Polymyxin B, a Protein Kinase C Inhibitor, Abolishes Preconditioning-induced Protection against Contractile Dysfunction in the Isolated Blood Perfused Rat Heart

1996 ◽  
Vol 28 (5) ◽  
pp. 977-987 ◽  
Author(s):  
A Cave
1989 ◽  
Vol 21 (12) ◽  
pp. 1415-1420 ◽  
Author(s):  
Stephen Rattigan ◽  
Aidan G.M. Davison ◽  
Perry J.F. Cleland ◽  
Michael G. Clark

Author(s):  
A. G. M. Davidson ◽  
P. J. F. Cleland ◽  
S. Rattigan ◽  
M. G. Clark

2013 ◽  
Vol 191 (5) ◽  
pp. 2247-2257 ◽  
Author(s):  
Takuya Matsumoto ◽  
Hitoshi Hasegawa ◽  
Sachiko Onishi ◽  
Jun Ishizaki ◽  
Koichiro Suemori ◽  
...  

1990 ◽  
Vol 96 (1) ◽  
pp. 99-106
Author(s):  
H.U. Keller ◽  
V. Niggli ◽  
A. Zimmermann ◽  
R. Portmann

The present study demonstrates new properties of H-7. The protein kinase inhibitor H-7 is a potent activator of several neutrophil functions. Stimulation of initially spherical nonmotile neutrophils elicits vigorous shape changes within a few seconds, increases in cytoskeletal actin, altered F-actin distribution, increased adhesiveness and a relatively small increase in pinocytic activity. H-7 has also chemokinetic activities. Depending on the experimental condition, H-7 may elicit or inhibit neutrophil locomotion. It failed to induce chemotaxis. Thus, the response pattern elicited by H-7 is different from that of other leukocyte activators such as chemotactic peptides, PMA or diacylglycerols. The finding that H-7 can elicit shape changes, actin polymerization and pinocytosis suggests that these events can occur without activation of protein kinase C (PKC). PMA-induced shape changes and stimulation of pinocytosis were not inhibited by H-7.


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