The connection between the cardiac glycoside‐induced senescent cell morphology and Rho/Rho kinase pathway

Cytoskeleton ◽  
2018 ◽  
Vol 75 (11) ◽  
pp. 461-471 ◽  
Author(s):  
Yaprak Dilber Şimay ◽  
Aysun Özdemir ◽  
Burçin İbişoğlu ◽  
Mustafa Ark
Keyword(s):  
Cell Morphology ◽  
Cardiac Glycoside ◽  
Rho Kinase ◽  
Senescent Cell ◽  
Kinase Pathway

Cardiac glycoside-induced cell death and Rho/Rho kinase pathway: Implication of different regulation in cancer cell lines

Steroids ◽  
2016 ◽  
Vol 109 ◽  
pp. 29-43 ◽  
Author(s):  
Aysun Özdemir ◽  
Yaprak Dilber Şimay ◽  
Burçin İbişoğlu ◽  
Biljana Yaren ◽  
Döne Bülbül ◽  
...  
Keyword(s):  
Cell Death ◽  
Cell Lines ◽  
Cancer Cell ◽  
Cardiac Glycoside ◽  
Rho Kinase ◽  
Cancer Cell Lines ◽  
Kinase Pathway

893 The Rho-kinase pathway is involved in fibrotic bladder hypertrophy and ureter dysfunction in a rat model of partial urethral obstruction

2014 ◽  
Vol 13 (1) ◽  
pp. e893
Author(s):  
R. Buono ◽  
F. Benigni ◽  
L. Villa ◽  
P. Hedlund
Keyword(s):  
Rat Model ◽  
Rho Kinase ◽  
Urethral Obstruction ◽  
Kinase Pathway

Rho A and the Rho kinase pathway regulate fibroblast contraction: Enhanced contraction in constitutively active Rho A fibroblast cells

2010 ◽  
Vol 399 (2) ◽  
pp. 292-299 ◽  
Author(s):  
Koji Nobe ◽  
Hiromi Nobe ◽  
Hiroko Yoshida ◽  
Michael S. Kolodney ◽  
Richard J. Paul ◽  
...  
Keyword(s):  
Rho Kinase ◽  
Fibroblast Cells ◽  
Rho A ◽  
Kinase Pathway ◽  
Constitutively Active

scholarly journals The RhoA/Rho kinase pathway in the myocardium

2007 ◽  
Vol 75 (1) ◽  
pp. 3-4 ◽  
Author(s):  
S PETERS ◽  
M MICHEL
Keyword(s):  
Rho Kinase ◽  
Kinase Pathway

scholarly journals Optimization of Corneal Epithelial Progenitor Cell Growth onBombyx moriSilk Fibroin Membranes

2016 ◽  
Vol 2016 ◽  
pp. 1-11 ◽  
Author(s):  
Thomas A. Hogerheyde ◽  
Shuko Suzuki ◽  
Jennifer Walshe ◽  
Laura J. Bray ◽  
Sally A. Stephenson ◽  
...  
Keyword(s):  
Silk Fibroin ◽  
Cell Morphology ◽  
Kinase Inhibitor ◽  
Keratinocyte Growth Factor ◽  
Rho Kinase ◽  
Corneal Epithelial Cell ◽  
Differentiation Markers ◽  
Corneal Epithelial ◽  
Collagen Iii

Scaffolds prepared from silk fibroin derived from cocoons of the domesticated silkworm mothBombyx morihave demonstrated potential to support the attachment and growth of human limbal epithelial (HLE) cellsin vitro. In this study, we attempted to further optimize protocols to promote the expansion of HLE cells onB. morisilk fibroin- (BMSF-) based scaffolds. BMSF films were initially coated with different extracellular matrix proteins and then analysed for their impact on corneal epithelial cell adhesion, cell morphology, and culture confluency. Results showed that collagen I, collagen III, and collagen IV consistently improved HCE-T cell adherence, promoted an elongated cell morphology, and increased culture confluency. By contrast, ECM coating had no significant effect on the performance of primary HLE cells cultured on BMSF films. In the second part of this study, primary HLE cells were grown on BMSF films in the presence of medium (SHEM) supplemented with keratinocyte growth factor (KGF) and the Rho kinase inhibitor, Y-27632. The results demonstrated that SHEM medium supplemented with KGF and Y-27632 dramatically increased expression of corneal differentiation markers, keratin 3 and keratin 12, whereas expression of the progenitor marker, p63, did not appear to be significantly influenced by the choice of culture medium.

Three dimensional real-time analysis of Rho/Rho kinase pathway in cultured endothelial cells by low-coherent quantitative phase microscope

2016 ◽  
Vol 84 (1) ◽  
pp. e27
Author(s):  
Masahiro Aoshima ◽  
Toyohiko Yamauchi ◽  
Yoshiki Tokura ◽  
Satoshi Hirakawa
Keyword(s):  
Endothelial Cells ◽  
Real Time ◽  
Three Dimensional ◽  
Rho Kinase ◽  
Time Analysis ◽  
Quantitative Phase ◽  
Real Time Analysis ◽  
Cultured Endothelial Cells ◽  
Kinase Pathway

RhoA-Rho kinase mediates synergistic ET-1 and phenylephrine contraction of rat corpus cavernosum

2003 ◽  
Vol 285 (5) ◽  
pp. R1145-R1152 ◽  
Author(s):  
Christopher J. Wingard ◽  
Shahid Husain ◽  
Jan Williams ◽  
Sharita James
Keyword(s):  
Kinase Inhibitor ◽  
Corpus Cavernosum ◽  
Rho Kinase ◽  
Stress Generation ◽  
Combined Stress ◽  
Fourfold Increase ◽  
Rho Kinase Inhibitor ◽  
Tissue Homogenates ◽  
Dose Dependent ◽  
Kinase Pathway

Maintenance of the detumescent state of the penis is believed to involve the actions of several vasoconstrictors. However, our mechanistic understanding of any synergistic vasoconstrictor influences is extremely limited. We tested the hypothesis that a vasoconstrictor combination of endothelin (ET-1) and phenylephrine (PE) augments the constrictor responses in rat corporal cavernosal tissues by a mechanism involving the RhoA-Rho kinase pathway. Independently, ET-1 (1 nM-30 μM) and PE (100 nM-100 μM) both caused dose-dependent contractions of isolated rat cavernosal tissues. In combination, ET-1 (30 nM) augmented the contractile effect of PE and shifted the calculated EC50 for PE (90 ± 12 to 45 ± 5 μM). The active stress generated by cavernosal strips during the ET-1 + PE combined stimulation (4.9 ± 0.2 mN/mm2) was greater than the combined stress generated with ET-1 (0.4 ± 0.1 mN/mm2) or PE (3.3 ± 0.2 mN/mm2) stimulations alone. Blockade of ETA receptors (30 nM; A-127722) reversed the augmented stress generation and the Rho-kinase inhibitor Y-27632 differentially and dose-dependently relaxed the tissue. The combined constrictor effect was associated with a fourfold increase of RhoA in the membrane faction of the tissue homogenates. We conclude that the ET-1 + PE combination potentiate vasoconstriction through mutual activation of the RhoA-Rho kinase pathway. The interactions of these agonists likely play important roles in the maintenance of the flaccid state and contribute to some forms of erectile dysfunction.

scholarly journals Activation of G protein-coupled bile acid receptor, TGR5, induces smooth muscle relaxation via both Epac- and PKA-mediated inhibition of RhoA/Rho kinase pathway

2013 ◽  
Vol 304 (5) ◽  
pp. G527-G535 ◽  
Author(s):  
Senthilkumar Rajagopal ◽  
Divya P. Kumar ◽  
Sunila Mahavadi ◽  
Sayak Bhattacharya ◽  
Ruizhe Zhou ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Kinase Activity ◽  
Muscle Relaxation ◽  
Rho Kinase ◽  
Muscle Cells ◽  
Receptor Activation ◽  
Gastric Smooth Muscle ◽  
Selective Ligand ◽  
Gastric Muscle ◽  
Kinase Pathway

The present study characterized the TGR5 expression and the signaling pathways coupled to this receptor that mediates the relaxation of gastric smooth muscle. TGR5 was detected in gastric muscle cells by RT-PCR and Western blotting. Treatment of cells with the TGR5-selective ligand oleanolic acid (OA) activated Gαs, but not Gαq, Gαi1, Gαi2, or Gαi3, and increased cAMP levels. OA did not elicit contraction, but caused relaxation of carbachol-induced contraction of gastric muscle cells from wild-type mice, but not tgr5−/− mice. OA, but not a selective exchange protein activated by cAMP (Epac) ligand (8-pCPT-2′-O-Me-cAMP), caused phosphorylation of RhoA and the phosphorylation was blocked by the PKA inhibitor, myristoylated PKI, and by the expression of phosphorylation-deficient mutant RhoA (S188A). Both OA and Epac ligand stimulated Ras-related protein 1 (Rap1) and inhibited carbachol (CCh)-induced Rho kinase activity. Expression of RhoA (S188A) or PKI partly reversed the inhibition of Rho kinase activity by OA but had no effect on inhibition by Epac ligand. However, suppression of Rap1 with siRNA blocked the inhibition of Rho kinase by Epac ligand, and partly reversed the inhibition by OA; the residual inhibition was blocked by PKI. Muscle relaxation in response to OA, but not Epac ligand, was partly reversed by PKI. We conclude that activation of TGR5 causes relaxation of gastric smooth muscle and the relaxation is mediated through inhibition of RhoA/Rho kinase pathway via both cAMP/Epac-dependent stimulation of Rap1 and cAMP/PKA-dependent phosphorylation of RhoA at Ser188. TGR5 receptor activation on smooth muscle reveals a novel mechanism for the regulation of gut motility by bile acids.

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