Involvement of calcium-dependent cysteine protease in fibronectin-induced chemotactic migration of NIH-L13 fibroblasts.
Fibronectin (FN)-induced chemotactic migration of NIH-L13 fibroblasts was suppressed by the inhibitors of cysteine proteases, leupeptin (IC50 = 3 microM), and the epoxysuccinyl derivatives [E-64c (10 microM), SUT-8801 (45 microM), and SUT-8818 (28 microM)], but hardly by phenylmethanesulfonyl fluoride (> 1 mM) and 1-tosyl-amido-2-phenylmethyl chloromethyl ketone (> 1 mM). E-64d, a membrane-permeant derivative of E-64c, was much more effective (IC50 = 4 microM) than E-64c in preventing the cell migration. Furthermore, the FN-induced cell migration was blocked partially with EGTA and was reversed by addition of Ca2+ ion. These results suggest that intracellular Ca(2+)-dependent cysteine proteases may be involved in the FN-induced chemotactic migration of NIH-L13 fibroblasts.
Fukai
F
F
Department of Patho-Physiology, Faculty of Pharmaceutical Sciences, Science University of Tokyo.
Ohtani
T
T
Ueki
M
M
Katayama
T
T
D016475:3T3 Cells; D000818:Animals; D002118:Calcium / Q000494:pharmacology*; D002154:Calpain / Q000378:metabolism*; D002633:Chemotaxis / Q000187:drug effects*; D004533:Egtazic Acid / Q000494:pharmacology; D005347:Fibroblasts / Q000187:drug effects / Q000201:enzymology / Q000502:physiology; D005353:Fibronectins / Q000494:pharmacology*; D007700:Kinetics; D051379:Mice; D011480:Protease Inhibitors / Q000494:pharmacology*
D005353:Fibronectins; D011480:Protease Inhibitors; D004533:Egtazic Acid; D002154:Calpain; D002118:Calcium