PMID- 17476691
OWN - NLM
STAT- MEDLINE
DCOM- 20071026
LR  - 20220227
IS  - 0021-9541 (Print)
IS  - 0021-9541 (Linking)
VI  - 213
IP  - 1
DP  - 2007 Oct
TI  - Roles of Rho/ROCK and MLCK in TNF-alpha-induced changes in endothelial morphology 
      and permeability.
PG  - 221-8
AB  - Tumor necrosis factor-alpha (TNF-alpha) is known to induce changes in endothelial 
      cell morphology and permeability, but the mechanisms have not been extensively 
      characterized. TNF-alpha rapidly induced RhoA activation and myosin light chain 
      phosphorylation, but caused only small changes to cortical F-actin, without 
      significantly increasing paracellular permeability up to 30 min after 
      stimulation. TNF-alpha subsequently caused a progressive increase in permeability 
      and in stress fiber reorganization, cell elongation, and intercellular gap 
      formation over 8-24 h. Consistent with the increased permeability, Occludin and 
      JAM-A were removed from tight junctions and ZO-1 was partially redistributed. 
      Rho/ROCK but not MLCK inhibition prevented the long-term TNF-alpha-induced 
      changes in F-actin and cell morphology, but ROCK inhibition did not affect 
      permeability. These results suggest that the gradual increase in permeability 
      induced by TNF-alpha does not reflect contractile mechanisms mediated by Rho, 
      ROCK, and MLCK, but involves long-term reorganization of tight junction proteins.
CI  - (c) 2007 Wiley-Liss, Inc.
FAU - McKenzie, Jenny A G
AU  - McKenzie JA
AD  - Ludwig Institute for Cancer Research, Royal Free and University College School of 
      Medicine, London, United Kingdom.
FAU - Ridley, Anne J
AU  - Ridley AJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Cell Physiol
JT  - Journal of cellular physiology
JID - 0050222
RN  - 0 (Actins)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (OCLN protein, human)
RN  - 0 (Occludin)
RN  - 0 (Tumor Necrosis Factor-alpha)
RN  - 0 (myosin IXB)
RN  - EC 2.7.11.1 (Protein Serine-Threonine Kinases)
RN  - EC 2.7.11.1 (rho-Associated Kinases)
RN  - EC 2.7.11.18 (Myosin-Light-Chain Kinase)
RN  - EC 3.6.4.1 (Myosins)
RN  - EC 3.6.5.2 (rho GTP-Binding Proteins)
SB  - IM
MH  - Actins/metabolism
MH  - Cell Membrane Permeability/drug effects
MH  - Cell Shape/drug effects
MH  - Cells, Cultured
MH  - Endothelial Cells/cytology/*drug effects/*metabolism
MH  - Humans
MH  - Intracellular Signaling Peptides and Proteins/*metabolism
MH  - Membrane Proteins/metabolism
MH  - Myosin-Light-Chain Kinase/metabolism
MH  - Myosins/metabolism
MH  - Occludin
MH  - Protein Serine-Threonine Kinases/*metabolism
MH  - Tight Junctions/drug effects
MH  - Tumor Necrosis Factor-alpha/*pharmacology
MH  - rho GTP-Binding Proteins/*metabolism
MH  - rho-Associated Kinases
EDAT- 2007/05/04 09:00
MHDA- 2007/10/30 09:00
CRDT- 2007/05/04 09:00
PHST- 2007/05/04 09:00 [pubmed]
PHST- 2007/10/30 09:00 [medline]
PHST- 2007/05/04 09:00 [entrez]
AID - 10.1002/jcp.21114 [doi]
PST - ppublish
SO  - J Cell Physiol. 2007 Oct;213(1):221-8. doi: 10.1002/jcp.21114.