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J Biol Chem, Vol. 274, Issue 43, 30361-30364, October 22, 1999
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From the Mildly oxidized low density lipoprotein
(mox-LDL) is critically involved in the early atherogenic responses of
the endothelium and increases endothelial permeability through an
unknown signal pathway. Here we show that (i) exposure of confluent
human endothelial cells (HUVEC) to mox-LDL but not to native LDL
induces the formation of actin stress fibers and intercellular gaps
within minutes, leading to an increase in endothelial permeability;
(ii) mox-LDL induces a transient decrease in myosin light chain (MLC)
phosphatase that is paralleled by an increase in MLC phosphorylation;
(iii) phosphorylated MLC stimulated by mox-LDL is incorporated into stress fibers; (iv) cytoskeletal rearrangements and MLC phosphorylation are inhibited by C3 transferase from Clostridium botulinum,
a specific Rho inhibitor, and Y-27632, an inhibitor of Rho kinase; and
(v) mox-LDL does not increase intracellular Ca2+
concentration. Our data indicate that mox-LDL induces endothelial cell
contraction through activation of Rho and its effector Rho kinase which
inhibits MLC phosphatase and phosphorylates MLC. We suggest that
inhibition of this novel cell signaling pathway of mox-LDL could be
relevant for the prevention of atherosclerosis.
Institut für Prophylaxe und
Epidemiologie der Kreislaufkrankheiten, Universität
München, Pettenkoferstrasse 9, 80336 München, Germany,
the ** Max-von-Pettenkofer-Institut für Medizinische
Mikrobiologie, Pettenkoferstrasse 9a, 80336 München, Germany,
and the Department of Biochemistry, Cardiovascular Research
Institute, University of Maastricht, P. O. Box 616, 6200 MD Maastricht, The Netherlands
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