Tyrosine Phosphorylation of Caveolin 1 by Oxidative Stress Is Reversible and Dependent on the c-src Tyrosine Kinase but Not Mitogen-Activated Protein Kinase Pathways in Placental Artery Endothelial Cells
Acute H 2 O 2 exposure to placental artery endothelial cells induced an array of tyrosine-phosphorylated proteins, including caveolin 1 (CAV1) rapid and transient tyr 14 phosphorylated in a time- and concentration-dependent manner. Basal tyr 14 phosphorylated CAV1 was primarily located at the edges...
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| Veröffentlicht in: | Biology of reproduction 2005-10, Vol.73 (4), p.761-772 |
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| creator | CHEN, Dong-Bao LI, Su-Min QIAN, Xiao-Xian MOON, Chongsoo JING ZHENG |
| description | Acute H 2 O 2 exposure to placental artery endothelial cells induced an array of tyrosine-phosphorylated proteins, including caveolin 1
(CAV1) rapid and transient tyr 14 phosphorylated in a time- and concentration-dependent manner. Basal tyr 14 phosphorylated CAV1 was primarily located at the edges of cells and associated with actin filaments. Phosphorylated CAV1
was markedly increased and diffused with the disorganization of actin filaments at 20 min, disappeared at 120 min treatment
with 0.2 mM H 2 O 2 . Treatment with H 2 O 2 also disorganized actin filaments and changed cell shape in a time-dependent manner. Pretreatment with antioxidants catalase
completely, whereas the other tested superoxide dismutase, N-acetyl- l -cysteine and sodium formate partially attenuated H 2 O 2 -induced CAV1 phosphorylation in a concentration-dependent manner. Acute treatment with H 2 O 2 activated multiple signaling pathways, including the mitogen-activated protein kinases (MAPK) members (MAPK3/1-ERK2/1, MAPK8/9-JNK1/2,
and MAPK11-p38 mapk ) and the c-src tyrosine kinase (CSK). Pharmacological studies demonstrated that, among these pathways, only the blockade
of CSK activation abolished H 2 O 2 -induced CAV1 phosphorylation. Additionally, H 2 O 2 -induced CAV1 phosphorylation was reversible rapidly ( |
| doi_str_mv | 10.1095/biolreprod.105.040881 |
| format | Article |
| fullrecord | <record><control><sourceid>pubmed_pasca</sourceid><recordid>TN_cdi_pubmed_primary_15958730</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>15958730</sourcerecordid><originalsourceid>FETCH-LOGICAL-h269t-cd7039fc308ccf59f176d4fd090b5cbf5d80fc26c8b38a5fc2352102c4cc13d73</originalsourceid><addsrcrecordid>eNpFkc1u1DAURi0EotPCI4DuhmWKHcf5WY6GAhWFjqCsI8e-aYw8dmS7E_KMvFQtMdDVtT8fnU_yJeQNo5eMduL9YLwNOAev811c0oq2LXtGNkyUXdGUdfucbCildcF5zc_IeYy_KGUVL_lLcsZEJ9qG0w35c7cGH41D2E8-zpMPq5XJeAd-hJ08orfGAYNhhdvfRuenI8KPFDBGuI7wHY8YohksgnQaPuCMTqNLkAVpQlBFDAr-d3wxTkaE4SHBN5_gq0n-Hl2xVVkrE2rYB58wF57AvUzTItcIOdpbqbJZWtiGhGGFK6d97rAmRzu0Nr4iL0ZpI74-zQvy8-PV3e5zcXP76Xq3vSmmsu5SoXRDeTcqTlulRtGNrKl1NWra0UGoYRS6paMqa9UOvJUiH7koGS1VpRTjuuEX5O1f7_wwHFD3czAHGdb-369m4N0JkFFJOwbplIlPXMPyfqruiZvM_bSYgH08SGuzlvfLsjS8r_qmZvwRicibSA</addsrcrecordid><sourcetype>Index Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Tyrosine Phosphorylation of Caveolin 1 by Oxidative Stress Is Reversible and Dependent on the c-src Tyrosine Kinase but Not Mitogen-Activated Protein Kinase Pathways in Placental Artery Endothelial Cells</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>BioOne Complete</source><source>Oxford University Press Journals All Titles (1996-Current)</source><creator>CHEN, Dong-Bao ; LI, Su-Min ; QIAN, Xiao-Xian ; MOON, Chongsoo ; JING ZHENG</creator><creatorcontrib>CHEN, Dong-Bao ; LI, Su-Min ; QIAN, Xiao-Xian ; MOON, Chongsoo ; JING ZHENG</creatorcontrib><description>Acute H 2 O 2 exposure to placental artery endothelial cells induced an array of tyrosine-phosphorylated proteins, including caveolin 1
(CAV1) rapid and transient tyr 14 phosphorylated in a time- and concentration-dependent manner. Basal tyr 14 phosphorylated CAV1 was primarily located at the edges of cells and associated with actin filaments. Phosphorylated CAV1
was markedly increased and diffused with the disorganization of actin filaments at 20 min, disappeared at 120 min treatment
with 0.2 mM H 2 O 2 . Treatment with H 2 O 2 also disorganized actin filaments and changed cell shape in a time-dependent manner. Pretreatment with antioxidants catalase
completely, whereas the other tested superoxide dismutase, N-acetyl- l -cysteine and sodium formate partially attenuated H 2 O 2 -induced CAV1 phosphorylation in a concentration-dependent manner. Acute treatment with H 2 O 2 activated multiple signaling pathways, including the mitogen-activated protein kinases (MAPK) members (MAPK3/1-ERK2/1, MAPK8/9-JNK1/2,
and MAPK11-p38 mapk ) and the c-src tyrosine kinase (CSK). Pharmacological studies demonstrated that, among these pathways, only the blockade
of CSK activation abolished H 2 O 2 -induced CAV1 phosphorylation. Additionally, H 2 O 2 -induced CAV1 phosphorylation was reversible rapidly (<10 min) upon H 2 O 2 withdrawal. Because maternal and fetal endothelia must make dynamic adaptations to oxidative stress resulting from enhanced
pregnancy-specific oxygen metabolism favoring prooxidant production, which is emerging as one of the leading causes of the
dysfunctional activated endothelium during pregnancy, these unique features of CAV1 phosphorylation on oxidative stress observed
implicate an important role of CAV1 in placental endothelial cell biology during pregnancy.
Abstract
Tyrosine phosphorylation of caveolin 1 by oxidative stress is reversible, inhibited by antioxidants, and dependent on the
CSK but not mitogen-activated protein kinase pathways in placental artery endothelial cells</description><identifier>ISSN: 0006-3363</identifier><identifier>EISSN: 1529-7268</identifier><identifier>DOI: 10.1095/biolreprod.105.040881</identifier><identifier>PMID: 15958730</identifier><identifier>CODEN: BIREBV</identifier><language>eng</language><publisher>Madison, WI: Society for the Study of Reproduction</publisher><subject>Animals ; Antioxidants - pharmacology ; Arteries - cytology ; Arteries - drug effects ; Arteries - metabolism ; Biological and medical sciences ; Caveolin 1 - metabolism ; Cells, Cultured ; CSK Tyrosine-Protein Kinase ; Dose-Response Relationship, Drug ; Endothelial Cells - drug effects ; Endothelial Cells - metabolism ; Female ; Fundamental and applied biological sciences. Psychology ; Hydrogen Peroxide - pharmacology ; Mammalian male genital system ; MAP Kinase Signaling System ; Morphology. Physiology ; Oxidative Stress ; Phosphorylation ; Placenta - cytology ; Placenta - drug effects ; Placenta - metabolism ; Pregnancy ; Protein-Tyrosine Kinases - metabolism ; Sheep ; src-Family Kinases ; Tyrosine - metabolism ; Vertebrates: reproduction</subject><ispartof>Biology of reproduction, 2005-10, Vol.73 (4), p.761-772</ispartof><rights>2005 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17126849$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15958730$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>CHEN, Dong-Bao</creatorcontrib><creatorcontrib>LI, Su-Min</creatorcontrib><creatorcontrib>QIAN, Xiao-Xian</creatorcontrib><creatorcontrib>MOON, Chongsoo</creatorcontrib><creatorcontrib>JING ZHENG</creatorcontrib><title>Tyrosine Phosphorylation of Caveolin 1 by Oxidative Stress Is Reversible and Dependent on the c-src Tyrosine Kinase but Not Mitogen-Activated Protein Kinase Pathways in Placental Artery Endothelial Cells</title><title>Biology of reproduction</title><addtitle>Biol Reprod</addtitle><description>Acute H 2 O 2 exposure to placental artery endothelial cells induced an array of tyrosine-phosphorylated proteins, including caveolin 1
(CAV1) rapid and transient tyr 14 phosphorylated in a time- and concentration-dependent manner. Basal tyr 14 phosphorylated CAV1 was primarily located at the edges of cells and associated with actin filaments. Phosphorylated CAV1
was markedly increased and diffused with the disorganization of actin filaments at 20 min, disappeared at 120 min treatment
with 0.2 mM H 2 O 2 . Treatment with H 2 O 2 also disorganized actin filaments and changed cell shape in a time-dependent manner. Pretreatment with antioxidants catalase
completely, whereas the other tested superoxide dismutase, N-acetyl- l -cysteine and sodium formate partially attenuated H 2 O 2 -induced CAV1 phosphorylation in a concentration-dependent manner. Acute treatment with H 2 O 2 activated multiple signaling pathways, including the mitogen-activated protein kinases (MAPK) members (MAPK3/1-ERK2/1, MAPK8/9-JNK1/2,
and MAPK11-p38 mapk ) and the c-src tyrosine kinase (CSK). Pharmacological studies demonstrated that, among these pathways, only the blockade
of CSK activation abolished H 2 O 2 -induced CAV1 phosphorylation. Additionally, H 2 O 2 -induced CAV1 phosphorylation was reversible rapidly (<10 min) upon H 2 O 2 withdrawal. Because maternal and fetal endothelia must make dynamic adaptations to oxidative stress resulting from enhanced
pregnancy-specific oxygen metabolism favoring prooxidant production, which is emerging as one of the leading causes of the
dysfunctional activated endothelium during pregnancy, these unique features of CAV1 phosphorylation on oxidative stress observed
implicate an important role of CAV1 in placental endothelial cell biology during pregnancy.
Abstract
Tyrosine phosphorylation of caveolin 1 by oxidative stress is reversible, inhibited by antioxidants, and dependent on the
CSK but not mitogen-activated protein kinase pathways in placental artery endothelial cells</description><subject>Animals</subject><subject>Antioxidants - pharmacology</subject><subject>Arteries - cytology</subject><subject>Arteries - drug effects</subject><subject>Arteries - metabolism</subject><subject>Biological and medical sciences</subject><subject>Caveolin 1 - metabolism</subject><subject>Cells, Cultured</subject><subject>CSK Tyrosine-Protein Kinase</subject><subject>Dose-Response Relationship, Drug</subject><subject>Endothelial Cells - drug effects</subject><subject>Endothelial Cells - metabolism</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen Peroxide - pharmacology</subject><subject>Mammalian male genital system</subject><subject>MAP Kinase Signaling System</subject><subject>Morphology. Physiology</subject><subject>Oxidative Stress</subject><subject>Phosphorylation</subject><subject>Placenta - cytology</subject><subject>Placenta - drug effects</subject><subject>Placenta - metabolism</subject><subject>Pregnancy</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Sheep</subject><subject>src-Family Kinases</subject><subject>Tyrosine - metabolism</subject><subject>Vertebrates: reproduction</subject><issn>0006-3363</issn><issn>1529-7268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkc1u1DAURi0EotPCI4DuhmWKHcf5WY6GAhWFjqCsI8e-aYw8dmS7E_KMvFQtMdDVtT8fnU_yJeQNo5eMduL9YLwNOAev811c0oq2LXtGNkyUXdGUdfucbCildcF5zc_IeYy_KGUVL_lLcsZEJ9qG0w35c7cGH41D2E8-zpMPq5XJeAd-hJ08orfGAYNhhdvfRuenI8KPFDBGuI7wHY8YohksgnQaPuCMTqNLkAVpQlBFDAr-d3wxTkaE4SHBN5_gq0n-Hl2xVVkrE2rYB58wF57AvUzTItcIOdpbqbJZWtiGhGGFK6d97rAmRzu0Nr4iL0ZpI74-zQvy8-PV3e5zcXP76Xq3vSmmsu5SoXRDeTcqTlulRtGNrKl1NWra0UGoYRS6paMqa9UOvJUiH7koGS1VpRTjuuEX5O1f7_wwHFD3czAHGdb-369m4N0JkFFJOwbplIlPXMPyfqruiZvM_bSYgH08SGuzlvfLsjS8r_qmZvwRicibSA</recordid><startdate>20051001</startdate><enddate>20051001</enddate><creator>CHEN, Dong-Bao</creator><creator>LI, Su-Min</creator><creator>QIAN, Xiao-Xian</creator><creator>MOON, Chongsoo</creator><creator>JING ZHENG</creator><general>Society for the Study of Reproduction</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope></search><sort><creationdate>20051001</creationdate><title>Tyrosine Phosphorylation of Caveolin 1 by Oxidative Stress Is Reversible and Dependent on the c-src Tyrosine Kinase but Not Mitogen-Activated Protein Kinase Pathways in Placental Artery Endothelial Cells</title><author>CHEN, Dong-Bao ; LI, Su-Min ; QIAN, Xiao-Xian ; MOON, Chongsoo ; JING ZHENG</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h269t-cd7039fc308ccf59f176d4fd090b5cbf5d80fc26c8b38a5fc2352102c4cc13d73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Animals</topic><topic>Antioxidants - pharmacology</topic><topic>Arteries - cytology</topic><topic>Arteries - drug effects</topic><topic>Arteries - metabolism</topic><topic>Biological and medical sciences</topic><topic>Caveolin 1 - metabolism</topic><topic>Cells, Cultured</topic><topic>CSK Tyrosine-Protein Kinase</topic><topic>Dose-Response Relationship, Drug</topic><topic>Endothelial Cells - drug effects</topic><topic>Endothelial Cells - metabolism</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen Peroxide - pharmacology</topic><topic>Mammalian male genital system</topic><topic>MAP Kinase Signaling System</topic><topic>Morphology. Physiology</topic><topic>Oxidative Stress</topic><topic>Phosphorylation</topic><topic>Placenta - cytology</topic><topic>Placenta - drug effects</topic><topic>Placenta - metabolism</topic><topic>Pregnancy</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Sheep</topic><topic>src-Family Kinases</topic><topic>Tyrosine - metabolism</topic><topic>Vertebrates: reproduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>CHEN, Dong-Bao</creatorcontrib><creatorcontrib>LI, Su-Min</creatorcontrib><creatorcontrib>QIAN, Xiao-Xian</creatorcontrib><creatorcontrib>MOON, Chongsoo</creatorcontrib><creatorcontrib>JING ZHENG</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>Biology of reproduction</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>CHEN, Dong-Bao</au><au>LI, Su-Min</au><au>QIAN, Xiao-Xian</au><au>MOON, Chongsoo</au><au>JING ZHENG</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tyrosine Phosphorylation of Caveolin 1 by Oxidative Stress Is Reversible and Dependent on the c-src Tyrosine Kinase but Not Mitogen-Activated Protein Kinase Pathways in Placental Artery Endothelial Cells</atitle><jtitle>Biology of reproduction</jtitle><addtitle>Biol Reprod</addtitle><date>2005-10-01</date><risdate>2005</risdate><volume>73</volume><issue>4</issue><spage>761</spage><epage>772</epage><pages>761-772</pages><issn>0006-3363</issn><eissn>1529-7268</eissn><coden>BIREBV</coden><abstract>Acute H 2 O 2 exposure to placental artery endothelial cells induced an array of tyrosine-phosphorylated proteins, including caveolin 1
(CAV1) rapid and transient tyr 14 phosphorylated in a time- and concentration-dependent manner. Basal tyr 14 phosphorylated CAV1 was primarily located at the edges of cells and associated with actin filaments. Phosphorylated CAV1
was markedly increased and diffused with the disorganization of actin filaments at 20 min, disappeared at 120 min treatment
with 0.2 mM H 2 O 2 . Treatment with H 2 O 2 also disorganized actin filaments and changed cell shape in a time-dependent manner. Pretreatment with antioxidants catalase
completely, whereas the other tested superoxide dismutase, N-acetyl- l -cysteine and sodium formate partially attenuated H 2 O 2 -induced CAV1 phosphorylation in a concentration-dependent manner. Acute treatment with H 2 O 2 activated multiple signaling pathways, including the mitogen-activated protein kinases (MAPK) members (MAPK3/1-ERK2/1, MAPK8/9-JNK1/2,
and MAPK11-p38 mapk ) and the c-src tyrosine kinase (CSK). Pharmacological studies demonstrated that, among these pathways, only the blockade
of CSK activation abolished H 2 O 2 -induced CAV1 phosphorylation. Additionally, H 2 O 2 -induced CAV1 phosphorylation was reversible rapidly (<10 min) upon H 2 O 2 withdrawal. Because maternal and fetal endothelia must make dynamic adaptations to oxidative stress resulting from enhanced
pregnancy-specific oxygen metabolism favoring prooxidant production, which is emerging as one of the leading causes of the
dysfunctional activated endothelium during pregnancy, these unique features of CAV1 phosphorylation on oxidative stress observed
implicate an important role of CAV1 in placental endothelial cell biology during pregnancy.
Abstract
Tyrosine phosphorylation of caveolin 1 by oxidative stress is reversible, inhibited by antioxidants, and dependent on the
CSK but not mitogen-activated protein kinase pathways in placental artery endothelial cells</abstract><cop>Madison, WI</cop><pub>Society for the Study of Reproduction</pub><pmid>15958730</pmid><doi>10.1095/biolreprod.105.040881</doi><tpages>12</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Biology of reproduction, 2005-10, Vol.73 (4), p.761-772 |
| issn | 0006-3363 1529-7268 |
| language | eng |
| recordid | cdi_pubmed_primary_15958730 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; BioOne Complete; Oxford University Press Journals All Titles (1996-Current) |
| subjects | Animals Antioxidants - pharmacology Arteries - cytology Arteries - drug effects Arteries - metabolism Biological and medical sciences Caveolin 1 - metabolism Cells, Cultured CSK Tyrosine-Protein Kinase Dose-Response Relationship, Drug Endothelial Cells - drug effects Endothelial Cells - metabolism Female Fundamental and applied biological sciences. Psychology Hydrogen Peroxide - pharmacology Mammalian male genital system MAP Kinase Signaling System Morphology. Physiology Oxidative Stress Phosphorylation Placenta - cytology Placenta - drug effects Placenta - metabolism Pregnancy Protein-Tyrosine Kinases - metabolism Sheep src-Family Kinases Tyrosine - metabolism Vertebrates: reproduction |
| title | Tyrosine Phosphorylation of Caveolin 1 by Oxidative Stress Is Reversible and Dependent on the c-src Tyrosine Kinase but Not Mitogen-Activated Protein Kinase Pathways in Placental Artery Endothelial Cells |
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