scholarly journals The pretubulysin-induced exposure of collagen is caused by endothelial cell retraction that results in an increased adhesion and decreased transmigration of tumor cells

Oncotarget ◽  
2017 ◽  
Vol 8 (44) ◽  
pp. 77622-77633 ◽  
Author(s):  
Rebecca Schwenk ◽  
Tanja Stehning ◽  
Iris Bischoff ◽  
Angelika Ullrich ◽  
Uli Kazmaier ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Tumor Cells ◽  
Endothelial Cell Retraction ◽  
Cell Retraction

Enhanced Endothelial Cell Retraction Mediated by 12(S)-HETE: A Proposed Mechanism for the Role of Platelets in Tumor Cell Metastasis

1994 ◽  
Vol 210 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Kenneth V. Honn ◽  
Dean G. Tang ◽  
Irma M. Grossi ◽  
Colette Renaud ◽  
Zofia M. Duniec ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Tumor Cell ◽  
Cell Metastasis ◽  
Tumor Cell Metastasis ◽  
Endothelial Cell Retraction ◽  
Cell Retraction

Mechanisms of HER2-Induced Endothelial Cell Retraction

2007 ◽  
Vol 14 (10) ◽  
pp. 2971-2978 ◽  
Author(s):  
W. Bradford Carter ◽  
Guilian Niu ◽  
Michael D. Ward ◽  
Gregory Small ◽  
Julianne E. Hahn ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Endothelial Cell Retraction ◽  
Cell Retraction

Increased endothelial cell retraction and tumor cell invasion by soluble factors derived from pancreatic cancer cells

1997 ◽  
Vol 4 (4) ◽  
pp. 361-368 ◽  
Author(s):  
Shoji Nakamori ◽  
Hirotaka Okamoto ◽  
Toshiyuki Kusama ◽  
Kiyoko Shinkai ◽  
Mutsuko Mukai ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Endothelial Cell ◽  
Tumor Cell ◽  
Cancer Cells ◽  
Cell Invasion ◽  
Tumor Cell Invasion ◽  
Soluble Factors ◽  
Pancreatic Cancer Cells ◽  
Endothelial Cell Retraction ◽  
Cell Retraction

scholarly journals 12(S)-HETE induces lymph endothelial cell retraction in�vitro by upregulation of SOX18

2018 ◽  
Author(s):  
Adryan Fristiohady ◽  
Daniela Milovanovic ◽  
Sigurd Krieger ◽  
Nicole Huttary ◽  
Chi Nguyen ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Endothelial Cell Retraction ◽  
Cell Retraction

Regulation of permeabilized endothelial cell retraction by myosin phosphorylation

1991 ◽  
Vol 261 (1) ◽  
pp. C32-C40 ◽  
Author(s):  
R. B. Wysolmerski ◽  
D. Lagunoff
Keyword(s):  
Endothelial Cell ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Specific Inhibitor ◽  
Light Chains ◽  
Myosin Light Chains ◽  
Inhibitory Peptide ◽  
Endothelial Cell Retraction ◽  
Cell Retraction ◽  
Gamma S

Permeabilized endothelial cell monolayers retracted on exposure to ATP and Ca2+. ADP, inosine triphosphate (ITP), GTP, adenosine 5'-(gamma-thio)triphosphate (ATP-gamma S), and 5'-adenylylimidodiphosphate failed to support retraction. However, ATP gamma S, a substrate for myosin light-chain kinase (MLCK) but not myosin adenosinetriphosphatase (ATPase), combined with ITP, a substrate for myosin ATPase but not MLCK, supported retraction. Two MLCK pseudosubstrate peptides, M5 and SM-1, inhibited endothelial cell retraction equally and more effectively than myosin kinase-inhibitory peptide with a sequence based on the phosphorylated site of myosin light chain. M5 was shown to inhibit thiophosphorylation of endothelial cell myosin light chains. Endothelial cells incubated with exogenous unregulated kinase in the presence of ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetra-acetic acid retracted on addition of ATP. This retraction was accompanied by thiophosphorylation of the 19 kDa myosin light chains in the presence of ATP gamma 35S. The N-ethylmaleimide-modified subfragment 1 of myosin heads, a specific inhibitor of actin-myosin interaction, prevented retraction. These data add support to the proposal of a central role for MLCK activation of myosin in endothelial retraction.

Role of myosin light-chain phosphorylation in endothelial cell retraction

1993 ◽  
Vol 265 (6) ◽  
pp. L606-L612 ◽  
Author(s):  
R. Sheldon ◽  
A. Moy ◽  
K. Lindsley ◽  
S. Shasby ◽  
D. M. Shasby
Keyword(s):  
Endothelial Cell ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Kinase Inhibitor ◽  
Umbilical Vein ◽  
Extracellular Calcium ◽  
Relative Specificity ◽  
Endothelial Cell Retraction ◽  
Mlc Phosphorylation ◽  
Cell Retraction

Endothelial cells retract centripetally when they are exposed to histamine and when extracellular calcium is chelated. This centripetal retraction implies that a centripetal tension must be expressed in the cells. We asked whether phosphorylation of the light chain of myosin (MLC) was important for the retraction to occur, and, by inference, expression of the tension. In human umbilical vein endothelial (HUVE) cells and in porcine pulmonary artery endothelial (PPAE) cells tryptic peptide maps indicated that MLC was phosphorylated by myosin light-chain kinase (MLCK). Activity of MLCK is inhibited by ML-9, a kinase inhibitor with relative specificity for MLCK, and when MLCK is phosphorylated by the adenosine 3',5'-cyclic monophosphate (cAMP)-dependent kinase. Pretreatment of HUVE cells or PPAE cells with ML-9 or forskolin-aminophylline (to increase cell cAMP) reduced basal MLC phosphorylation and prevented an expected increase in MLC phosphorylation following exposure of HUVE cells to histamine. Pretreatment of HUVE cells with ML-9 or forskolin-aminophylline prevented HUVE cell retraction (measured as an increase in permeability of a monolayer of HUVE cells) in response to histamine. Pretreatment of PPAE cells with ML-9 or forskolin-aminophylline prevented PPAE cell retraction in response to chelation of extracellular calcium. These data support the hypothesis that phosphorylation of MLC is an important component of endothelial cell retraction.

scholarly journals HER2neu over‐expression induces endothelial cell retraction

2001 ◽  
Vol 91 (3) ◽  
pp. 295-299 ◽  
Author(s):  
W. Bradford Carter ◽  
James B. Hoying ◽  
Carl Boswell ◽  
Stuart K. Williams
Keyword(s):  
Endothelial Cell ◽  
Over Expression ◽  
Endothelial Cell Retraction ◽  
Cell Retraction
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