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001-es BibID:BIBFORM047427
Első szerző:Adyshev, Djanybek M.
Cím:Ezrin/radixin/moesin proteins differentially regulate endothelial hyperpermeability after thrombin / Djanybek M. Adyshev, Steven M. Dudek, Nurgul Moldobaeva, Kyung-mi Kim, Shwu-Fan Ma, Anita Kasa, Joe G. N. Garcia, Alexander D. Verin
Dátum:2013
ISSN:1040-0605
Megjegyzések:Endothelial cell (EC) barrier disruption induced by inflammatory agonists such as thrombin leads to potentially lethal physiological dysfunction such as alveolar flooding, hypoxemia and pulmonary edema. Thrombin stimulates paracellular gap and F-actin stress fiber formation, triggers actomyosin contraction and alters EC permeability through multiple mechanisms that include protein kinase C (PKC) activation. We previously have shown that the ezrin, radixin, and moesin (ERM) actin-binding proteins differentially participate in S1P-induced EC barrier enhancement. Phosphorylation of a conserved threonine residue in the C terminus of ERM proteins causes conformational changes in ERM to unmask binding sites and is considered a hallmark of ERM activation. In the present study we test the hypothesis that ERM proteins are phosphorylated on this critical threonine residue by thrombin-induced signaling events and explore the role of the ERM family in modulating thrombin-induced cytoskeletal rearrangement and EC barrier function. Thrombin promotes ERM phosphorylation at this threonine residue (Ezrin-567, Radixin-564, Moesin-558) in a PKC-dependent fashion and induces translocation of phosphorylated ERM to the EC periphery. Thrombin-induced ERM threonine phosphorylation is likely synergistically mediated by protease-activated receptors PAR1 and PAR2. Using the siRNA approach, depletion of either moesin alone, or of all three ERM proteins, significantly attenuates thrombin-induced increase in EC barrier permeability (TER), cytoskeletal rearrangements, paracellular gap formation and accumulation of di-phospho-MLC. In contrast, radixin depletion exerts opposing effects on these indices. These data suggest that ERM proteins play important differential roles in the thrombin-induced modulation of EC permeability, with moesin promoting barrier dysfunction and radixin opposing it
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
thrombin
ERM
PKC
phosphorylation
Megjelenés:American Journal of Physiology-Lung Cellular and Molecular Physiology 305 : 3 (2013), p. L240-L255. -
További szerzők:Dudek, Steven Moldobaeva, Nurgul Kim, Kyung-mi Ma, Shwu-Fan Kovács-Kása Anita (1983-) Garcia, Joe G. N. Verin, Alexander
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001-es BibID:BIBFORM046501
035-os BibID:PMID:23583905
Első szerző:Kim, Kyung-mi
Cím:Putative protein partners for the human CPI-17 protein revealed by bacterial two-hybrid screening / Kyung-mi Kim, Djanybek M. Adyshev, Anita Kása, Evgeny A. Zemskov, Irina A. Kolosova, Csilla Csortos, Alexander D. Verin
Dátum:2013
ISSN:0026-2862
Megjegyzések:We have previously demonstrated that PKC-potentiated inhibitory protein of protein phosphatase-1 (CPI-17) is expressed in lung endothelium. CPI-17, a specific inhibitor of myosin light chain phosphatase (MLCP), is involved in the endothelial cytoskeletal and barrier regulation. In this paper, we report the identification of fourteen putative CPI-17 interacting proteins in the lung using BacterioMatch Two-Hybrid System. Five of them: plectin 1 isoform 1, alpha II spectrin, OK/SW-CL.16, gelsolin isoform a, and junction plakoglobin are involved in actin cytoskeleton organization and cell adhesion, suggesting possible significance of these binding partners in CPI-17-mediated cytoskeletal reorganization of endothelial cells. Furthermore, we confirmed the specific interaction between plakoglobin and CPI-17, which is affected by the phosphorylation status of CPI-17 in human lung microvascular endothelial cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Microvascular Research. - 88 (2013), p. 19-24. -
További szerzők:Adyshev, Djanybek M. Kovács-Kása Anita (1983-) Zemskov, Evgeny A. Kolosova, Irina Csortos Csilla (1956-) (biokémikus) Verin, Alexander
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