Human endothelial cell damage by neutrophil-derived cathepsin G. Role of cytoskeleton rearrangement and matrix-bound plasminogen activator inhibitor-1.

@article{Iacoviello1995HumanEC,
  title={Human endothelial cell damage by neutrophil-derived cathepsin G. Role of cytoskeleton rearrangement and matrix-bound plasminogen activator inhibitor-1.},
  author={Licia Iacoviello and V. Kolpakov and Lorena Salvatore and Concetta Amore and Giuseppe Pintucci and Giovanni de Gaetano and Maria Benedetta Donati},
  journal={Arteriosclerosis, thrombosis, and vascular biology},
  year={1995},
  volume={15 11},
  pages={2037-46}
}
Cathepsin G, a major protease released by activated neutrophils, induces functional and morphological damage to human endothelial cells. We studied the mechanisms involved and ways to reverse this damage. Cathepsin G induced a concentration- and time-dependent injury to human umbilical vein endothelial cell (HUVEC) morphology simultaneous with cytoskeleton rearrangement. Preincubation of the endothelial monolayer with phallacidin completely prevented damage to cell morphology by cathepsin g… CONTINUE READING

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