Molecular identification of the first SIFamide receptor
SIFamide is the short name and also the C terminus of the Drosophila neuropeptide AYRKPPFNGSIFamide. SIFamide has been isolated or predicted from various insects and crustaceans, and appears to be extremely well conserved among these arthropods. However, the function of this neuropeptide is still en...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2006-02, Vol.340 (2), p.696-701 |
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| creator | Jørgensen, Lars M. Hauser, Frank Cazzamali, Giuseppe Williamson, Michael Grimmelikhuijzen, Cornelis J.P. |
| description | SIFamide is the short name and also the C terminus of the
Drosophila neuropeptide AYRKPPFNGSIFamide. SIFamide has been isolated or predicted from various insects and crustaceans, and appears to be extremely well conserved among these arthropods. However, the function of this neuropeptide is still enigmatic. Here, we have identified the
Drosophila gene (CG10823) coding for the SIFamide receptor. When expressed in Chinese hamster ovary cells, the receptor is only activated by
Drosophila SIFamide (EC
50, 2
×
10
−8
M) and not by a library of 32 other insect neuropeptides and eight biogenic amines. Database searches revealed SIFamide receptor orthologues in the genomes from the malaria mosquito
Anopheles gambiae, the silkworm
Bombyx mori, the red flour beetle
Tribolium castaneum, and the honey bee
Apis mellifera. An alignment of the five insect SIFamide or SIFamide-like receptors showed, again, an impressive sequence conservation (67–77% amino acid sequence identities between the seven-transmembrane areas; 82–87% sequence similarities). The identification of well-conserved SIFamide receptor orthologues in all other insects with a sequenced genome, suggests that the SIFamide/receptor couple must have an essential function in arthropods. This paper is the first report on the identification of a SIFamide receptor. |
| doi_str_mv | 10.1016/j.bbrc.2005.12.062 |
| format | Article |
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Drosophila neuropeptide AYRKPPFNGSIFamide. SIFamide has been isolated or predicted from various insects and crustaceans, and appears to be extremely well conserved among these arthropods. However, the function of this neuropeptide is still enigmatic. Here, we have identified the
Drosophila gene (CG10823) coding for the SIFamide receptor. When expressed in Chinese hamster ovary cells, the receptor is only activated by
Drosophila SIFamide (EC
50, 2
×
10
−8
M) and not by a library of 32 other insect neuropeptides and eight biogenic amines. Database searches revealed SIFamide receptor orthologues in the genomes from the malaria mosquito
Anopheles gambiae, the silkworm
Bombyx mori, the red flour beetle
Tribolium castaneum, and the honey bee
Apis mellifera. An alignment of the five insect SIFamide or SIFamide-like receptors showed, again, an impressive sequence conservation (67–77% amino acid sequence identities between the seven-transmembrane areas; 82–87% sequence similarities). The identification of well-conserved SIFamide receptor orthologues in all other insects with a sequenced genome, suggests that the SIFamide/receptor couple must have an essential function in arthropods. This paper is the first report on the identification of a SIFamide receptor.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2005.12.062</identifier><identifier>PMID: 16378592</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Anopheles gambiae ; Apis mellifera ; Arthropoda ; Base Sequence ; Bombyx mori ; CHO Cells ; Cricetinae ; Cricetulus ; Crustaceans ; DNA, Complementary ; Drosophila ; Drosophila melanogaster - genetics ; Drosophila melanogaster - metabolism ; Drosophila Proteins - genetics ; Drosophila Proteins - isolation & purification ; Endocrinology ; G protein-coupled receptor ; GPCR ; Honey bee ; Insects ; Malaria ; Molecular Sequence Data ; Mosquito ; Neurohormone ; Neuropeptide ; Neuropeptides - metabolism ; Peptide hormone ; Receptors, G-Protein-Coupled ; Receptors, Neuropeptide - genetics ; Receptors, Neuropeptide - isolation & purification ; Tribolium castaneum</subject><ispartof>Biochemical and biophysical research communications, 2006-02, Vol.340 (2), p.696-701</ispartof><rights>2005 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c385t-941544b15fcc0431f312459600c4420e1eae4c29dcafbec5be48e0ef047f715d3</citedby><cites>FETCH-LOGICAL-c385t-941544b15fcc0431f312459600c4420e1eae4c29dcafbec5be48e0ef047f715d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2005.12.062$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16378592$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jørgensen, Lars M.</creatorcontrib><creatorcontrib>Hauser, Frank</creatorcontrib><creatorcontrib>Cazzamali, Giuseppe</creatorcontrib><creatorcontrib>Williamson, Michael</creatorcontrib><creatorcontrib>Grimmelikhuijzen, Cornelis J.P.</creatorcontrib><title>Molecular identification of the first SIFamide receptor</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>SIFamide is the short name and also the C terminus of the
Drosophila neuropeptide AYRKPPFNGSIFamide. SIFamide has been isolated or predicted from various insects and crustaceans, and appears to be extremely well conserved among these arthropods. However, the function of this neuropeptide is still enigmatic. Here, we have identified the
Drosophila gene (CG10823) coding for the SIFamide receptor. When expressed in Chinese hamster ovary cells, the receptor is only activated by
Drosophila SIFamide (EC
50, 2
×
10
−8
M) and not by a library of 32 other insect neuropeptides and eight biogenic amines. Database searches revealed SIFamide receptor orthologues in the genomes from the malaria mosquito
Anopheles gambiae, the silkworm
Bombyx mori, the red flour beetle
Tribolium castaneum, and the honey bee
Apis mellifera. An alignment of the five insect SIFamide or SIFamide-like receptors showed, again, an impressive sequence conservation (67–77% amino acid sequence identities between the seven-transmembrane areas; 82–87% sequence similarities). The identification of well-conserved SIFamide receptor orthologues in all other insects with a sequenced genome, suggests that the SIFamide/receptor couple must have an essential function in arthropods. This paper is the first report on the identification of a SIFamide receptor.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Anopheles gambiae</subject><subject>Apis mellifera</subject><subject>Arthropoda</subject><subject>Base Sequence</subject><subject>Bombyx mori</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>Cricetulus</subject><subject>Crustaceans</subject><subject>DNA, Complementary</subject><subject>Drosophila</subject><subject>Drosophila melanogaster - genetics</subject><subject>Drosophila melanogaster - metabolism</subject><subject>Drosophila Proteins - genetics</subject><subject>Drosophila Proteins - isolation & purification</subject><subject>Endocrinology</subject><subject>G protein-coupled receptor</subject><subject>GPCR</subject><subject>Honey bee</subject><subject>Insects</subject><subject>Malaria</subject><subject>Molecular Sequence Data</subject><subject>Mosquito</subject><subject>Neurohormone</subject><subject>Neuropeptide</subject><subject>Neuropeptides - metabolism</subject><subject>Peptide hormone</subject><subject>Receptors, G-Protein-Coupled</subject><subject>Receptors, Neuropeptide - genetics</subject><subject>Receptors, Neuropeptide - isolation & purification</subject><subject>Tribolium castaneum</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0D9PwzAQh2ELgWgpfAEGlIkt4c6xnURiQRWFSkUMgMRmJc5ZuMqfYqdIfHtStRIbTLe89xsexi4REgRUN-ukqrxJOIBMkCeg-BGbIhQQcwRxzKYAoGJe4PuEnYWwBkAUqjhlE1RplsuCT1n21Ddktk3pI1dTNzjrTDm4vot6Gw0fFFnnwxC9LBdlOwaRJ0Oboffn7MSWTaCLw52xt8X96_wxXj0_LOd3q9ikuRziQqAUokJpjQGRok2RC1koACMEB0IqSRhe1Ka0FRlZkcgJyILIbIayTmfser-78f3nlsKgWxcMNU3ZUb8NWmUKuFTy35BDLjOQ2RjyfWh8H4InqzfetaX_1gh656rXeueqd64auR5dx6erw_q2aqn-fTlAjsHtPqAR48uR18E46gzVbiQbdN27v_Z_APjTiDg</recordid><startdate>20060210</startdate><enddate>20060210</enddate><creator>Jørgensen, Lars M.</creator><creator>Hauser, Frank</creator><creator>Cazzamali, Giuseppe</creator><creator>Williamson, Michael</creator><creator>Grimmelikhuijzen, Cornelis J.P.</creator><general>Elsevier Inc</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>7SS</scope><scope>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20060210</creationdate><title>Molecular identification of the first SIFamide receptor</title><author>Jørgensen, Lars M. ; Hauser, Frank ; Cazzamali, Giuseppe ; Williamson, Michael ; Grimmelikhuijzen, Cornelis J.P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c385t-941544b15fcc0431f312459600c4420e1eae4c29dcafbec5be48e0ef047f715d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Anopheles gambiae</topic><topic>Apis mellifera</topic><topic>Arthropoda</topic><topic>Base Sequence</topic><topic>Bombyx mori</topic><topic>CHO Cells</topic><topic>Cricetinae</topic><topic>Cricetulus</topic><topic>Crustaceans</topic><topic>DNA, Complementary</topic><topic>Drosophila</topic><topic>Drosophila melanogaster - genetics</topic><topic>Drosophila melanogaster - metabolism</topic><topic>Drosophila Proteins - genetics</topic><topic>Drosophila Proteins - isolation & purification</topic><topic>Endocrinology</topic><topic>G protein-coupled receptor</topic><topic>GPCR</topic><topic>Honey bee</topic><topic>Insects</topic><topic>Malaria</topic><topic>Molecular Sequence Data</topic><topic>Mosquito</topic><topic>Neurohormone</topic><topic>Neuropeptide</topic><topic>Neuropeptides - metabolism</topic><topic>Peptide hormone</topic><topic>Receptors, G-Protein-Coupled</topic><topic>Receptors, Neuropeptide - genetics</topic><topic>Receptors, Neuropeptide - isolation & purification</topic><topic>Tribolium castaneum</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jørgensen, Lars M.</creatorcontrib><creatorcontrib>Hauser, Frank</creatorcontrib><creatorcontrib>Cazzamali, Giuseppe</creatorcontrib><creatorcontrib>Williamson, Michael</creatorcontrib><creatorcontrib>Grimmelikhuijzen, Cornelis J.P.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</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>Jørgensen, Lars M.</au><au>Hauser, Frank</au><au>Cazzamali, Giuseppe</au><au>Williamson, Michael</au><au>Grimmelikhuijzen, Cornelis J.P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular identification of the first SIFamide receptor</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2006-02-10</date><risdate>2006</risdate><volume>340</volume><issue>2</issue><spage>696</spage><epage>701</epage><pages>696-701</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>SIFamide is the short name and also the C terminus of the
Drosophila neuropeptide AYRKPPFNGSIFamide. SIFamide has been isolated or predicted from various insects and crustaceans, and appears to be extremely well conserved among these arthropods. However, the function of this neuropeptide is still enigmatic. Here, we have identified the
Drosophila gene (CG10823) coding for the SIFamide receptor. When expressed in Chinese hamster ovary cells, the receptor is only activated by
Drosophila SIFamide (EC
50, 2
×
10
−8
M) and not by a library of 32 other insect neuropeptides and eight biogenic amines. Database searches revealed SIFamide receptor orthologues in the genomes from the malaria mosquito
Anopheles gambiae, the silkworm
Bombyx mori, the red flour beetle
Tribolium castaneum, and the honey bee
Apis mellifera. An alignment of the five insect SIFamide or SIFamide-like receptors showed, again, an impressive sequence conservation (67–77% amino acid sequence identities between the seven-transmembrane areas; 82–87% sequence similarities). The identification of well-conserved SIFamide receptor orthologues in all other insects with a sequenced genome, suggests that the SIFamide/receptor couple must have an essential function in arthropods. This paper is the first report on the identification of a SIFamide receptor.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16378592</pmid><doi>10.1016/j.bbrc.2005.12.062</doi><tpages>6</tpages></addata></record> |
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| subjects | Amino Acid Sequence Animals Anopheles gambiae Apis mellifera Arthropoda Base Sequence Bombyx mori CHO Cells Cricetinae Cricetulus Crustaceans DNA, Complementary Drosophila Drosophila melanogaster - genetics Drosophila melanogaster - metabolism Drosophila Proteins - genetics Drosophila Proteins - isolation & purification Endocrinology G protein-coupled receptor GPCR Honey bee Insects Malaria Molecular Sequence Data Mosquito Neurohormone Neuropeptide Neuropeptides - metabolism Peptide hormone Receptors, G-Protein-Coupled Receptors, Neuropeptide - genetics Receptors, Neuropeptide - isolation & purification Tribolium castaneum |
| title | Molecular identification of the first SIFamide receptor |
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