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Titolo:
Protein phosphatase 2B inhibitor potentiates endothelial PKC activity and barrier dysfunction
Autore:
Lum, H; Podolski, JL; Gurnack, ME; Schulz, IT; Huang, F; Holian, O;
Indirizzi:
Rush Presbyterian St Lukes Med Ctr, Dept Pharmacol, Chicago, IL 60612 USA Rush Presbyterian St Lukes Med Ctr Chicago IL USA 60612 ago, IL 60612 USA Cook Cty Hosp, Div Gastroenterol, Chicago, IL 60612 USA Cook Cty Hosp Chicago IL USA 60612 v Gastroenterol, Chicago, IL 60612 USA
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-LUNG CELLULAR AND MOLECULAR PHYSIOLOGY
fascicolo: 3, volume: 281, anno: 2001,
pagine: L546 - L555
SICI:
1040-0605(200109)281:3<L546:PP2IPE>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
KINASE-C ISOZYMES; DOWN-REGULATION; CYCLOSPORINE-A; B ACTIVATION; BETA-CATENIN; OKADAIC ACID; CELL-CELL; PERMEABILITY; PHOSPHORYLATION; ALPHA;
Keywords:
protein kinase C-alpha; transendothelial resistance; FK506; endothelial permeability;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: Lum, H Rush Presbyterian St Lukes Med Ctr, Dept Pharmacol, 2242 W HarrisonSt,Suite 260, Chicago, IL 60612 USA Rush Presbyterian St Lukes Med Ctr 2242 W Harrison St,Suite 260 Chicago IL USA 60612
Citazione:
H. Lum et al., "Protein phosphatase 2B inhibitor potentiates endothelial PKC activity and barrier dysfunction", AM J P-LUNG, 281(3), 2001, pp. L546-L555

Abstract

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 ofbarrier 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-alpha but not PKC-beta phosphorylation. FK506 but not calyculin A or okadaic acid inhibited recovery from thethrombin-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 phosphorylationof PKC-zeta was reduced during the recovery phase. These results indicatedthat PP2B may play a physiologically important role in returning endothelial barrier dysfunction to normal through the regulation of PKC.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 19:47:34