Staurosporine, a potent protein kinase C inhibitor, fails to inhibit 12-O-tetradecanoylphorbol-13-acetate-caused ornithine decarboxylase induction in isolated mouse epidermal cells

1987 ◽  
Vol 148 (2) ◽  
pp. 740-746 ◽  
Author(s):  
Itsumi Kiyoto ◽  
Satoshi Yamamoto ◽  
Eriko Aizu ◽  
Ryuichi Kato
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Ornithine Decarboxylase ◽  
Epidermal Cells ◽  
Kinase C ◽  
Protein Kinase C Inhibitor

scholarly journals Increased Expression of Ornithine Decarboxylase by Gamma-ray in Mouse Epidermal Cells: Relationship with Protein Kinase C Signaling Pathway.

1998 ◽  
Vol 39 (3) ◽  
pp. 175-184 ◽  
Author(s):  
HYUN-JUNG SONG ◽  
TAI-HWAN KIM ◽  
CHUL-KOO CHO ◽  
SEONG-YUL YOO ◽  
KYUNG-SOOK PARK ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Signaling Pathway ◽  
Ornithine Decarboxylase ◽  
Gamma Ray ◽  
Epidermal Cells ◽  
Kinase C

scholarly journals Suppression of c-fos precursor RNA splicing by the protein kinase C inhibitor H7 [1-(5-isoquinolinesulphonyl)-2-methylpiperazine]

1991 ◽  
Vol 278 (1) ◽  
pp. 305-308 ◽  
Author(s):  
M Harbers ◽  
H Hilz
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Rna Splicing ◽  
Epidermal Cells ◽  
Pkc Inhibitor ◽  
Oncogene Expression ◽  
Kinase C ◽  
Protein Kinase C Inhibitor ◽  
Precursor Rna ◽  
Dose Dependent

In JB6 epidermal cells, induction of fos proto-oncogene expression by phorbol 12-myristate 13-acetate can be inhibited by the protein kinase C (PKC) inhibitor H7 [1-5(isoquinolinesulphonyl)-2-methylpiperazine]. The compound causes also a dose-dependent suppression of fos precursor RNA splicing which, however, appears to react somewhat less sensitively to H7 than does PKC activity. This indicates that H7-induced accumulation of fos precursor RNA is not due to inhibition of PKC. Support for this interpretation comes from the finding that other inhibitors of PKC, such as N-(2-guanidinoethyl)-5-isoquinolinesulphonamide dihydrochloride, sphingosine, staurosporine or N-(6-aminohexyl)-5-chloro-1-naphthalenesulphonamide, do not suppress splicing when applied at PKC-inhibiting concentrations.

scholarly journals Protein Kinase C Inhibitor Generates Stable Human Tolerogenic Dendritic Cells

2013 ◽  
Vol 191 (5) ◽  
pp. 2247-2257 ◽  
Author(s):  
Takuya Matsumoto ◽  
Hitoshi Hasegawa ◽  
Sachiko Onishi ◽  
Jun Ishizaki ◽  
Koichiro Suemori ◽  
...  
Keyword(s):  
Dendritic Cells ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Kinase C ◽  
Tolerogenic Dendritic Cells ◽  
Protein Kinase C Inhibitor

The protein kinase C inhibitor H-7 activates human neutrophils: effect on shape, actin polymerization, fluid pinocytosis and locomotion

1990 ◽  
Vol 96 (1) ◽  
pp. 99-106
Author(s):  
H.U. Keller ◽  
V. Niggli ◽  
A. Zimmermann ◽  
R. Portmann
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Actin Polymerization ◽  
Kinase Inhibitor ◽  
Human Neutrophils ◽  
Kinase C ◽  
Chemotactic Peptides ◽  
Protein Kinase C Inhibitor ◽  
Shape Changes ◽  
Stimulation Of

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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