Cation channels in oocytes and early states of development: a novel type of nonselective cation channel activated by adrenaline in a clonal mesoderm-like cell line (MES-1).
The expression of receptors and ion channels alters during growth, maturation, and after fertilization of oocytes reflecting functional changes. Besides voltage-dependent ion channels, oocyte membranes possess an IP3-activated cation channel mediating a prolonged Ca2+ influx. The Ca2+ is thought to be involved in maturation and fertilization. Alternatively, mono- and divalent cations can enter oocytes via stretch-activated channels. The oocyte channel population is further modified during subsequent embryogenesis, suggesting that ionic channels obviously become expressed at specific states of embryological differentiation and in tissue-specific manner. The resulting differences in functional ion channel populations of adult cells underlie the large diversity of cells and their function. Conversely, differentiation and cell proliferation themselves depend on ion transport. Ca2+ ions have been shown to play a pivotal role in these processes. Nonselective cation channels represent one possible pathway for Ca2+ entry into the cell and, therefore, might be involved in the regulation of embryological development. Undifferentiated embryonal carcinoma cells (P19), visceral endoderm-like cells (END-2), epithelioid ectoderm-like cells (EPI-7), mesoderm-like cells (MES-1), and parietal yolk sac cells (PYS-2) have been used as a model to study the expression of ionic channels during early development. In MES-1 cells a nonselective cation current was activated by adrenaline. Interestingly, the intracellular pathway for activation of these channels involved the cascade of activation of the cAMP-dependent protein kinase (PKA) resulting in protein phosphorylation. This mechanism is well known for Ca2+ channel stimulation in cardiac and skeletal muscle both originating from the mesoderm.
Kleppisch
T
T
Institut für Physiologie, Humboldt-Universität zu Berlin, FRG.
Wobus
A M
AM
Hescheler
J
J
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D001920:Bradykinin / Q000494:pharmacology; D002118:Calcium / Q000378:metabolism*; D015220:Calcium Channels / Q000187:drug effects / Q000502:physiology; D002217:Carbachol / Q000494:pharmacology; D002412:Cations / Q000378:metabolism; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D002999:Clone Cells; D005576:Colforsin / Q000494:pharmacology; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism; D004837:Epinephrine / Q000494:pharmacology*; D005260:Female; D007473:Ion Channels / Q000187:drug effects / Q000502:physiology*; D007545:Isoproterenol / Q000494:pharmacology; D008648:Mesoderm / Q000166:cytology / Q000502:physiology*; D008954:Models, Biological; D009865:Oocytes / Q000502:physiology*; D012701:Serotonin / Q000494:pharmacology; D013004:Somatostatin / Q000494:pharmacology; D013724:Teratoma; D014981:Xenopus
D015220:Calcium Channels; D002412:Cations; D007473:Ion Channels; D005576:Colforsin; D012701:Serotonin; D013004:Somatostatin; D000255:Adenosine Triphosphate; D002217:Carbachol; D017868:Cyclic AMP-Dependent Protein Kinases; D007545:Isoproterenol; D001920:Bradykinin; D002118:Calcium; D004837:Epinephrine