mosquito Aedes aegypti (L.) leucokinin receptor is a multiligand receptor for the three Aedes kinins
A cDNA cloned from Aedes aegypti (L.) (Aedae) female Malpighian tubule (AY596453) encodes a 584 amino acid residue protein (65.2 kDa) predicted as a G protein-coupled receptor and orthologue of the drosokinin receptor from Drosophila melanogaster and highly similar to the tick Boophilus microplus my...
Gespeichert in:
| Veröffentlicht in: | Insect molecular biology 2005, Vol.14 (1), p.55-67 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 67 |
|---|---|
| container_issue | 1 |
| container_start_page | 55 |
| container_title | Insect molecular biology |
| container_volume | 14 |
| creator | Pietrantonio, P.V Jagge, C Taneja-Bageshwar, S Nachman, R.J Barhoumi, R |
| description | A cDNA cloned from Aedes aegypti (L.) (Aedae) female Malpighian tubule (AY596453) encodes a 584 amino acid residue protein (65.2 kDa) predicted as a G protein-coupled receptor and orthologue of the drosokinin receptor from Drosophila melanogaster and highly similar to the tick Boophilus microplus myokinin receptor (AF228521). Based on the similarity to this Aedes sequence, we also propose a correction for the Anopheles gambiae protein sequence EAA05450. When expressed in CHO-K1 cells, the Aedes receptor behaved as a multiligand receptor and functionally responded to concentrations greater than or equal to 1 nM of Aedae kinins 1-3, respectively, as determined by a calcium bioluminescence plate assay and single cell intracellular calcium measurements by confocal fluorescence cytometry. Estimates of EC50 values by the plate assay were 16.04 nM for Aedae-K-3, 26.6 nM for Aedae-K-2 and 48.8 nM for Aedae-K-1 and were statistically significantly different. These results suggest that the observed differences in physiological responses to the three Aedes kinins in the Aedes isolated Malpighian tubule reported elsewhere could now be explained by differences in intracellular signalling events triggered by the different peptides on the same receptor and not necessarily due to the existence of various receptors for the three Aedes kinins. |
| doi_str_mv | 10.1111/j.1365-2583.2004.00531.x |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_67376993</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>67376993</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4591-56dbfd35a172afa916360d3aded1e0e6c3324496e4a6be432491dd6a6e8a2dd73</originalsourceid><addsrcrecordid>eNqNkV9v0zAUxS0EYmXwFSBPCB4SruP4ppZ42Sb2B3VDCCZ4s9z4prhLms5OtPbb4zbV9giWrmzr_s6xfC5jCYeMx_VpmXGBMs3lVGQ5QJEBSMGzzTM2eWw8ZxNQmKccSnnEXoWwBICpQvWSHXGJKMpSTphtu3A_uL5LTshSSAwttuveJR9m2cekoaHq7tzKrRJPFa37zicuMkk7NL1r3MKs7FOnjtX_oVie6GC3F4fX7EVtmkBvDvsxuz3_8vPsMp19u7g6O5mlVSEVTyXaeW2FNLzMTW0UR4FghbFkOQFhJUReFAqpMDinIl4UtxYN0tTk1pbimL0ffde-ux8o9Lp1oaKmMSvqhqCxFCUqJf4J8jJaQ44RnI5g5bsQPNV67V1r_FZz0LtR6KXeJa53ievdKPR-FHoTpW8PbwzzluyT8JB9BD6PwINraPvfxvrq-jQeojwd5S70tHmUG3-3_6fUv24u9A3-_g7F9Vd9Gfl3I1-bTpuFd0Hf_siBC-AAHKUSfwEBdK_J</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17491026</pqid></control><display><type>article</type><title>mosquito Aedes aegypti (L.) leucokinin receptor is a multiligand receptor for the three Aedes kinins</title><source>Wiley Online Library - AutoHoldings Journals</source><source>MEDLINE</source><creator>Pietrantonio, P.V ; Jagge, C ; Taneja-Bageshwar, S ; Nachman, R.J ; Barhoumi, R</creator><creatorcontrib>Pietrantonio, P.V ; Jagge, C ; Taneja-Bageshwar, S ; Nachman, R.J ; Barhoumi, R</creatorcontrib><description>A cDNA cloned from Aedes aegypti (L.) (Aedae) female Malpighian tubule (AY596453) encodes a 584 amino acid residue protein (65.2 kDa) predicted as a G protein-coupled receptor and orthologue of the drosokinin receptor from Drosophila melanogaster and highly similar to the tick Boophilus microplus myokinin receptor (AF228521). Based on the similarity to this Aedes sequence, we also propose a correction for the Anopheles gambiae protein sequence EAA05450. When expressed in CHO-K1 cells, the Aedes receptor behaved as a multiligand receptor and functionally responded to concentrations greater than or equal to 1 nM of Aedae kinins 1-3, respectively, as determined by a calcium bioluminescence plate assay and single cell intracellular calcium measurements by confocal fluorescence cytometry. Estimates of EC50 values by the plate assay were 16.04 nM for Aedae-K-3, 26.6 nM for Aedae-K-2 and 48.8 nM for Aedae-K-1 and were statistically significantly different. These results suggest that the observed differences in physiological responses to the three Aedes kinins in the Aedes isolated Malpighian tubule reported elsewhere could now be explained by differences in intracellular signalling events triggered by the different peptides on the same receptor and not necessarily due to the existence of various receptors for the three Aedes kinins.</description><identifier>ISSN: 0962-1075</identifier><identifier>EISSN: 1365-2583</identifier><identifier>DOI: 10.1111/j.1365-2583.2004.00531.x</identifier><identifier>PMID: 15663775</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>Aedes - genetics ; Aedes - metabolism ; Aedes aegypti ; Amino Acid Sequence ; amino acid sequences ; Animals ; Anopheles gambiae ; Base Sequence ; Boophilus microplus ; calcium ; Calcium - metabolism ; CHO Cells ; Cloning, Molecular ; complementary DNA ; Cricetinae ; Culicidae ; Drosophila melanogaster ; Female ; G-protein-coupled receptors ; gene expression ; insect diuresis ; insect excretion ; insect GPCR (G protein-coupled receptor) (myo)kinin receptor ; ion transport ; Ixodidae ; kinins ; Kinins - metabolism ; leucokinin(s) ; Malpighian tubules ; Malpighian Tubules - metabolism ; Microscopy, Confocal ; Molecular Sequence Data ; nucleotide sequences ; receptors ; Receptors, Neuropeptide - genetics ; Receptors, Neuropeptide - metabolism ; Recombinant Proteins - genetics ; Reverse Transcriptase Polymerase Chain Reaction ; RNA - chemistry ; RNA - genetics ; Sequence Alignment ; Transfection</subject><ispartof>Insect molecular biology, 2005, Vol.14 (1), p.55-67</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4591-56dbfd35a172afa916360d3aded1e0e6c3324496e4a6be432491dd6a6e8a2dd73</citedby><cites>FETCH-LOGICAL-c4591-56dbfd35a172afa916360d3aded1e0e6c3324496e4a6be432491dd6a6e8a2dd73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1365-2583.2004.00531.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-2583.2004.00531.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,4024,27923,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15663775$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pietrantonio, P.V</creatorcontrib><creatorcontrib>Jagge, C</creatorcontrib><creatorcontrib>Taneja-Bageshwar, S</creatorcontrib><creatorcontrib>Nachman, R.J</creatorcontrib><creatorcontrib>Barhoumi, R</creatorcontrib><title>mosquito Aedes aegypti (L.) leucokinin receptor is a multiligand receptor for the three Aedes kinins</title><title>Insect molecular biology</title><addtitle>Insect Mol Biol</addtitle><description>A cDNA cloned from Aedes aegypti (L.) (Aedae) female Malpighian tubule (AY596453) encodes a 584 amino acid residue protein (65.2 kDa) predicted as a G protein-coupled receptor and orthologue of the drosokinin receptor from Drosophila melanogaster and highly similar to the tick Boophilus microplus myokinin receptor (AF228521). Based on the similarity to this Aedes sequence, we also propose a correction for the Anopheles gambiae protein sequence EAA05450. When expressed in CHO-K1 cells, the Aedes receptor behaved as a multiligand receptor and functionally responded to concentrations greater than or equal to 1 nM of Aedae kinins 1-3, respectively, as determined by a calcium bioluminescence plate assay and single cell intracellular calcium measurements by confocal fluorescence cytometry. Estimates of EC50 values by the plate assay were 16.04 nM for Aedae-K-3, 26.6 nM for Aedae-K-2 and 48.8 nM for Aedae-K-1 and were statistically significantly different. These results suggest that the observed differences in physiological responses to the three Aedes kinins in the Aedes isolated Malpighian tubule reported elsewhere could now be explained by differences in intracellular signalling events triggered by the different peptides on the same receptor and not necessarily due to the existence of various receptors for the three Aedes kinins.</description><subject>Aedes - genetics</subject><subject>Aedes - metabolism</subject><subject>Aedes aegypti</subject><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Animals</subject><subject>Anopheles gambiae</subject><subject>Base Sequence</subject><subject>Boophilus microplus</subject><subject>calcium</subject><subject>Calcium - metabolism</subject><subject>CHO Cells</subject><subject>Cloning, Molecular</subject><subject>complementary DNA</subject><subject>Cricetinae</subject><subject>Culicidae</subject><subject>Drosophila melanogaster</subject><subject>Female</subject><subject>G-protein-coupled receptors</subject><subject>gene expression</subject><subject>insect diuresis</subject><subject>insect excretion</subject><subject>insect GPCR (G protein-coupled receptor) (myo)kinin receptor</subject><subject>ion transport</subject><subject>Ixodidae</subject><subject>kinins</subject><subject>Kinins - metabolism</subject><subject>leucokinin(s)</subject><subject>Malpighian tubules</subject><subject>Malpighian Tubules - metabolism</subject><subject>Microscopy, Confocal</subject><subject>Molecular Sequence Data</subject><subject>nucleotide sequences</subject><subject>receptors</subject><subject>Receptors, Neuropeptide - genetics</subject><subject>Receptors, Neuropeptide - metabolism</subject><subject>Recombinant Proteins - genetics</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RNA - chemistry</subject><subject>RNA - genetics</subject><subject>Sequence Alignment</subject><subject>Transfection</subject><issn>0962-1075</issn><issn>1365-2583</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkV9v0zAUxS0EYmXwFSBPCB4SruP4ppZ42Sb2B3VDCCZ4s9z4prhLms5OtPbb4zbV9giWrmzr_s6xfC5jCYeMx_VpmXGBMs3lVGQ5QJEBSMGzzTM2eWw8ZxNQmKccSnnEXoWwBICpQvWSHXGJKMpSTphtu3A_uL5LTshSSAwttuveJR9m2cekoaHq7tzKrRJPFa37zicuMkk7NL1r3MKs7FOnjtX_oVie6GC3F4fX7EVtmkBvDvsxuz3_8vPsMp19u7g6O5mlVSEVTyXaeW2FNLzMTW0UR4FghbFkOQFhJUReFAqpMDinIl4UtxYN0tTk1pbimL0ffde-ux8o9Lp1oaKmMSvqhqCxFCUqJf4J8jJaQ44RnI5g5bsQPNV67V1r_FZz0LtR6KXeJa53ievdKPR-FHoTpW8PbwzzluyT8JB9BD6PwINraPvfxvrq-jQeojwd5S70tHmUG3-3_6fUv24u9A3-_g7F9Vd9Gfl3I1-bTpuFd0Hf_siBC-AAHKUSfwEBdK_J</recordid><startdate>2005</startdate><enddate>2005</enddate><creator>Pietrantonio, P.V</creator><creator>Jagge, C</creator><creator>Taneja-Bageshwar, S</creator><creator>Nachman, R.J</creator><creator>Barhoumi, R</creator><general>Blackwell Science Ltd</general><scope>FBQ</scope><scope>BSCLL</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>7SS</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>2005</creationdate><title>mosquito Aedes aegypti (L.) leucokinin receptor is a multiligand receptor for the three Aedes kinins</title><author>Pietrantonio, P.V ; Jagge, C ; Taneja-Bageshwar, S ; Nachman, R.J ; Barhoumi, R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4591-56dbfd35a172afa916360d3aded1e0e6c3324496e4a6be432491dd6a6e8a2dd73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Aedes - genetics</topic><topic>Aedes - metabolism</topic><topic>Aedes aegypti</topic><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Animals</topic><topic>Anopheles gambiae</topic><topic>Base Sequence</topic><topic>Boophilus microplus</topic><topic>calcium</topic><topic>Calcium - metabolism</topic><topic>CHO Cells</topic><topic>Cloning, Molecular</topic><topic>complementary DNA</topic><topic>Cricetinae</topic><topic>Culicidae</topic><topic>Drosophila melanogaster</topic><topic>Female</topic><topic>G-protein-coupled receptors</topic><topic>gene expression</topic><topic>insect diuresis</topic><topic>insect excretion</topic><topic>insect GPCR (G protein-coupled receptor) (myo)kinin receptor</topic><topic>ion transport</topic><topic>Ixodidae</topic><topic>kinins</topic><topic>Kinins - metabolism</topic><topic>leucokinin(s)</topic><topic>Malpighian tubules</topic><topic>Malpighian Tubules - metabolism</topic><topic>Microscopy, Confocal</topic><topic>Molecular Sequence Data</topic><topic>nucleotide sequences</topic><topic>receptors</topic><topic>Receptors, Neuropeptide - genetics</topic><topic>Receptors, Neuropeptide - metabolism</topic><topic>Recombinant Proteins - genetics</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>RNA - chemistry</topic><topic>RNA - genetics</topic><topic>Sequence Alignment</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pietrantonio, P.V</creatorcontrib><creatorcontrib>Jagge, C</creatorcontrib><creatorcontrib>Taneja-Bageshwar, S</creatorcontrib><creatorcontrib>Nachman, R.J</creatorcontrib><creatorcontrib>Barhoumi, R</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><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>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Insect molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pietrantonio, P.V</au><au>Jagge, C</au><au>Taneja-Bageshwar, S</au><au>Nachman, R.J</au><au>Barhoumi, R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>mosquito Aedes aegypti (L.) leucokinin receptor is a multiligand receptor for the three Aedes kinins</atitle><jtitle>Insect molecular biology</jtitle><addtitle>Insect Mol Biol</addtitle><date>2005</date><risdate>2005</risdate><volume>14</volume><issue>1</issue><spage>55</spage><epage>67</epage><pages>55-67</pages><issn>0962-1075</issn><eissn>1365-2583</eissn><abstract>A cDNA cloned from Aedes aegypti (L.) (Aedae) female Malpighian tubule (AY596453) encodes a 584 amino acid residue protein (65.2 kDa) predicted as a G protein-coupled receptor and orthologue of the drosokinin receptor from Drosophila melanogaster and highly similar to the tick Boophilus microplus myokinin receptor (AF228521). Based on the similarity to this Aedes sequence, we also propose a correction for the Anopheles gambiae protein sequence EAA05450. When expressed in CHO-K1 cells, the Aedes receptor behaved as a multiligand receptor and functionally responded to concentrations greater than or equal to 1 nM of Aedae kinins 1-3, respectively, as determined by a calcium bioluminescence plate assay and single cell intracellular calcium measurements by confocal fluorescence cytometry. Estimates of EC50 values by the plate assay were 16.04 nM for Aedae-K-3, 26.6 nM for Aedae-K-2 and 48.8 nM for Aedae-K-1 and were statistically significantly different. These results suggest that the observed differences in physiological responses to the three Aedes kinins in the Aedes isolated Malpighian tubule reported elsewhere could now be explained by differences in intracellular signalling events triggered by the different peptides on the same receptor and not necessarily due to the existence of various receptors for the three Aedes kinins.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>15663775</pmid><doi>10.1111/j.1365-2583.2004.00531.x</doi><tpages>13</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0962-1075 |
| ispartof | Insect molecular biology, 2005, Vol.14 (1), p.55-67 |
| issn | 0962-1075 1365-2583 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_67376993 |
| source | Wiley Online Library - AutoHoldings Journals; MEDLINE |
| subjects | Aedes - genetics Aedes - metabolism Aedes aegypti Amino Acid Sequence amino acid sequences Animals Anopheles gambiae Base Sequence Boophilus microplus calcium Calcium - metabolism CHO Cells Cloning, Molecular complementary DNA Cricetinae Culicidae Drosophila melanogaster Female G-protein-coupled receptors gene expression insect diuresis insect excretion insect GPCR (G protein-coupled receptor) (myo)kinin receptor ion transport Ixodidae kinins Kinins - metabolism leucokinin(s) Malpighian tubules Malpighian Tubules - metabolism Microscopy, Confocal Molecular Sequence Data nucleotide sequences receptors Receptors, Neuropeptide - genetics Receptors, Neuropeptide - metabolism Recombinant Proteins - genetics Reverse Transcriptase Polymerase Chain Reaction RNA - chemistry RNA - genetics Sequence Alignment Transfection |
| title | mosquito Aedes aegypti (L.) leucokinin receptor is a multiligand receptor for the three Aedes kinins |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-01T19%3A34%3A20IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=mosquito%20Aedes%20aegypti%20(L.)%20leucokinin%20receptor%20is%20a%20multiligand%20receptor%20for%20the%20three%20Aedes%20kinins&rft.jtitle=Insect%20molecular%20biology&rft.au=Pietrantonio,%20P.V&rft.date=2005&rft.volume=14&rft.issue=1&rft.spage=55&rft.epage=67&rft.pages=55-67&rft.issn=0962-1075&rft.eissn=1365-2583&rft_id=info:doi/10.1111/j.1365-2583.2004.00531.x&rft_dat=%3Cproquest_cross%3E67376993%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=17491026&rft_id=info:pmid/15663775&rfr_iscdi=true |