhDAKOxA1GaWdrhAlQiO37Ov57CnFvzPlyQ4hI_W9GynO2TaqMbJeast2ZxBTzDmRt6cUBpeerQC7OrWrU7s6tavTZeHz5fLcDtS94BeJS_7lkruMrvdpERDyC1ZpXcpGL5g-Y7RI-Bco2YyBRqQuJMLJdjG89sF_vxyRkw</recordid><startdate>19930514</startdate><enddate>19930514</enddate><creator>Kawasaki, E.</creator><creator>Moriuchi, R.</creator><creator>Watanabe, M.</creator><creator>Saitoh, K.</creator><creator>Brunicardi, F.C.</creator><creator>Watt, P.C.</creator><creator>Yamaguchi, T.</creator><creator>Mullen, Y.</creator><creator>Akazawa, S.</creator><creator>Miyamoto, T.</creator><creator>Nagataki, S.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</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>19930514</creationdate><title>Cloning and Expression of Large Isoform of Glutamic Acid Decarboxylase from Human Pancreatic-Islet</title><author>Kawasaki, E. ; Moriuchi, R. ; Watanabe, M. ; Saitoh, K. ; Brunicardi, F.C. ; Watt, P.C. ; Yamaguchi, T. ; Mullen, Y. ; Akazawa, S. ; Miyamoto, T. ; Nagataki, S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c434t-201c510f10d6f35b7a0dc09a69838f163c35633b51195cd016e958a84cc3c073</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Brain - enzymology</topic><topic>Cloning, Molecular</topic><topic>DNA Probes</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression</topic><topic>Gene Library</topic><topic>Glutamate Decarboxylase - genetics</topic><topic>Glutamate Decarboxylase - isolation & purification</topic><topic>Glutamate Decarboxylase - metabolism</topic><topic>Humans</topic><topic>Islets of Langerhans - enzymology</topic><topic>Isoenzymes - genetics</topic><topic>Isoenzymes - isolation & purification</topic><topic>Isoenzymes - metabolism</topic><topic>Kinetics</topic><topic>Lyases</topic><topic>Molecular Sequence Data</topic><topic>Oligonucleotide Probes</topic><topic>Rats</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kawasaki, E.</creatorcontrib><creatorcontrib>Moriuchi, R.</creatorcontrib><creatorcontrib>Watanabe, M.</creatorcontrib><creatorcontrib>Saitoh, K.</creatorcontrib><creatorcontrib>Brunicardi, F.C.</creatorcontrib><creatorcontrib>Watt, P.C.</creatorcontrib><creatorcontrib>Yamaguchi, T.</creatorcontrib><creatorcontrib>Mullen, Y.</creatorcontrib><creatorcontrib>Akazawa, S.</creatorcontrib><creatorcontrib>Miyamoto, T.</creatorcontrib><creatorcontrib>Nagataki, S.</creatorcontrib><collection>Pascal-Francis</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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kawasaki, E.</au><au>Moriuchi, R.</au><au>Watanabe, M.</au><au>Saitoh, K.</au><au>Brunicardi, F.C.</au><au>Watt, P.C.</au><au>Yamaguchi, T.</au><au>Mullen, Y.</au><au>Akazawa, S.</au><au>Miyamoto, T.</au><au>Nagataki, S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and Expression of Large Isoform of Glutamic Acid Decarboxylase from Human Pancreatic-Islet</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1993-05-14</date><risdate>1993</risdate><volume>192</volume><issue>3</issue><spage>1353</spage><epage>1359</epage><pages>1353-1359</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>Glutamic acid decarboxylase (GAD) catalyzes formation of γ-aminobutyric acid from glutamic acid and is a major autoantigen in insulin-dependent diabetes mellitus. Its two isoforms, GAD65 and GAD67, are encoded by two separate genes. We prepared human islet cDNA library and screened it with cDNA probes of rat brain GAD67. We cloned the cDNA for GAD67, the large isoform of glutamic acid decarboxylase, and determined its nucleotide sequence. Sequencing of the resulting clone identified a 1,785 residue open-reading frame encoded a 594 amino acid polypeptide that showed a 99.4% similarity with GAD67 from human brain. The bacterially expressed human islet GAD67 protein was enzymatically active and immunoreactive. The isolation of cDNA for this additional islet GAD isoforms will be important in studying the etiology and pathogenesis of IDDM.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>8507203</pmid><doi>10.1006/bbrc.1993.1565</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1993-05, Vol.192 (3), p.1353-1359 |
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| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Base Sequence Biological and medical sciences Brain - enzymology Cloning, Molecular DNA Probes Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Gene Expression Gene Library Glutamate Decarboxylase - genetics Glutamate Decarboxylase - isolation & purification Glutamate Decarboxylase - metabolism Humans Islets of Langerhans - enzymology Isoenzymes - genetics Isoenzymes - isolation & purification Isoenzymes - metabolism Kinetics Lyases Molecular Sequence Data Oligonucleotide Probes Rats Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Sequence Homology, Amino Acid |
| title | Cloning and Expression of Large Isoform of Glutamic Acid Decarboxylase from Human Pancreatic-Islet |
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