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1 Department of Pharmacology, Rush-Presbyterian-St. Luke's Medical Center, and 2 Division of Gastroenterology, Cook County Hospital, Chicago, Illinois 60612
Serine/threonine (Ser/Thr) protein
phosphatases (PPs) are implicated in the recovery from endothelial
barrier dysfunction caused by inflammatory mediators. We hypothesized
that Ser/Thr PPs may regulate protein kinase C (PKC), a critical
signaling molecule in barrier dysfunction, in the promotion of barrier
recovery. Western analysis indicated that bovine pulmonary
microvascular endothelial cells (BPMECs) expressed the three major
Ser/Thr PPs, PP1, PP2A, and PP2B. Pretreatment with 100 ng/ml of FK506
(a PP2B inhibitor) but not with the PP1 and PP2A inhibitors calyculin A
or okadaic acid potentiated the thrombin-induced increase in PKC
phosphotransferase activity. FK506 also potentiated thrombin-induced PKC-
but not PKC-
phosphorylation. FK506 but not calyculin A or
okadaic acid inhibited recovery from the thrombin-induced decrease in
transendothelial resistance. Neither FK506 nor okadaic acid altered the
thrombin-induced resistance decrease, whereas calyculin A potentiated
the decrease. Downregulation of PKC with phorbol 12-myristate
13-acetate rescued the FK506-mediated inhibition of recovery, which was
consistent with the finding that the thrombin-induced phosphorylation
of PKC- was reduced during the recovery phase. These results
indicated that PP2B may play a physiologically important role in
returning endothelial barrier dysfunction to normal through the
regulation of PKC.
protein kinase C-; transendothelial resistance; FK506; endothelial permeability
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