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Calpains: a physiological regulator of the endothelial barrier?

¹Department of Physiology, University of Munich, Munich; ²Max-Planck Institute for Biochemistry, Martinsried; ³Technical University of Munich, Munich; and ⁴Department of Clinical Chemistry and Clinical Biochemistry, University of Munich, Munich, Germany

Submitted 30 July 2004 ; accepted in final form 14 December 2005

The intracellular protease calpain, abundant in endothelial cells (EC), is assumed to be inactive under physiological conditions but may account for Ca²⁺-linked pathophysiological events. However, nonstimulated EC contained autolyzed, activated calpain. Adding 12–48 µM calpain inhibitor I (CI) or 0.5–1 µM of the novel, membrane-permeable conjugate of calpastatin peptide-penetratin (CPP) caused rapid rounding and retraction of cultured EC (phase contrast, capacitance) and translocation of Syk, Rac, and Rho to the membrane, signifying activation upon inhibition of calpain. Isolated hearts (guinea pig) perfused with 12 µM CI or 0.5 µM CPP developed coronary leak. We conclude that calpain is constitutively active in EC and regulates vascular permeability by governing cell-cell attachment.

cell retraction; calpastatin; endothelium; coronary permeability; reperfusion

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