title: Differing mechanisms of cAMP- versus seawater-induced oocyte maturation in marine nemertean worms II. The roles of tyrosine kinases and phosphatases.
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.
authors.affiliation: Department of Biology, University of New Mexcio, Albuquerque, 87131, USA. sstr@unm.edu
authors.forename: Stephen A
authors.initials: SA
authors.lastname: Stricker
authors.forename: Toni L
authors.initials: TL
authors.lastname: Smythe
mesh_terms: D000818:Animals; D000845:Annelida / Q000502:physiology*; D002070:Butadienes / Q000494:pharmacology; D000242:Cyclic AMP / Q000494:pharmacology*; D005057:Eukaryotic Cells; D019833:Genistein / Q000494:pharmacology; D047908:Intracellular Signaling Peptides and Proteins / Q000378:metabolism; D016200:Maturation-Promoting Factor / Q000378:metabolism; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism; D008954:Models, Biological; D009570:Nitriles / Q000494:pharmacology; D009865:Oocytes / Q000187:drug effects*; D017027:Protein Tyrosine Phosphatases / Q000502:physiology*; D011505:Protein-Tyrosine Kinases / Q000378:metabolism / Q000502:physiology*; D020794:Receptor Protein-Tyrosine Kinases / Q000037:antagonists & inhibitors; D018719:Erb-b2 Receptor Tyrosine Kinases / Q000037:antagonists & inhibitors; D012623:Seawater; D013267:Stilbenes / Q000494:pharmacology; D000072377:Syk Kinase; D020687:cdc25 Phosphatases / Q000037:antagonists & inhibitors; D019061:src-Family Kinases / Q000037:antagonists & inhibitors
chemical_list: D002070:Butadienes; D000242:Cyclic AMP; D019833:Genistein; D047908:Intracellular Signaling Peptides and Proteins; D016200:Maturation-Promoting Factor; D020928:Mitogen-Activated Protein Kinases; D009570:Nitriles; D017027:Protein Tyrosine Phosphatases; D011505:Protein-Tyrosine Kinases; D020794:Receptor Protein-Tyrosine Kinases; D018719:Erb-b2 Receptor Tyrosine Kinases; D013267:Stilbenes; D000072377:Syk Kinase; D020687:cdc25 Phosphatases; D019061:src-Family Kinases; C113580:U 0126; C041525:3,3',4,5'-tetrahydroxystilbene; C000606896:SYK protein, human