Histamine and thrombin modulate endothelial focal adhesion through centripetal and centrifugal forces

J Clin Invest. 1996 Feb 15;97(4):1020-7. doi: 10.1172/JCI118493.


We examined the contribution of actin-myosin contraction to the modulation of human umbilical vein endothelial cell focal adhesion caused by histamine and thrombin. Focal adhesion was measured as the electrical resistance across a cultured monolayer grown on a microelectrode. Actin-myosin contraction was measured as isometric tension of cultured monolayers grown on a collagen gel. Histamine immediately decreased electrical resistance but returned to basal levels within 3-5 min. Histamine did not increase isometric tension. Thrombin also immediately decreased electrical resistance, but, however, resistance did not return to basal levels for 40-60 min. Thrombin also increased isometric tension, ML-7, an inhibitor of myosin light chain kinase, prevented increases in myosin light chain phosphorylation and increases in tension development in cells exposed to thrombin. ML-7 did not prevent a decline in electrical resistance in cells exposed to thrombin. Instead, ML-7 restored the electrical resistance to basal levels in a shorter period of time (20 min) than cells exposed to thrombin alone. Also, histamine subsequently increased electrical resistance to above basal levels, and thrombin initiated an increase in resistance during the time of peak tension development. Hence, histamine and thrombin modulate endothelial cell focal adhesion through centripetal and centrifugal forces.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Biophysical Phenomena
  • Biophysics
  • Cell Adhesion
  • Cells, Cultured
  • Endothelium, Vascular / cytology*
  • Histamine / physiology*
  • Humans
  • Myosin Light Chains / metabolism
  • Myosin-Light-Chain Kinase / metabolism
  • Thrombin / physiology*


  • Myosin Light Chains
  • Histamine
  • Myosin-Light-Chain Kinase
  • Thrombin