Differing mechanisms of cAMP- versus seawater-induced oocyte maturation in marine nemertean worms II. The roles of tyrosine kinases and phosphatases
Instead of blocking oocyte maturation as it does in most animals, cAMP causes oocytes of marine nemertean worms to initiate maturation (=germinal vesicle breakdown, “GVBD”). To characterize cAMP‐induced GVBD in nemerteans, inhibitors of tyrosine kinase signaling were tested on Cerebratulus sp. oocyt...
Gespeichert in:
Veröffentlicht in: | Molecular reproduction and development 2006-12, Vol.73 (12), p.1564-1577 |
---|---|
Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 1577 |
---|---|
container_issue | 12 |
container_start_page | 1564 |
container_title | Molecular reproduction and development |
container_volume | 73 |
creator | Stricker, Stephen A. Smythe, Toni L. |
description | Instead of blocking oocyte maturation as it does in most animals, cAMP causes oocytes of marine nemertean worms to initiate maturation (=germinal vesicle breakdown, “GVBD”). To characterize cAMP‐induced GVBD in nemerteans, inhibitors of tyrosine kinase signaling were tested on Cerebratulus sp. oocytes that had been incubated in cAMP‐elevating drugs versus seawater (SW) alone. Such tests yielded similar results for Src‐like tyrosine kinase blockers, as the inhibitors prevented mitogen‐activated protein kinase (MAPK) activation without stopping either GVBD or maturation‐promoting factor (MPF) activation in both SW and cAMP‐elevating treatments. Alternatively, genistein, a general tyrosine kinase antagonist, and piceatannol, an inhibitor of the tyrosine kinase Syk, reduced GVBD and MAPK/MPF activities in SW‐, but not cAMP‐induced maturation. Similarly, inhibitors of the human epidermal growth factor receptor‐2 (HER‐2) tyrosine kinase prevented GVBD and MAPK/MPF activations in oocytes treated with SW, but not with cAMP‐elevating drugs. Antagonists of either protein tyrosine phosphatases (PTPs) or the dual‐specificity phosphatase Cdc25 also reduced GVBD and MAPK/MPF activities in SW‐treated oocytes without generally affecting cAMP‐induced maturation. Collectively, these data suggest cAMP triggers GVBD via pathways that do not require MAPK activation or several components of tyrosine kinase signaling. In addition, such differences in tyrosine kinase cascades, coupled with the dissimilar patterns of Ser/Thr kinase signaling described in the accompanying study, indicate that nemertean oocytes are capable of utilizing multiple mechanisms to activate MPF during GVBD. Mol. Reprod. Dev. 73: 1564–1577, 2006. © 2006 Wiley‐Liss, Inc. |
doi_str_mv | 10.1002/mrd.20596 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_68902095</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>68902095</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4886-1a3ad03ec35f651f4d6babf6e172cf86b7d2f84a5bfe43b3d106ab4acee75f7a3</originalsourceid><addsrcrecordid>eNqFkUFv0zAUxyMEYmNw4AsgX5i0Qzo7Tpz4OK1stFoBoaEiLtaL80zNEqfYCaXfgw-MuxZ2QpxsP_3e78nvnyQvGZ0wSrPzzjeTjBZSPEqOGZVVmpWyeLy75zTNi-zzUfIshG-UUikr-jQ5YkLSTObyOPk1tcagt-4r6VCvwNnQBdIboi8WH1LyA30YAwkIGxjQp9Y1o8aG9L3eDkg6GEYPg-0dsS6-ogeJww79gODIpvdRNptNyO0Kie9bvFcPW9-HHXlnHYRYA9eQ9aoP6xUMu8Lz5ImBNuCLw3mSfLp6c3v5Nr15fz27vLhJdV5VImXAoaEcNS-MKJjJG1FDbQSyMtOmEnXZZKbKoagN5rzmDaMC6hw0YlmYEvhJcrr3rn3_fcQwqM4GjW0LDvsxKFHFNVFZ_BdkkvNCVmUEz_agjl8MHo1aexv3slWMql1WKmal7rOK7KuDdKw7bB7IQzgReH0AIGhojQenbXjgqozxSu648z23sS1u_z1RLT5O_4xO9x02DPjzbwf4OyVKXhZq-e5aTefzRfllvlRL_hvHQr4K</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>19335987</pqid></control><display><type>article</type><title>Differing mechanisms of cAMP- versus seawater-induced oocyte maturation in marine nemertean worms II. The roles of tyrosine kinases and phosphatases</title><source>MEDLINE</source><source>Access via Wiley Online Library</source><creator>Stricker, Stephen A. ; Smythe, Toni L.</creator><creatorcontrib>Stricker, Stephen A. ; Smythe, Toni L.</creatorcontrib><description>Instead of blocking oocyte maturation as it does in most animals, cAMP causes oocytes of marine nemertean worms to initiate maturation (=germinal vesicle breakdown, “GVBD”). To characterize cAMP‐induced GVBD in nemerteans, inhibitors of tyrosine kinase signaling were tested on Cerebratulus sp. oocytes that had been incubated in cAMP‐elevating drugs versus seawater (SW) alone. Such tests yielded similar results for Src‐like tyrosine kinase blockers, as the inhibitors prevented mitogen‐activated protein kinase (MAPK) activation without stopping either GVBD or maturation‐promoting factor (MPF) activation in both SW and cAMP‐elevating treatments. Alternatively, genistein, a general tyrosine kinase antagonist, and piceatannol, an inhibitor of the tyrosine kinase Syk, reduced GVBD and MAPK/MPF activities in SW‐, but not cAMP‐induced maturation. Similarly, inhibitors of the human epidermal growth factor receptor‐2 (HER‐2) tyrosine kinase prevented GVBD and MAPK/MPF activations in oocytes treated with SW, but not with cAMP‐elevating drugs. Antagonists of either protein tyrosine phosphatases (PTPs) or the dual‐specificity phosphatase Cdc25 also reduced GVBD and MAPK/MPF activities in SW‐treated oocytes without generally affecting cAMP‐induced maturation. Collectively, these data suggest cAMP triggers GVBD via pathways that do not require MAPK activation or several components of tyrosine kinase signaling. In addition, such differences in tyrosine kinase cascades, coupled with the dissimilar patterns of Ser/Thr kinase signaling described in the accompanying study, indicate that nemertean oocytes are capable of utilizing multiple mechanisms to activate MPF during GVBD. Mol. Reprod. Dev. 73: 1564–1577, 2006. © 2006 Wiley‐Liss, Inc.</description><identifier>ISSN: 1040-452X</identifier><identifier>EISSN: 1098-2795</identifier><identifier>DOI: 10.1002/mrd.20596</identifier><identifier>PMID: 16902949</identifier><identifier>CODEN: MREDEE</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Animals ; Annelida - physiology ; Annelida and closely related phyla: sipuncula. Echiura. Nemertinea ; Biological and medical sciences ; Butadienes - pharmacology ; Cdc25 ; cdc25 Phosphatases - antagonists & inhibitors ; Cerebratulus ; Cyclic AMP - pharmacology ; Eukaryotic Cells ; follicle cells ; Fundamental and applied biological sciences. Psychology ; Genistein - pharmacology ; HER-2 ; Intracellular Signaling Peptides and Proteins - metabolism ; Invertebrates ; Marine ; Maturation-Promoting Factor - metabolism ; Mitogen-Activated Protein Kinases - metabolism ; Models, Biological ; Nitriles - pharmacology ; Oocytes - drug effects ; Protein Tyrosine Phosphatases - physiology ; Protein-Tyrosine Kinases - metabolism ; Protein-Tyrosine Kinases - physiology ; PTP ; Receptor Protein-Tyrosine Kinases - antagonists & inhibitors ; Receptor, ErbB-2 - antagonists & inhibitors ; Seawater ; Src ; src-Family Kinases - antagonists & inhibitors ; Stilbenes - pharmacology ; Syk Kinase</subject><ispartof>Molecular reproduction and development, 2006-12, Vol.73 (12), p.1564-1577</ispartof><rights>Copyright © 2006 Wiley‐Liss, Inc.</rights><rights>2007 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4886-1a3ad03ec35f651f4d6babf6e172cf86b7d2f84a5bfe43b3d106ab4acee75f7a3</citedby><cites>FETCH-LOGICAL-c4886-1a3ad03ec35f651f4d6babf6e172cf86b7d2f84a5bfe43b3d106ab4acee75f7a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fmrd.20596$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fmrd.20596$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,781,785,1418,27929,27930,45579,45580</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18213899$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16902949$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Stricker, Stephen A.</creatorcontrib><creatorcontrib>Smythe, Toni L.</creatorcontrib><title>Differing mechanisms of cAMP- versus seawater-induced oocyte maturation in marine nemertean worms II. The roles of tyrosine kinases and phosphatases</title><title>Molecular reproduction and development</title><addtitle>Mol. Reprod. Dev</addtitle><description>Instead of blocking oocyte maturation as it does in most animals, cAMP causes oocytes of marine nemertean worms to initiate maturation (=germinal vesicle breakdown, “GVBD”). To characterize cAMP‐induced GVBD in nemerteans, inhibitors of tyrosine kinase signaling were tested on Cerebratulus sp. oocytes that had been incubated in cAMP‐elevating drugs versus seawater (SW) alone. Such tests yielded similar results for Src‐like tyrosine kinase blockers, as the inhibitors prevented mitogen‐activated protein kinase (MAPK) activation without stopping either GVBD or maturation‐promoting factor (MPF) activation in both SW and cAMP‐elevating treatments. Alternatively, genistein, a general tyrosine kinase antagonist, and piceatannol, an inhibitor of the tyrosine kinase Syk, reduced GVBD and MAPK/MPF activities in SW‐, but not cAMP‐induced maturation. Similarly, inhibitors of the human epidermal growth factor receptor‐2 (HER‐2) tyrosine kinase prevented GVBD and MAPK/MPF activations in oocytes treated with SW, but not with cAMP‐elevating drugs. Antagonists of either protein tyrosine phosphatases (PTPs) or the dual‐specificity phosphatase Cdc25 also reduced GVBD and MAPK/MPF activities in SW‐treated oocytes without generally affecting cAMP‐induced maturation. Collectively, these data suggest cAMP triggers GVBD via pathways that do not require MAPK activation or several components of tyrosine kinase signaling. In addition, such differences in tyrosine kinase cascades, coupled with the dissimilar patterns of Ser/Thr kinase signaling described in the accompanying study, indicate that nemertean oocytes are capable of utilizing multiple mechanisms to activate MPF during GVBD. Mol. Reprod. Dev. 73: 1564–1577, 2006. © 2006 Wiley‐Liss, Inc.</description><subject>Animals</subject><subject>Annelida - physiology</subject><subject>Annelida and closely related phyla: sipuncula. Echiura. Nemertinea</subject><subject>Biological and medical sciences</subject><subject>Butadienes - pharmacology</subject><subject>Cdc25</subject><subject>cdc25 Phosphatases - antagonists & inhibitors</subject><subject>Cerebratulus</subject><subject>Cyclic AMP - pharmacology</subject><subject>Eukaryotic Cells</subject><subject>follicle cells</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genistein - pharmacology</subject><subject>HER-2</subject><subject>Intracellular Signaling Peptides and Proteins - metabolism</subject><subject>Invertebrates</subject><subject>Marine</subject><subject>Maturation-Promoting Factor - metabolism</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>Models, Biological</subject><subject>Nitriles - pharmacology</subject><subject>Oocytes - drug effects</subject><subject>Protein Tyrosine Phosphatases - physiology</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Protein-Tyrosine Kinases - physiology</subject><subject>PTP</subject><subject>Receptor Protein-Tyrosine Kinases - antagonists & inhibitors</subject><subject>Receptor, ErbB-2 - antagonists & inhibitors</subject><subject>Seawater</subject><subject>Src</subject><subject>src-Family Kinases - antagonists & inhibitors</subject><subject>Stilbenes - pharmacology</subject><subject>Syk Kinase</subject><issn>1040-452X</issn><issn>1098-2795</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFv0zAUxyMEYmNw4AsgX5i0Qzo7Tpz4OK1stFoBoaEiLtaL80zNEqfYCaXfgw-MuxZ2QpxsP_3e78nvnyQvGZ0wSrPzzjeTjBZSPEqOGZVVmpWyeLy75zTNi-zzUfIshG-UUikr-jQ5YkLSTObyOPk1tcagt-4r6VCvwNnQBdIboi8WH1LyA30YAwkIGxjQp9Y1o8aG9L3eDkg6GEYPg-0dsS6-ogeJww79gODIpvdRNptNyO0Kie9bvFcPW9-HHXlnHYRYA9eQ9aoP6xUMu8Lz5ImBNuCLw3mSfLp6c3v5Nr15fz27vLhJdV5VImXAoaEcNS-MKJjJG1FDbQSyMtOmEnXZZKbKoagN5rzmDaMC6hw0YlmYEvhJcrr3rn3_fcQwqM4GjW0LDvsxKFHFNVFZ_BdkkvNCVmUEz_agjl8MHo1aexv3slWMql1WKmal7rOK7KuDdKw7bB7IQzgReH0AIGhojQenbXjgqozxSu648z23sS1u_z1RLT5O_4xO9x02DPjzbwf4OyVKXhZq-e5aTefzRfllvlRL_hvHQr4K</recordid><startdate>200612</startdate><enddate>200612</enddate><creator>Stricker, Stephen A.</creator><creator>Smythe, Toni L.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley-Liss</general><scope>BSCLL</scope><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>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>200612</creationdate><title>Differing mechanisms of cAMP- versus seawater-induced oocyte maturation in marine nemertean worms II. The roles of tyrosine kinases and phosphatases</title><author>Stricker, Stephen A. ; Smythe, Toni L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4886-1a3ad03ec35f651f4d6babf6e172cf86b7d2f84a5bfe43b3d106ab4acee75f7a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Animals</topic><topic>Annelida - physiology</topic><topic>Annelida and closely related phyla: sipuncula. Echiura. Nemertinea</topic><topic>Biological and medical sciences</topic><topic>Butadienes - pharmacology</topic><topic>Cdc25</topic><topic>cdc25 Phosphatases - antagonists & inhibitors</topic><topic>Cerebratulus</topic><topic>Cyclic AMP - pharmacology</topic><topic>Eukaryotic Cells</topic><topic>follicle cells</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genistein - pharmacology</topic><topic>HER-2</topic><topic>Intracellular Signaling Peptides and Proteins - metabolism</topic><topic>Invertebrates</topic><topic>Marine</topic><topic>Maturation-Promoting Factor - metabolism</topic><topic>Mitogen-Activated Protein Kinases - metabolism</topic><topic>Models, Biological</topic><topic>Nitriles - pharmacology</topic><topic>Oocytes - drug effects</topic><topic>Protein Tyrosine Phosphatases - physiology</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Protein-Tyrosine Kinases - physiology</topic><topic>PTP</topic><topic>Receptor Protein-Tyrosine Kinases - antagonists & inhibitors</topic><topic>Receptor, ErbB-2 - antagonists & inhibitors</topic><topic>Seawater</topic><topic>Src</topic><topic>src-Family Kinases - antagonists & inhibitors</topic><topic>Stilbenes - pharmacology</topic><topic>Syk Kinase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Stricker, Stephen A.</creatorcontrib><creatorcontrib>Smythe, Toni L.</creatorcontrib><collection>Istex</collection><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>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular reproduction and development</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Stricker, Stephen A.</au><au>Smythe, Toni L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differing mechanisms of cAMP- versus seawater-induced oocyte maturation in marine nemertean worms II. The roles of tyrosine kinases and phosphatases</atitle><jtitle>Molecular reproduction and development</jtitle><addtitle>Mol. Reprod. Dev</addtitle><date>2006-12</date><risdate>2006</risdate><volume>73</volume><issue>12</issue><spage>1564</spage><epage>1577</epage><pages>1564-1577</pages><issn>1040-452X</issn><eissn>1098-2795</eissn><coden>MREDEE</coden><abstract>Instead of blocking oocyte maturation as it does in most animals, cAMP causes oocytes of marine nemertean worms to initiate maturation (=germinal vesicle breakdown, “GVBD”). To characterize cAMP‐induced GVBD in nemerteans, inhibitors of tyrosine kinase signaling were tested on Cerebratulus sp. oocytes that had been incubated in cAMP‐elevating drugs versus seawater (SW) alone. Such tests yielded similar results for Src‐like tyrosine kinase blockers, as the inhibitors prevented mitogen‐activated protein kinase (MAPK) activation without stopping either GVBD or maturation‐promoting factor (MPF) activation in both SW and cAMP‐elevating treatments. Alternatively, genistein, a general tyrosine kinase antagonist, and piceatannol, an inhibitor of the tyrosine kinase Syk, reduced GVBD and MAPK/MPF activities in SW‐, but not cAMP‐induced maturation. Similarly, inhibitors of the human epidermal growth factor receptor‐2 (HER‐2) tyrosine kinase prevented GVBD and MAPK/MPF activations in oocytes treated with SW, but not with cAMP‐elevating drugs. Antagonists of either protein tyrosine phosphatases (PTPs) or the dual‐specificity phosphatase Cdc25 also reduced GVBD and MAPK/MPF activities in SW‐treated oocytes without generally affecting cAMP‐induced maturation. Collectively, these data suggest cAMP triggers GVBD via pathways that do not require MAPK activation or several components of tyrosine kinase signaling. In addition, such differences in tyrosine kinase cascades, coupled with the dissimilar patterns of Ser/Thr kinase signaling described in the accompanying study, indicate that nemertean oocytes are capable of utilizing multiple mechanisms to activate MPF during GVBD. Mol. Reprod. Dev. 73: 1564–1577, 2006. © 2006 Wiley‐Liss, Inc.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>16902949</pmid><doi>10.1002/mrd.20596</doi><tpages>14</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1040-452X |
ispartof | Molecular reproduction and development, 2006-12, Vol.73 (12), p.1564-1577 |
issn | 1040-452X 1098-2795 |
language | eng |
recordid | cdi_proquest_miscellaneous_68902095 |
source | MEDLINE; Access via Wiley Online Library |
subjects | Animals Annelida - physiology Annelida and closely related phyla: sipuncula. Echiura. Nemertinea Biological and medical sciences Butadienes - pharmacology Cdc25 cdc25 Phosphatases - antagonists & inhibitors Cerebratulus Cyclic AMP - pharmacology Eukaryotic Cells follicle cells Fundamental and applied biological sciences. Psychology Genistein - pharmacology HER-2 Intracellular Signaling Peptides and Proteins - metabolism Invertebrates Marine Maturation-Promoting Factor - metabolism Mitogen-Activated Protein Kinases - metabolism Models, Biological Nitriles - pharmacology Oocytes - drug effects Protein Tyrosine Phosphatases - physiology Protein-Tyrosine Kinases - metabolism Protein-Tyrosine Kinases - physiology PTP Receptor Protein-Tyrosine Kinases - antagonists & inhibitors Receptor, ErbB-2 - antagonists & inhibitors Seawater Src src-Family Kinases - antagonists & inhibitors Stilbenes - pharmacology Syk Kinase |
title | Differing mechanisms of cAMP- versus seawater-induced oocyte maturation in marine nemertean worms II. The roles of tyrosine kinases and phosphatases |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-11T21%3A16%3A53IST&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=Differing%20mechanisms%20of%20cAMP-%20versus%20seawater-induced%20oocyte%20maturation%20in%20marine%20nemertean%20worms%20II.%20The%20roles%20of%20tyrosine%20kinases%20and%20phosphatases&rft.jtitle=Molecular%20reproduction%20and%20development&rft.au=Stricker,%20Stephen%20A.&rft.date=2006-12&rft.volume=73&rft.issue=12&rft.spage=1564&rft.epage=1577&rft.pages=1564-1577&rft.issn=1040-452X&rft.eissn=1098-2795&rft.coden=MREDEE&rft_id=info:doi/10.1002/mrd.20596&rft_dat=%3Cproquest_cross%3E68902095%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=19335987&rft_id=info:pmid/16902949&rfr_iscdi=true |