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Titolo:
Role of cAMP-dependent protein kinase A activity in endothelial cell cytoskeleton rearrangement
Autore:
Liu, F; Verin, AD; Borbiev, T; Garcia, JGN;
Indirizzi:
Johns Hopkins Univ, Sch Med, Johns Hopkins Asthma & Allergy Ctr, Dept Med,Div Pulm & Crit Care Med, Baltimore, MD 21224 USA Johns Hopkins Univ Baltimore MD USA 21224 re Med, Baltimore, MD 21224 USA
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-LUNG CELLULAR AND MOLECULAR PHYSIOLOGY
fascicolo: 6, volume: 280, anno: 2001,
pagine: L1309 - L1317
SICI:
1040-0605(200106)280:6<L1309:ROCPKA>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
SMOOTH-MUSCLE; BARRIER DYSFUNCTION; CYCLIC-AMP; ADENYLYL CYCLASES; GAP FORMATION; MAP KINASES; CALDESMON; PHOSPHORYLATION; INHIBITION; PERMEABILITY;
Keywords:
Raf-1; mitogen-activated protein kinase; caldesmon;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Garcia, JGN Johns Hopkins Univ, Sch Med, Johns Hopkins Asthma & Allergy Ctr, Dept Med,Div Pulm & Crit Care Med, 5501 Hopkins Bayview Circle,4B-77, Baltimore, MD 21224 USA Johns Hopkins Univ 5501 Hopkins Bayview Circle,4B-77 Baltimore MD USA 21224
Citazione:
F. Liu et al., "Role of cAMP-dependent protein kinase A activity in endothelial cell cytoskeleton rearrangement", AM J P-LUNG, 280(6), 2001, pp. L1309-L1317

Abstract

To examine signaling mechanisms relevant to cAMP/protein kinase A (PKA)-dependent endothelial cell barrier regulation, we investigated the impact of the cAMP/PKA inhibitors Rp diastereomer of adenosine 3', 5'-cyclic monophosphorothioate (Rp-cAMPS) and PKA inhibitor (PKI) on bovine pulmonary artery and bovine lung microvascular endothelial cell cytoskeleton reorganization. Rp-cAMPS as well as PKI significantly increased the formation of actin stress fibers and intercellular gaps but did not alter myosin light chain (MLC) phosphorylation, suggesting that the Rp-cAMPS-induced contractile phenotype evolves in an MLC-independent fashion. We next examined the role of extracellular signal-regulated kinases (ERKs) in Rp-cAMPS- and PKI-induced actin rearrangement. The activities of both ERK1/2 and its upstream activator Raf-1 were transiently enhanced by Rp-cAMPS and linked to the phosphorylation of the well-known ERK cytoskeletal target caldesmon. Inhibition of the Raf-1 target ERK kinase (MEK) either attenuated or abolished Rp-cAMPS- and PKI-induced ERK activation, caldesmon phosphorylation, and stress fiber formation. In summary, our data elucidate the involvement of the p42/44 ERK pathway in cytoskeletal rearrangement evoked by reductions in PKA activity and suggest the involvement of significant cross talk between cAMP- and ERK-dependent signaling pathways in endothelial cell cytoskeletal organization andbarrier regulation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 16:33:29