Ca2+-mobilizing Actions of Platelet-Derived Growth Factor Differ from Those of Bombesin and Vasopressin in Swiss 3T3 Mouse Cells
Addition of the mitogenic peptides bombesin and vasopressin to quiescent Swiss 3T3 mouse cells increased the cytosolic Ca2+ concentration without any measurable delay. In contrast, there was a significant lag period (16 ± 1.2 s) before platelet-derived growth factor (PDGF) increased cytosolic Ca2+ c...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1987-08, Vol.84 (16), p.5768-5772 |
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creator | Lopez-Rivas, Abelardo Mendoza, Stanley A. Nånberg, Eewa Sinnett-Smith, James Rozengurt, Enrique |
description | Addition of the mitogenic peptides bombesin and vasopressin to quiescent Swiss 3T3 mouse cells increased the cytosolic Ca2+ concentration without any measurable delay. In contrast, there was a significant lag period (16 ± 1.2 s) before platelet-derived growth factor (PDGF) increased cytosolic Ca2+ concentration. This lag was not diminished at high concentrations of either porcine or human PDGF. Similar results were obtained in 3T3 cells loaded with quin-2 or fura-2. The differences in the effects of bombesin, vasopressin, and PDGF on Ca2+ movements were also substantiated by measurements of 45Ca2+ efflux and of cellular 45Ca2+ content. Activation of protein kinase C by phorbol esters inhibited Ca2+ mobilization induced by either bombesin or vasopressin. In contrast, phorbol esters had no effect on PDGF-induced cytosolic Ca2+ concentration increase or acceleration of 45Ca2+ efflux. Finally, bombesin and vasopressin caused a rapid increase in the production of inositol 1,4,5-trisphosphate and inositol 1,3,4-trisphosphate, whereas PDGF, even at a saturating concentration, exerted only a small effect. These results indicate that the signal transduction pathways activated by PDGF that lead to Ca2+ mobilization can be distinguished from those utilized by bombesin and vasopressin. |
doi_str_mv | 10.1073/pnas.84.16.5768 |
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In contrast, there was a significant lag period (16 ± 1.2 s) before platelet-derived growth factor (PDGF) increased cytosolic Ca2+ concentration. This lag was not diminished at high concentrations of either porcine or human PDGF. Similar results were obtained in 3T3 cells loaded with quin-2 or fura-2. The differences in the effects of bombesin, vasopressin, and PDGF on Ca2+ movements were also substantiated by measurements of 45Ca2+ efflux and of cellular 45Ca2+ content. Activation of protein kinase C by phorbol esters inhibited Ca2+ mobilization induced by either bombesin or vasopressin. In contrast, phorbol esters had no effect on PDGF-induced cytosolic Ca2+ concentration increase or acceleration of 45Ca2+ efflux. Finally, bombesin and vasopressin caused a rapid increase in the production of inositol 1,4,5-trisphosphate and inositol 1,3,4-trisphosphate, whereas PDGF, even at a saturating concentration, exerted only a small effect. These results indicate that the signal transduction pathways activated by PDGF that lead to Ca2+ mobilization can be distinguished from those utilized by bombesin and vasopressin.</description><identifier>ISSN: 0027-8424</identifier><identifier>ISSN: 1091-6490</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.84.16.5768</identifier><identifier>PMID: 3039507</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>3T3 cells ; Animals ; Biological and medical sciences ; Bombesin - pharmacology ; Calcium - metabolism ; Cell growth ; Cell Line ; Cell physiology ; Cells ; Cultured cells ; DNA Replication - drug effects ; Fibroblasts - drug effects ; Fibroblasts - metabolism ; Fundamental and applied biological sciences. Psychology ; Humans ; Inositol phosphates ; Inositols ; Kinetics ; Mice ; Mitogens ; Molecular and cellular biology ; Phorbol esters ; Phorbol Esters - pharmacology ; Phosphatidylinositols - metabolism ; Platelet-Derived Growth Factor - pharmacology ; Responses to growth factors, tumor promotors, other factors ; Swine ; Swiss 3T3 cells ; Vasopressins - pharmacology</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1987-08, Vol.84 (16), p.5768-5772</ispartof><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4798-5f0eb69aba584f67a3756092a42aea66cb25bac5dd13d744eb24194f7012bea83</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/84/16.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/30121$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/30121$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,552,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8342436$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3039507$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://urn.kb.se/resolve?urn=urn:nbn:se:kau:diva-29820$$DView record from Swedish Publication Index$$Hfree_for_read</backlink><backlink>$$Uhttps://urn.kb.se/resolve?urn=urn:nbn:se:oru:diva-79037$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Lopez-Rivas, Abelardo</creatorcontrib><creatorcontrib>Mendoza, Stanley A.</creatorcontrib><creatorcontrib>Nånberg, Eewa</creatorcontrib><creatorcontrib>Sinnett-Smith, James</creatorcontrib><creatorcontrib>Rozengurt, Enrique</creatorcontrib><title>Ca2+-mobilizing Actions of Platelet-Derived Growth Factor Differ from Those of Bombesin and Vasopressin in Swiss 3T3 Mouse Cells</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Addition of the mitogenic peptides bombesin and vasopressin to quiescent Swiss 3T3 mouse cells increased the cytosolic Ca2+ concentration without any measurable delay. In contrast, there was a significant lag period (16 ± 1.2 s) before platelet-derived growth factor (PDGF) increased cytosolic Ca2+ concentration. This lag was not diminished at high concentrations of either porcine or human PDGF. Similar results were obtained in 3T3 cells loaded with quin-2 or fura-2. The differences in the effects of bombesin, vasopressin, and PDGF on Ca2+ movements were also substantiated by measurements of 45Ca2+ efflux and of cellular 45Ca2+ content. Activation of protein kinase C by phorbol esters inhibited Ca2+ mobilization induced by either bombesin or vasopressin. In contrast, phorbol esters had no effect on PDGF-induced cytosolic Ca2+ concentration increase or acceleration of 45Ca2+ efflux. Finally, bombesin and vasopressin caused a rapid increase in the production of inositol 1,4,5-trisphosphate and inositol 1,3,4-trisphosphate, whereas PDGF, even at a saturating concentration, exerted only a small effect. These results indicate that the signal transduction pathways activated by PDGF that lead to Ca2+ mobilization can be distinguished from those utilized by bombesin and vasopressin.</description><subject>3T3 cells</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Bombesin - pharmacology</subject><subject>Calcium - metabolism</subject><subject>Cell growth</subject><subject>Cell Line</subject><subject>Cell physiology</subject><subject>Cells</subject><subject>Cultured cells</subject><subject>DNA Replication - drug effects</subject><subject>Fibroblasts - drug effects</subject><subject>Fibroblasts - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Inositol phosphates</subject><subject>Inositols</subject><subject>Kinetics</subject><subject>Mice</subject><subject>Mitogens</subject><subject>Molecular and cellular biology</subject><subject>Phorbol esters</subject><subject>Phorbol Esters - pharmacology</subject><subject>Phosphatidylinositols - metabolism</subject><subject>Platelet-Derived Growth Factor - pharmacology</subject><subject>Responses to growth factors, tumor promotors, other factors</subject><subject>Swine</subject><subject>Swiss 3T3 cells</subject><subject>Vasopressins - pharmacology</subject><issn>0027-8424</issn><issn>1091-6490</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>D8T</sourceid><recordid>eNqNks-L1DAUx4so67h6FgQlB8GDdja_2jSHPYwz7iqsKDjuNby2yUzWthmSdkc9-aebMkPZvYiQEB7fz_e9wPclyXOC5wQLdrbrIMwLPif5PBN58SCZESxJmnOJHyYzjKlIC0754-RJCDcYY5kV-CQ5YZjJDItZ8mcJ9G3autI29rftNmhR9dZ1ATmDvjbQ60b36Up7e6trdOndvt-iC6h659HKGqM9Mt61aL11QY-e964tdbAdgq5G1xDczusw1vF829sQEFsz9NkNEV_qpglPk0cGmqCfHd_T5PvFh_XyY3r15fLTcnGVVlzIIs0M1mUuoYSs4CYXwESWY0mBU9CQ51VJsxKqrK4JqwXnuqScSG4EJrTUULDT5N2hb9jr3VCqnbct-F_KgVUre71Qzm_iHZSQmIn_w3_AoKgsKI74-QGPbKvrSne9h-ae677S2a3auNvRLjmP_rODv_IuBK_NZCVYjUGrMWhVcEVyNQYdHS_vTpz4Y7JRf33UIVTQGA9dZcOEFSxuBcsj9uaIjf0ndZqjzNA0vf7ZR_LVP8kIvDgANyGux50PEUrYX1Yp1Ic</recordid><startdate>19870801</startdate><enddate>19870801</enddate><creator>Lopez-Rivas, Abelardo</creator><creator>Mendoza, Stanley A.</creator><creator>Nånberg, Eewa</creator><creator>Sinnett-Smith, James</creator><creator>Rozengurt, Enrique</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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>5PM</scope><scope>ADTPV</scope><scope>AOWAS</scope><scope>DG3</scope><scope>AABEP</scope><scope>D8T</scope><scope>D91</scope><scope>ZZAVC</scope></search><sort><creationdate>19870801</creationdate><title>Ca2+-mobilizing Actions of Platelet-Derived Growth Factor Differ from Those of Bombesin and Vasopressin in Swiss 3T3 Mouse Cells</title><author>Lopez-Rivas, Abelardo ; Mendoza, Stanley A. ; Nånberg, Eewa ; Sinnett-Smith, James ; Rozengurt, Enrique</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4798-5f0eb69aba584f67a3756092a42aea66cb25bac5dd13d744eb24194f7012bea83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>3T3 cells</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Bombesin - pharmacology</topic><topic>Calcium - metabolism</topic><topic>Cell growth</topic><topic>Cell Line</topic><topic>Cell physiology</topic><topic>Cells</topic><topic>Cultured cells</topic><topic>DNA Replication - drug effects</topic><topic>Fibroblasts - drug effects</topic><topic>Fibroblasts - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Inositol phosphates</topic><topic>Inositols</topic><topic>Kinetics</topic><topic>Mice</topic><topic>Mitogens</topic><topic>Molecular and cellular biology</topic><topic>Phorbol esters</topic><topic>Phorbol Esters - pharmacology</topic><topic>Phosphatidylinositols - metabolism</topic><topic>Platelet-Derived Growth Factor - pharmacology</topic><topic>Responses to growth factors, tumor promotors, other factors</topic><topic>Swine</topic><topic>Swiss 3T3 cells</topic><topic>Vasopressins - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lopez-Rivas, Abelardo</creatorcontrib><creatorcontrib>Mendoza, Stanley A.</creatorcontrib><creatorcontrib>Nånberg, Eewa</creatorcontrib><creatorcontrib>Sinnett-Smith, James</creatorcontrib><creatorcontrib>Rozengurt, Enrique</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>PubMed Central (Full Participant titles)</collection><collection>SwePub</collection><collection>SwePub Articles</collection><collection>SWEPUB Karlstads universitet</collection><collection>SWEPUB Örebro universitet full text</collection><collection>SWEPUB Freely available online</collection><collection>SWEPUB Örebro universitet</collection><collection>SwePub Articles full text</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lopez-Rivas, Abelardo</au><au>Mendoza, Stanley A.</au><au>Nånberg, Eewa</au><au>Sinnett-Smith, James</au><au>Rozengurt, Enrique</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ca2+-mobilizing Actions of Platelet-Derived Growth Factor Differ from Those of Bombesin and Vasopressin in Swiss 3T3 Mouse Cells</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1987-08-01</date><risdate>1987</risdate><volume>84</volume><issue>16</issue><spage>5768</spage><epage>5772</epage><pages>5768-5772</pages><issn>0027-8424</issn><issn>1091-6490</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>Addition of the mitogenic peptides bombesin and vasopressin to quiescent Swiss 3T3 mouse cells increased the cytosolic Ca2+ concentration without any measurable delay. In contrast, there was a significant lag period (16 ± 1.2 s) before platelet-derived growth factor (PDGF) increased cytosolic Ca2+ concentration. This lag was not diminished at high concentrations of either porcine or human PDGF. Similar results were obtained in 3T3 cells loaded with quin-2 or fura-2. The differences in the effects of bombesin, vasopressin, and PDGF on Ca2+ movements were also substantiated by measurements of 45Ca2+ efflux and of cellular 45Ca2+ content. Activation of protein kinase C by phorbol esters inhibited Ca2+ mobilization induced by either bombesin or vasopressin. In contrast, phorbol esters had no effect on PDGF-induced cytosolic Ca2+ concentration increase or acceleration of 45Ca2+ efflux. Finally, bombesin and vasopressin caused a rapid increase in the production of inositol 1,4,5-trisphosphate and inositol 1,3,4-trisphosphate, whereas PDGF, even at a saturating concentration, exerted only a small effect. These results indicate that the signal transduction pathways activated by PDGF that lead to Ca2+ mobilization can be distinguished from those utilized by bombesin and vasopressin.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>3039507</pmid><doi>10.1073/pnas.84.16.5768</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | 3T3 cells Animals Biological and medical sciences Bombesin - pharmacology Calcium - metabolism Cell growth Cell Line Cell physiology Cells Cultured cells DNA Replication - drug effects Fibroblasts - drug effects Fibroblasts - metabolism Fundamental and applied biological sciences. Psychology Humans Inositol phosphates Inositols Kinetics Mice Mitogens Molecular and cellular biology Phorbol esters Phorbol Esters - pharmacology Phosphatidylinositols - metabolism Platelet-Derived Growth Factor - pharmacology Responses to growth factors, tumor promotors, other factors Swine Swiss 3T3 cells Vasopressins - pharmacology |
title | Ca2+-mobilizing Actions of Platelet-Derived Growth Factor Differ from Those of Bombesin and Vasopressin in Swiss 3T3 Mouse Cells |
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