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...

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Veröffentlicht in:Molecular reproduction and development 2006-12, Vol.73 (12), p.1564-1577
Hauptverfasser: Stricker, Stephen A., Smythe, Toni L.
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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
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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. 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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. 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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 &amp; inhibitors</topic><topic>Receptor, ErbB-2 - antagonists &amp; inhibitors</topic><topic>Seawater</topic><topic>Src</topic><topic>src-Family Kinases - antagonists &amp; 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 &amp; Fisheries Abstracts (ASFA) 1: Biological Sciences &amp; Living Resources</collection><collection>Aquatic Science &amp; 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>
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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
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