Maxadilan. Cloning and functional expression of the gene encoding this potent vasodilator peptide
Maxadilan is a potent vasodilator peptide released into the skin when the sand fly Lutzomyia longipalpis, an important vector of leishmania, probes for a blood meal. As several lines of evidence suggest that this peptide may play a critical role in the enhancement of leishmania infectivity attribute...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-01, Vol.267 (2), p.1062-1066 |
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| container_title | The Journal of biological chemistry |
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| creator | Lerner, E A Shoemaker, C B |
| description | Maxadilan is a potent vasodilator peptide released into the skin when the sand fly Lutzomyia longipalpis, an important vector of leishmania, probes for a blood meal. As several lines of evidence suggest that this peptide may play a critical role in the enhancement of leishmania infectivity attributed to sand fly saliva, the peptide has been proposed as a candidate antigen for a leishmanial vaccine. Although maxadilan is the most potent vasodilator peptide known and shares several properties with calcitonin gene-related peptide (CGRP), studies of its structure, physiological effects, and biological roles have been limited by the miniscule quantities available. Here we report the isolation of cDNA and genomic DNA clones that encode maxadilan. The predicted translation product shows no significant homology with any previously isolated proteins. The coding DNA has been expressed in Escherichia coli and the purified recombinant peptide is biologically active with a specific activity comparable to the natural peptide. Recombinant maxadilan will be useful in studies of vascular biology and could lead to novel therapeutic and prophylactic agents. |
| doi_str_mv | 10.1016/S0021-9258(18)48395-0 |
| format | Article |
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Cloning and functional expression of the gene encoding this potent vasodilator peptide</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Lerner, E A ; Shoemaker, C B</creator><creatorcontrib>Lerner, E A ; Shoemaker, C B</creatorcontrib><description>Maxadilan is a potent vasodilator peptide released into the skin when the sand fly Lutzomyia longipalpis, an important vector of leishmania, probes for a blood meal. As several lines of evidence suggest that this peptide may play a critical role in the enhancement of leishmania infectivity attributed to sand fly saliva, the peptide has been proposed as a candidate antigen for a leishmanial vaccine. Although maxadilan is the most potent vasodilator peptide known and shares several properties with calcitonin gene-related peptide (CGRP), studies of its structure, physiological effects, and biological roles have been limited by the miniscule quantities available. Here we report the isolation of cDNA and genomic DNA clones that encode maxadilan. The predicted translation product shows no significant homology with any previously isolated proteins. The coding DNA has been expressed in Escherichia coli and the purified recombinant peptide is biologically active with a specific activity comparable to the natural peptide. Recombinant maxadilan will be useful in studies of vascular biology and could lead to novel therapeutic and prophylactic agents.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)48395-0</identifier><identifier>PMID: 1730635</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Biological and medical sciences ; Calcitonin Gene-Related Peptide - genetics ; Chromatography, High Pressure Liquid ; Cloning, Molecular ; Diptera ; DNA - genetics ; Erythema - chemically induced ; Escherichia coli - metabolism ; Fundamental and applied biological sciences. Psychology ; Gene Expression ; genes ; Genes. Genome ; Humans ; Insect Hormones - genetics ; Insect Hormones - isolation & purification ; Insect Proteins ; Leishmania ; Lutzomyia longipalpis ; maxadilan ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; nucleotide sequence ; Polymerase Chain Reaction ; predictions ; Protein Biosynthesis ; Psychodidae ; Recombinant Proteins - genetics ; RNA, Messenger - genetics ; Sequence Homology, Nucleic Acid ; use ; vaccines ; Vasodilator Agents - isolation & purification</subject><ispartof>The Journal of biological chemistry, 1992-01, Vol.267 (2), p.1062-1066</ispartof><rights>1992 © 1992 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c494t-2cbbf9fb1fa88d3f25138d972f13e768f839666b74c692ef710f1bd0ca665a6c3</citedby><cites>FETCH-LOGICAL-c494t-2cbbf9fb1fa88d3f25138d972f13e768f839666b74c692ef710f1bd0ca665a6c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5194237$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1730635$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lerner, E A</creatorcontrib><creatorcontrib>Shoemaker, C B</creatorcontrib><title>Maxadilan. Cloning and functional expression of the gene encoding this potent vasodilator peptide</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Maxadilan is a potent vasodilator peptide released into the skin when the sand fly Lutzomyia longipalpis, an important vector of leishmania, probes for a blood meal. As several lines of evidence suggest that this peptide may play a critical role in the enhancement of leishmania infectivity attributed to sand fly saliva, the peptide has been proposed as a candidate antigen for a leishmanial vaccine. Although maxadilan is the most potent vasodilator peptide known and shares several properties with calcitonin gene-related peptide (CGRP), studies of its structure, physiological effects, and biological roles have been limited by the miniscule quantities available. Here we report the isolation of cDNA and genomic DNA clones that encode maxadilan. The predicted translation product shows no significant homology with any previously isolated proteins. The coding DNA has been expressed in Escherichia coli and the purified recombinant peptide is biologically active with a specific activity comparable to the natural peptide. Recombinant maxadilan will be useful in studies of vascular biology and could lead to novel therapeutic and prophylactic agents.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Calcitonin Gene-Related Peptide - genetics</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Cloning, Molecular</subject><subject>Diptera</subject><subject>DNA - genetics</subject><subject>Erythema - chemically induced</subject><subject>Escherichia coli - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression</subject><subject>genes</subject><subject>Genes. Genome</subject><subject>Humans</subject><subject>Insect Hormones - genetics</subject><subject>Insect Hormones - isolation & purification</subject><subject>Insect Proteins</subject><subject>Leishmania</subject><subject>Lutzomyia longipalpis</subject><subject>maxadilan</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>nucleotide sequence</subject><subject>Polymerase Chain Reaction</subject><subject>predictions</subject><subject>Protein Biosynthesis</subject><subject>Psychodidae</subject><subject>Recombinant Proteins - genetics</subject><subject>RNA, Messenger - genetics</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>use</subject><subject>vaccines</subject><subject>Vasodilator Agents - isolation & purification</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMuKFDEUQIMoYzv6CQNBRHRRYx5VqdRqkMYXjLhQwV1IJTddkeqkTNLj-Pemp5pxaTaXcM99HYQuKLmkhIo3XwlhtBlYJ19R-bqVfOga8gBtKJG84R398RBt7pHH6EnOP0l97UDP0BntORG82yD9Wd9q62cdLvF2jsGHHdbBYncIpvgY9IzhdkmQc_3g6HCZAO8gAIZgoj3iZfIZL7FAKPhG53jsVmLCCyzFW3iKHjk9Z3h2iufo-_t337Yfm-svHz5t3143ph3a0jAzjm5wI3VaSssd6yiXduiZoxx6IV09UAgx9q0RAwPXU-LoaInRQnRaGH6OXq59lxR_HSAXtffZwFxPg3jIigo6tLIdKtitoEkx5wROLcnvdfqjKFFHtepOrTp6U1SqO7WK1LqL04DDuAf7r2p1WfMvTnmdjZ5d0sH4fI91dTzjfcWer9jkd9Nvn0CNPpoJ9oqJXrG6gWAVulohqMZuPCSVja_GwdYCU5SN_j_b_gXv86Hf</recordid><startdate>19920115</startdate><enddate>19920115</enddate><creator>Lerner, E A</creator><creator>Shoemaker, C B</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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>7QL</scope><scope>7SS</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>19920115</creationdate><title>Maxadilan. Cloning and functional expression of the gene encoding this potent vasodilator peptide</title><author>Lerner, E A ; Shoemaker, C B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c494t-2cbbf9fb1fa88d3f25138d972f13e768f839666b74c692ef710f1bd0ca665a6c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Calcitonin Gene-Related Peptide - genetics</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Cloning, Molecular</topic><topic>Diptera</topic><topic>DNA - genetics</topic><topic>Erythema - chemically induced</topic><topic>Escherichia coli - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression</topic><topic>genes</topic><topic>Genes. Genome</topic><topic>Humans</topic><topic>Insect Hormones - genetics</topic><topic>Insect Hormones - isolation & purification</topic><topic>Insect Proteins</topic><topic>Leishmania</topic><topic>Lutzomyia longipalpis</topic><topic>maxadilan</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>nucleotide sequence</topic><topic>Polymerase Chain Reaction</topic><topic>predictions</topic><topic>Protein Biosynthesis</topic><topic>Psychodidae</topic><topic>Recombinant Proteins - genetics</topic><topic>RNA, Messenger - genetics</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>use</topic><topic>vaccines</topic><topic>Vasodilator Agents - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lerner, E A</creatorcontrib><creatorcontrib>Shoemaker, C B</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lerner, E A</au><au>Shoemaker, C B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Maxadilan. Cloning and functional expression of the gene encoding this potent vasodilator peptide</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-01-15</date><risdate>1992</risdate><volume>267</volume><issue>2</issue><spage>1062</spage><epage>1066</epage><pages>1062-1066</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Maxadilan is a potent vasodilator peptide released into the skin when the sand fly Lutzomyia longipalpis, an important vector of leishmania, probes for a blood meal. As several lines of evidence suggest that this peptide may play a critical role in the enhancement of leishmania infectivity attributed to sand fly saliva, the peptide has been proposed as a candidate antigen for a leishmanial vaccine. Although maxadilan is the most potent vasodilator peptide known and shares several properties with calcitonin gene-related peptide (CGRP), studies of its structure, physiological effects, and biological roles have been limited by the miniscule quantities available. Here we report the isolation of cDNA and genomic DNA clones that encode maxadilan. The predicted translation product shows no significant homology with any previously isolated proteins. The coding DNA has been expressed in Escherichia coli and the purified recombinant peptide is biologically active with a specific activity comparable to the natural peptide. Recombinant maxadilan will be useful in studies of vascular biology and could lead to novel therapeutic and prophylactic agents.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>1730635</pmid><doi>10.1016/S0021-9258(18)48395-0</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1992-01, Vol.267 (2), p.1062-1066 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Biological and medical sciences Calcitonin Gene-Related Peptide - genetics Chromatography, High Pressure Liquid Cloning, Molecular Diptera DNA - genetics Erythema - chemically induced Escherichia coli - metabolism Fundamental and applied biological sciences. Psychology Gene Expression genes Genes. Genome Humans Insect Hormones - genetics Insect Hormones - isolation & purification Insect Proteins Leishmania Lutzomyia longipalpis maxadilan Molecular and cellular biology Molecular genetics Molecular Sequence Data nucleotide sequence Polymerase Chain Reaction predictions Protein Biosynthesis Psychodidae Recombinant Proteins - genetics RNA, Messenger - genetics Sequence Homology, Nucleic Acid use vaccines Vasodilator Agents - isolation & purification |
| title | Maxadilan. Cloning and functional expression of the gene encoding this potent vasodilator peptide |
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