scholarly journals Replacement of Ser657 of Protein Kinase C-alpha by Alanine Leads to Premature Down Regulation After Phorbol-Ester-Induced Translocation to the Membrane

1996 ◽  
Vol 240 (3) ◽  
pp. 747-750 ◽  
Author(s):  
Stephan Gysin ◽  
Roland Imber
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phorbol Ester ◽  
Down Regulation ◽  
Kinase C ◽  
Protein Kinase C Alpha

scholarly journals Phorbol ester-induced myeloid differentiation is mediated by protein kinase C-alpha and -delta and not by protein kinase C-beta II, -epsilon, -zeta, and -eta.

1993 ◽  
Vol 268 (27) ◽  
pp. 20110-20115
Author(s):  
H Mischak ◽  
J.H. Pierce ◽  
J Goodnight ◽  
M.G. Kazanietz ◽  
P.M. Blumberg ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phorbol Ester ◽  
Myeloid Differentiation ◽  
Kinase C ◽  
Protein Kinase C Alpha ◽  
Protein Kinase C Beta

scholarly journals Abnormal protein kinase C down regulation and reduced substrate levels in non-phorbol ester-responsive 3T3-TNR9 cells.

1990 ◽  
Vol 10 (5) ◽  
pp. 2122-2132 ◽  
Author(s):  
H P Biemann ◽  
R L Erikson
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phorbol Ester ◽  
Kinase Activity ◽  
Subcellular Location ◽  
Parental Cell ◽  
Down Regulation ◽  
Kinase C ◽  
Cell Variant ◽  
Swiss 3T3 Cell

The cell line TNR9 (E. Butler-Gralla and H. R. Herschman, J. Cell. Physiol. 107:59-67, 1981) in a Swiss 3T3 cell variant that expresses protein kinase C (PKC) but is mitogenically nonresponsive to the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA). We have found that PKCs purified from variant and parental cells are identical as judged by kinase activity, protease mapping, and column chromatography. We analyzed cellular levels and subcellular location of PKC in TPA-treated 3T3 and TNR9 cells via immunoprecipitation of [35S]methionine-labeled protein and assay of immune-complex PKC kinase activity. TNR9 cells grew to higher densities than parental 3T3 cells. TNR9 cells at maximal density did not down regulate PKC in response to long-term TPA treatment. We compared the 80-kilodalton (kDa) PKC substrate phosphorylation in 3T3 and TNR9 cells by using two-dimensional gels and found that TNR9 cells treated with TPA for 30 min contained only 10 to 15% as much 32Pi associated with the 80-kDa as did parental cells. The TNR9 80-kDa substrate was present at reduced levels compared with the parental-cell 80-kDa substrate as judged by immunoblot and silver staining. Thus, the loss of mitogenic responsiveness to TPA in TNR9 cells is accompanied by resistance to TPA-mediated down regulation of PKC and reduced phosphosubstrate levels.

Possible role of Na+ influx in phorbol ester-induced down-regulation of protein kinase C in HL60 cells

FEBS Letters ◽  
1993 ◽  
Vol 328 (3) ◽  
pp. 280-284 ◽  
Author(s):  
Noriko Takeuchi ◽  
Eikichi Hashimoto ◽  
Toru Nakamura ◽  
Fumito Takeuchi ◽  
Kiyonao Sada ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phorbol Ester ◽  
Down Regulation ◽  
Hl60 Cells ◽  
Kinase C

Induction of protein kinase C down-regulation by the phorbol ester TPA in a calpain/protein kinase C complex

1992 ◽  
Vol 52 (3) ◽  
pp. 399-403 ◽  
Author(s):  
Michel Savart ◽  
Pascale Letard ◽  
Sandrine Bultel ◽  
Andre Ducastaing
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phorbol Ester ◽  
Down Regulation ◽  
Kinase C ◽  
C Complex

Nuclear import of protein kinase C occurs by a mechanism distinct from the mechanism used by proteins with a classical nuclear localization signal

1998 ◽  
Vol 111 (13) ◽  
pp. 1823-1830 ◽  
Author(s):  
D. Schmalz ◽  
F. Hucho ◽  
K. Buchner
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Nuclear Localization ◽  
Phorbol Ester ◽  
Nuclear Import ◽  
Nuclear Localization Signal ◽  
Nuclear Pore ◽  
Kinase C ◽  
Localization Signal ◽  
Protein Kinase C Alpha

Protein kinase C does not have any known nuclear localization signal but, nevertheless, is redistributed from the cytoplasm to the nucleus upon various stimuli. In NIH 3T3 fibroblasts stimulation with phorbol ester leads to a translocation of protein kinase C alpha to the plasma membrane and into the cell nucleus. We compared the mechanism of protein kinase C alpha's transport into the nucleus with the transport mechanism of a protein with a classical nuclear localization signal at several steps. To this end, we co-microinjected fluorescently labeled bovine serum albumin to which a nuclear localization signal peptide was coupled, together with substances interfering with conventional nuclear protein import. Thereafter, the distribution of both the nuclear localization signal-bearing reporter protein and protein kinase C alpha was analyzed in the same cells. We can show that, in contrast to the nuclear localization signal-dependent transport, the phorbol ester-induced transport of protein kinase C alpha is not affected by microinjection of antibodies against the nuclear import factor p97/importin/karyopherin beta or microinjection of non-hydrolyzable GTP-analogs. This suggests that nuclear import of protein kinase C alpha is independent of p97/importin/karyopherin beta and independent of GTP. At the nuclear pore there are differences between the mechanisms too, since nuclear transport of protein kinase C alpha cannot be inhibited by wheat germ agglutinin or an antibody against nuclear pore complex proteins. Together these findings demonstrate that the nuclear import of protein kinase C alpha occurs by a mechanism distinct from the one used by classical nuclear localization signal-bearing proteins at several stages.

Rapid down-regulation of protein kinase C and membrane association in phorbol ester-treated leukemia cells

FEBS Letters ◽  
1985 ◽  
Vol 190 (1) ◽  
pp. 50-54 ◽  
Author(s):  
R.Gitendra Wickremasinghe ◽  
Andrea Piga ◽  
Dario Campana ◽  
John C. Yaxley ◽  
A.Victor Hoffbrand
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phorbol Ester ◽  
Leukemia Cells ◽  
Membrane Association ◽  
Down Regulation ◽  
Kinase C
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