Transfected human somatostatin receptor type 2, SSTR2, not only inhibits adenylate cyclase but also stimulates phospholipase C and Ca2+ mobilization
COS-7 cells were transfected with human somatostatin (SRIF) receptor type 1 and 2 (human SSTR1 and SSTR2, respectively) cDNAs. In human SSTR2-expressing cells, SRIF not only inhibited forskolin-induced cAMP accumulation but also stimulated phospholipase C and Ca2+ mobilization. While the inhibition...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 1994-04, Vol.200 (2), p.986-992 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 992 |
|---|---|
| container_issue | 2 |
| container_start_page | 986 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 200 |
| creator | TOMURA, H OKAJIMA, F MOHAMMED AKBAR MOHAMMED ABDUL MAJID KIMIE SHO KONDO, Y |
| description | COS-7 cells were transfected with human somatostatin (SRIF) receptor type 1 and 2 (human SSTR1 and SSTR2, respectively) cDNAs. In human SSTR2-expressing cells, SRIF not only inhibited forskolin-induced cAMP accumulation but also stimulated phospholipase C and Ca2+ mobilization. While the inhibition of cAMP accumulation was completely reversed by pertussis toxin (PTX) treatment of the cells, SRIF-induced activation of phospholipase C and Ca2+ mobilization was partially but not completely inhibited by the toxin treatment. In human SSTR1-expressing cells, however, SRIF induced only slight inhibition of cAMP accumulation and stimulation of phospholipase C-Ca2+ system. We conclude that the transfected SSTR2 can couple to phospholipase C as well as adenylate cyclase in a stimulatory and inhibitory manner, respectively. Both PTX-sensitive and -insensitive GTP-binding proteins may be involved in the SSTR2 signal transduction mechanisms. |
| doi_str_mv | 10.1006/bbrc.1994.1547 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_76481710</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>76481710</sourcerecordid><originalsourceid>FETCH-LOGICAL-c251t-ca8e9dc6ea8b787687f71de449f5b000bd2c014b60b2d417f31bdc8ae8a61153</originalsourceid><addsrcrecordid>eNo9kU2r1DAUhoMo1_Hq1p2QhbjRjjmdTNMsZfALLgjeWbgrJx9lImlSk3RRf4c_2JQ73EU4i_d5T0geQl4D2wNj3Uelkt6DlHwPRy6ekB0wyZoWGH9KdqwSTSvh13PyIuffjAHwTt6QGyFrGfod-XdOGPJodbGGXpYJA81xwhJzweICTVbbucREyzpb2n6g9_fnn3WEWGgMfqUuXJxyJVM0Nqwei6V61R6zpWopFH2ONBc3LVuU6XyJuR7v5o04UQyGnrB9T6eonHd_66UxvCTPxlq0r67zlpy_fD6fvjV3P75-P326a3R7hNJo7K00urPYK9GLrhejAGM5l-NR1acr02oGXHVMtYaDGA-gjO7R9tgBHA-35N3D2jnFP4vNZZhc1tZ7DDYueRAd70EAq-D-AdQp5pzsOMzJTZjWAdiwWRg2C8NmYdgs1MKb6-ZFTdY84tdvr_nba45Zox-rA-3yI8aZBGBw-A-oaJKp</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>76481710</pqid></control><display><type>article</type><title>Transfected human somatostatin receptor type 2, SSTR2, not only inhibits adenylate cyclase but also stimulates phospholipase C and Ca2+ mobilization</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>TOMURA, H ; OKAJIMA, F ; MOHAMMED AKBAR ; MOHAMMED ABDUL MAJID ; KIMIE SHO ; KONDO, Y</creator><creatorcontrib>TOMURA, H ; OKAJIMA, F ; MOHAMMED AKBAR ; MOHAMMED ABDUL MAJID ; KIMIE SHO ; KONDO, Y</creatorcontrib><description>COS-7 cells were transfected with human somatostatin (SRIF) receptor type 1 and 2 (human SSTR1 and SSTR2, respectively) cDNAs. In human SSTR2-expressing cells, SRIF not only inhibited forskolin-induced cAMP accumulation but also stimulated phospholipase C and Ca2+ mobilization. While the inhibition of cAMP accumulation was completely reversed by pertussis toxin (PTX) treatment of the cells, SRIF-induced activation of phospholipase C and Ca2+ mobilization was partially but not completely inhibited by the toxin treatment. In human SSTR1-expressing cells, however, SRIF induced only slight inhibition of cAMP accumulation and stimulation of phospholipase C-Ca2+ system. We conclude that the transfected SSTR2 can couple to phospholipase C as well as adenylate cyclase in a stimulatory and inhibitory manner, respectively. Both PTX-sensitive and -insensitive GTP-binding proteins may be involved in the SSTR2 signal transduction mechanisms.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.1994.1547</identifier><identifier>PMID: 7910018</identifier><identifier>CODEN: BBRCA9</identifier><language>eng</language><publisher>San Diego, CA: Elsevier</publisher><subject>Adenosine Triphosphate - pharmacology ; Adenylate Cyclase Toxin ; Adenylyl Cyclase Inhibitors ; Animals ; Biological and medical sciences ; Calcium - metabolism ; Cell Line ; Cell receptors ; Cell structures and functions ; DNA, Complementary - genetics ; Fundamental and applied biological sciences. Psychology ; GTP-Binding Proteins - metabolism ; Humans ; Miscellaneous ; Molecular and cellular biology ; Pertussis Toxin ; Receptors, Somatostatin - classification ; Receptors, Somatostatin - genetics ; Receptors, Somatostatin - metabolism ; Somatostatin - metabolism ; Somatostatin - pharmacology ; Transfection ; Type C Phospholipases - metabolism ; Virulence Factors, Bordetella - pharmacology</subject><ispartof>Biochemical and biophysical research communications, 1994-04, Vol.200 (2), p.986-992</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c251t-ca8e9dc6ea8b787687f71de449f5b000bd2c014b60b2d417f31bdc8ae8a61153</citedby></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=4091101$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7910018$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>TOMURA, H</creatorcontrib><creatorcontrib>OKAJIMA, F</creatorcontrib><creatorcontrib>MOHAMMED AKBAR</creatorcontrib><creatorcontrib>MOHAMMED ABDUL MAJID</creatorcontrib><creatorcontrib>KIMIE SHO</creatorcontrib><creatorcontrib>KONDO, Y</creatorcontrib><title>Transfected human somatostatin receptor type 2, SSTR2, not only inhibits adenylate cyclase but also stimulates phospholipase C and Ca2+ mobilization</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>COS-7 cells were transfected with human somatostatin (SRIF) receptor type 1 and 2 (human SSTR1 and SSTR2, respectively) cDNAs. In human SSTR2-expressing cells, SRIF not only inhibited forskolin-induced cAMP accumulation but also stimulated phospholipase C and Ca2+ mobilization. While the inhibition of cAMP accumulation was completely reversed by pertussis toxin (PTX) treatment of the cells, SRIF-induced activation of phospholipase C and Ca2+ mobilization was partially but not completely inhibited by the toxin treatment. In human SSTR1-expressing cells, however, SRIF induced only slight inhibition of cAMP accumulation and stimulation of phospholipase C-Ca2+ system. We conclude that the transfected SSTR2 can couple to phospholipase C as well as adenylate cyclase in a stimulatory and inhibitory manner, respectively. Both PTX-sensitive and -insensitive GTP-binding proteins may be involved in the SSTR2 signal transduction mechanisms.</description><subject>Adenosine Triphosphate - pharmacology</subject><subject>Adenylate Cyclase Toxin</subject><subject>Adenylyl Cyclase Inhibitors</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Calcium - metabolism</subject><subject>Cell Line</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>DNA, Complementary - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GTP-Binding Proteins - metabolism</subject><subject>Humans</subject><subject>Miscellaneous</subject><subject>Molecular and cellular biology</subject><subject>Pertussis Toxin</subject><subject>Receptors, Somatostatin - classification</subject><subject>Receptors, Somatostatin - genetics</subject><subject>Receptors, Somatostatin - metabolism</subject><subject>Somatostatin - metabolism</subject><subject>Somatostatin - pharmacology</subject><subject>Transfection</subject><subject>Type C Phospholipases - metabolism</subject><subject>Virulence Factors, Bordetella - pharmacology</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kU2r1DAUhoMo1_Hq1p2QhbjRjjmdTNMsZfALLgjeWbgrJx9lImlSk3RRf4c_2JQ73EU4i_d5T0geQl4D2wNj3Uelkt6DlHwPRy6ekB0wyZoWGH9KdqwSTSvh13PyIuffjAHwTt6QGyFrGfod-XdOGPJodbGGXpYJA81xwhJzweICTVbbucREyzpb2n6g9_fnn3WEWGgMfqUuXJxyJVM0Nqwei6V61R6zpWopFH2ONBc3LVuU6XyJuR7v5o04UQyGnrB9T6eonHd_66UxvCTPxlq0r67zlpy_fD6fvjV3P75-P326a3R7hNJo7K00urPYK9GLrhejAGM5l-NR1acr02oGXHVMtYaDGA-gjO7R9tgBHA-35N3D2jnFP4vNZZhc1tZ7DDYueRAd70EAq-D-AdQp5pzsOMzJTZjWAdiwWRg2C8NmYdgs1MKb6-ZFTdY84tdvr_nba45Zox-rA-3yI8aZBGBw-A-oaJKp</recordid><startdate>19940429</startdate><enddate>19940429</enddate><creator>TOMURA, H</creator><creator>OKAJIMA, F</creator><creator>MOHAMMED AKBAR</creator><creator>MOHAMMED ABDUL MAJID</creator><creator>KIMIE SHO</creator><creator>KONDO, Y</creator><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>19940429</creationdate><title>Transfected human somatostatin receptor type 2, SSTR2, not only inhibits adenylate cyclase but also stimulates phospholipase C and Ca2+ mobilization</title><author>TOMURA, H ; OKAJIMA, F ; MOHAMMED AKBAR ; MOHAMMED ABDUL MAJID ; KIMIE SHO ; KONDO, Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c251t-ca8e9dc6ea8b787687f71de449f5b000bd2c014b60b2d417f31bdc8ae8a61153</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Adenosine Triphosphate - pharmacology</topic><topic>Adenylate Cyclase Toxin</topic><topic>Adenylyl Cyclase Inhibitors</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Calcium - metabolism</topic><topic>Cell Line</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>DNA, Complementary - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GTP-Binding Proteins - metabolism</topic><topic>Humans</topic><topic>Miscellaneous</topic><topic>Molecular and cellular biology</topic><topic>Pertussis Toxin</topic><topic>Receptors, Somatostatin - classification</topic><topic>Receptors, Somatostatin - genetics</topic><topic>Receptors, Somatostatin - metabolism</topic><topic>Somatostatin - metabolism</topic><topic>Somatostatin - pharmacology</topic><topic>Transfection</topic><topic>Type C Phospholipases - metabolism</topic><topic>Virulence Factors, Bordetella - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>TOMURA, H</creatorcontrib><creatorcontrib>OKAJIMA, F</creatorcontrib><creatorcontrib>MOHAMMED AKBAR</creatorcontrib><creatorcontrib>MOHAMMED ABDUL MAJID</creatorcontrib><creatorcontrib>KIMIE SHO</creatorcontrib><creatorcontrib>KONDO, Y</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>TOMURA, H</au><au>OKAJIMA, F</au><au>MOHAMMED AKBAR</au><au>MOHAMMED ABDUL MAJID</au><au>KIMIE SHO</au><au>KONDO, Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Transfected human somatostatin receptor type 2, SSTR2, not only inhibits adenylate cyclase but also stimulates phospholipase C and Ca2+ mobilization</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1994-04-29</date><risdate>1994</risdate><volume>200</volume><issue>2</issue><spage>986</spage><epage>992</epage><pages>986-992</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>COS-7 cells were transfected with human somatostatin (SRIF) receptor type 1 and 2 (human SSTR1 and SSTR2, respectively) cDNAs. In human SSTR2-expressing cells, SRIF not only inhibited forskolin-induced cAMP accumulation but also stimulated phospholipase C and Ca2+ mobilization. While the inhibition of cAMP accumulation was completely reversed by pertussis toxin (PTX) treatment of the cells, SRIF-induced activation of phospholipase C and Ca2+ mobilization was partially but not completely inhibited by the toxin treatment. In human SSTR1-expressing cells, however, SRIF induced only slight inhibition of cAMP accumulation and stimulation of phospholipase C-Ca2+ system. We conclude that the transfected SSTR2 can couple to phospholipase C as well as adenylate cyclase in a stimulatory and inhibitory manner, respectively. Both PTX-sensitive and -insensitive GTP-binding proteins may be involved in the SSTR2 signal transduction mechanisms.</abstract><cop>San Diego, CA</cop><pub>Elsevier</pub><pmid>7910018</pmid><doi>10.1006/bbrc.1994.1547</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 1994-04, Vol.200 (2), p.986-992 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76481710 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Adenosine Triphosphate - pharmacology Adenylate Cyclase Toxin Adenylyl Cyclase Inhibitors Animals Biological and medical sciences Calcium - metabolism Cell Line Cell receptors Cell structures and functions DNA, Complementary - genetics Fundamental and applied biological sciences. Psychology GTP-Binding Proteins - metabolism Humans Miscellaneous Molecular and cellular biology Pertussis Toxin Receptors, Somatostatin - classification Receptors, Somatostatin - genetics Receptors, Somatostatin - metabolism Somatostatin - metabolism Somatostatin - pharmacology Transfection Type C Phospholipases - metabolism Virulence Factors, Bordetella - pharmacology |
| title | Transfected human somatostatin receptor type 2, SSTR2, not only inhibits adenylate cyclase but also stimulates phospholipase C and Ca2+ mobilization |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-30T05%3A35%3A31IST&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=Transfected%20human%20somatostatin%20receptor%20type%202,%20SSTR2,%20not%20only%20inhibits%20adenylate%20cyclase%20but%20also%20stimulates%20phospholipase%20C%20and%20Ca2+%20mobilization&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=TOMURA,%20H&rft.date=1994-04-29&rft.volume=200&rft.issue=2&rft.spage=986&rft.epage=992&rft.pages=986-992&rft.issn=0006-291X&rft.eissn=1090-2104&rft.coden=BBRCA9&rft_id=info:doi/10.1006/bbrc.1994.1547&rft_dat=%3Cproquest_cross%3E76481710%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=76481710&rft_id=info:pmid/7910018&rfr_iscdi=true |