Protein kinase C affects reformation of endothelial junctions in xenopus XTH-2 cells.
Endothelial cells can reversibly be forced to suppress the formation of endothelial junctions (EJ) by cultivation in a low calcium medium. The authors localized vinculin and cadherin as marker proteins of EJ and actin as a cytoskeletal component by fluorescence microscopy, and used this cell model to study the reformation of endothelial junctions under conditions of activation and inhibition of protein kinase C (PKC). Inhibition of PKC by H-7 leads to an acceleration of EJ reformation, while constitutive activation by TPA inhibits the reformation process.
Werner
N S
NS
Innere Klinik und Poliklinik (Tumorforschung), Universitätsklinikum Essen, Hufelandstr. 55, Essen, D-45122, Germany.
Meyer
R
R
Achenbach
F
F
D019307:1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine / Q000494:pharmacology; D000818:Animals; D015820:Cadherins / Q000502:physiology; D002460:Cell Line; D004730:Endothelium, Vascular / Q000166:cytology* / Q000502:physiology*; D004789:Enzyme Activation / Q000502:physiology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D007365:Intercellular Junctions / Q000502:physiology*; D010703:Phorbol Esters / Q000494:pharmacology; D011493:Protein Kinase C / Q000502:physiology*; D015398:Signal Transduction; D016596:Vinculin / Q000502:physiology; D014981:Xenopus
D015820:Cadherins; D004791:Enzyme Inhibitors; D010703:Phorbol Esters; D016596:Vinculin; D019307:1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine; D011493:Protein Kinase C