Comparison of amino acid sequence of the C-terminal domain of insulin-responsive glucose transporter (GLUT4) in livestock mammals
The nucleotide sequence of cDNA coding the 38-amino acid of the C-terminal domain of insulin-responsive glucose transporter (GLUT4) was determined by the method of reverse transcription-polymerase chain reaction in the sheep, goat and pig, and compared with that of bovine which have been shown to ha...
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| Veröffentlicht in: | Journal of Veterinary Medical Science 1998, Vol.60(6), pp.769-771 |
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| container_title | Journal of Veterinary Medical Science |
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| creator | Abe, H. (National Inst. of Animal Industry, Kukizaki, Ibaraki (Japan)) Kawakita, Y Miyashige, T Morimatsu, M Saito, M |
| description | The nucleotide sequence of cDNA coding the 38-amino acid of the C-terminal domain of insulin-responsive glucose transporter (GLUT4) was determined by the method of reverse transcription-polymerase chain reaction in the sheep, goat and pig, and compared with that of bovine which have been shown to have a unique amino acid conversion of Asn508 to His. The deduced amino acid sequence was completely identical in the three species, and did not have the amino acid conversion at position 508. Western blot analysis confirmed that an antiserum raised against a rat C-terminal peptide cross-reacted efficiently with GLUT4 of these livestock mammals. |
| doi_str_mv | 10.1292/jvms.60.769 |
| format | Article |
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(National Inst. of Animal Industry, Kukizaki, Ibaraki (Japan)) ; Kawakita, Y ; Miyashige, T ; Morimatsu, M ; Saito, M</creator><creatorcontrib>Abe, H. (National Inst. of Animal Industry, Kukizaki, Ibaraki (Japan)) ; Kawakita, Y ; Miyashige, T ; Morimatsu, M ; Saito, M</creatorcontrib><description>The nucleotide sequence of cDNA coding the 38-amino acid of the C-terminal domain of insulin-responsive glucose transporter (GLUT4) was determined by the method of reverse transcription-polymerase chain reaction in the sheep, goat and pig, and compared with that of bovine which have been shown to have a unique amino acid conversion of Asn508 to His. The deduced amino acid sequence was completely identical in the three species, and did not have the amino acid conversion at position 508. Western blot analysis confirmed that an antiserum raised against a rat C-terminal peptide cross-reacted efficiently with GLUT4 of these livestock mammals.</description><identifier>ISSN: 0916-7250</identifier><identifier>EISSN: 1347-7439</identifier><identifier>DOI: 10.1292/jvms.60.769</identifier><identifier>PMID: 9673955</identifier><language>eng</language><publisher>Japan: JAPANESE SOCIETY OF VETERINARY SCIENCE</publisher><subject>ACIDE AMINE ; ADN ; Amino Acid Sequence ; AMINO ACIDS ; AMINOACIDOS ; Animals ; Animals, Domestic ; Base Sequence ; BETAIL ; Cattle ; DNA ; DNA, Complementary ; GANADO ; GLUCOSA ; GLUCOSE ; Glucose Transporter Type 4 ; GLUT4 ; Goats ; Humans ; INSULIN ; INSULINA ; INSULINE ; LIVESTOCK ; MAMIFEROS ; MAMMALS ; MAMMIFERE ; Mice ; Molecular Sequence Data ; Monosaccharide Transport Proteins - biosynthesis ; Monosaccharide Transport Proteins - chemistry ; Monosaccharide Transport Proteins - genetics ; Muscle Proteins ; NUTRIENT TRANSPORT ; Organ Specificity ; PCR ; Peptide Fragments - chemistry ; Polymerase Chain Reaction - methods ; Rats ; Sequence Alignment ; Sequence Homology, Amino Acid ; Sequence Homology, Nucleic Acid ; Sheep ; Swine ; TRANSPORT DES SUBSTANCES NUTRITIVES ; TRANSPORTE DE NUTRIENTES</subject><ispartof>Journal of Veterinary Medical Science, 1998, Vol.60(6), pp.769-771</ispartof><rights>1998 by the Japanese Society of Veterinary Science</rights><rights>Copyright Japan Science and Technology Agency 1998</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c620t-340951eed6e4faaf1364d0444a2067384ef7b8b86720225eaa086ac6cf28e3753</citedby><cites>FETCH-LOGICAL-c620t-340951eed6e4faaf1364d0444a2067384ef7b8b86720225eaa086ac6cf28e3753</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,1881,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9673955$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Abe, H. 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Western blot analysis confirmed that an antiserum raised against a rat C-terminal peptide cross-reacted efficiently with GLUT4 of these livestock mammals.</description><subject>ACIDE AMINE</subject><subject>ADN</subject><subject>Amino Acid Sequence</subject><subject>AMINO ACIDS</subject><subject>AMINOACIDOS</subject><subject>Animals</subject><subject>Animals, Domestic</subject><subject>Base Sequence</subject><subject>BETAIL</subject><subject>Cattle</subject><subject>DNA</subject><subject>DNA, Complementary</subject><subject>GANADO</subject><subject>GLUCOSA</subject><subject>GLUCOSE</subject><subject>Glucose Transporter Type 4</subject><subject>GLUT4</subject><subject>Goats</subject><subject>Humans</subject><subject>INSULIN</subject><subject>INSULINA</subject><subject>INSULINE</subject><subject>LIVESTOCK</subject><subject>MAMIFEROS</subject><subject>MAMMALS</subject><subject>MAMMIFERE</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Monosaccharide Transport Proteins - biosynthesis</subject><subject>Monosaccharide Transport Proteins - chemistry</subject><subject>Monosaccharide Transport Proteins - genetics</subject><subject>Muscle Proteins</subject><subject>NUTRIENT TRANSPORT</subject><subject>Organ Specificity</subject><subject>PCR</subject><subject>Peptide Fragments - chemistry</subject><subject>Polymerase Chain Reaction - methods</subject><subject>Rats</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Sheep</subject><subject>Swine</subject><subject>TRANSPORT DES SUBSTANCES NUTRITIVES</subject><subject>TRANSPORTE DE NUTRIENTES</subject><issn>0916-7250</issn><issn>1347-7439</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkUGLFDEQhYMo6-zqybMQEESRHtPpdLpzU4Z1VQb0sHsONenq2Yydzph0L3j0n1vjDCN4SUG9L1W8eoy9KMWylEa-3z2EvNRi2WjziC3KSjVFoyrzmC2EKXXRyFo8ZZc574SQpdLmgl0Y3VSmrhfs9yqGPSSf48hjzyH4MXJwvuMZf844Ojy0p3vkq2LCRDIMvIsB_F_ej3ke_FgkzPs4Zv-AfDvMLmbkU4KRmol-8Tc367tb9ZZwPhCTp-h-8AAhwJCfsSc9FXx-qlfs7tP17epzsf5282X1cV04LcVUVEqYukTsNKoeoC8rrTqhlAIpyEyrsG827abVjRRS1gggWg1Ou162WDV1dcVeH-fuUyRnebLBZ4fDACPGOduWrqMrowl89R-4i3Mi39nS9WiBanVJ1Lsj5VLMOWFv98kHSL9sKewhFnuIxWphKRaiX55mzpuA3Zk95UD6h6O-yxNs8axDmrwb8DxLHx8aeZbcPSSL478VPUQLW4rUfv1eGkO-Gi3r6g9TyKnI</recordid><startdate>19980601</startdate><enddate>19980601</enddate><creator>Abe, H. 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(National Inst. of Animal Industry, Kukizaki, Ibaraki (Japan))</creatorcontrib><creatorcontrib>Kawakita, Y</creatorcontrib><creatorcontrib>Miyashige, T</creatorcontrib><creatorcontrib>Morimatsu, M</creatorcontrib><creatorcontrib>Saito, M</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Chemoreception Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of Veterinary Medical Science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Abe, H. 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The deduced amino acid sequence was completely identical in the three species, and did not have the amino acid conversion at position 508. Western blot analysis confirmed that an antiserum raised against a rat C-terminal peptide cross-reacted efficiently with GLUT4 of these livestock mammals.</abstract><cop>Japan</cop><pub>JAPANESE SOCIETY OF VETERINARY SCIENCE</pub><pmid>9673955</pmid><doi>10.1292/jvms.60.769</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of Veterinary Medical Science, 1998, Vol.60(6), pp.769-771 |
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| source | J-STAGE (Free - Japanese); MEDLINE; Free E-Journal (出版社公開部分のみ）; Alma/SFX Local Collection |
| subjects | ACIDE AMINE ADN Amino Acid Sequence AMINO ACIDS AMINOACIDOS Animals Animals, Domestic Base Sequence BETAIL Cattle DNA DNA, Complementary GANADO GLUCOSA GLUCOSE Glucose Transporter Type 4 GLUT4 Goats Humans INSULIN INSULINA INSULINE LIVESTOCK MAMIFEROS MAMMALS MAMMIFERE Mice Molecular Sequence Data Monosaccharide Transport Proteins - biosynthesis Monosaccharide Transport Proteins - chemistry Monosaccharide Transport Proteins - genetics Muscle Proteins NUTRIENT TRANSPORT Organ Specificity PCR Peptide Fragments - chemistry Polymerase Chain Reaction - methods Rats Sequence Alignment Sequence Homology, Amino Acid Sequence Homology, Nucleic Acid Sheep Swine TRANSPORT DES SUBSTANCES NUTRITIVES TRANSPORTE DE NUTRIENTES |
| title | Comparison of amino acid sequence of the C-terminal domain of insulin-responsive glucose transporter (GLUT4) in livestock mammals |
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