Protein kinase C consensus sites and the regulation of renal Na/Pi-cotransport (NaPi-2) expressed in XENOPUS laevis oocytes

1995 ◽  
Vol 430 (5) ◽  
pp. 819-824 ◽  
Author(s):  
Gillian Hayes ◽  
Andreas E. Busch ◽  
Florian Lang ◽  
J�rg Biber ◽  
Heini Murer
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Xenopus Laevis ◽  
Xenopus Laevis Oocytes ◽  
Kinase C

scholarly journals Evidence for a role of protein kinase C zeta subspecies in maturation of Xenopus laevis oocytes.

1992 ◽  
Vol 12 (9) ◽  
pp. 3776-3783 ◽  
Author(s):  
I Dominguez ◽  
M T Diaz-Meco ◽  
M M Municio ◽  
E Berra ◽  
A García de Herreros ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Growth Factors ◽  
Protein Kinase ◽  
Xenopus Laevis ◽  
Critical Role ◽  
Study Data ◽  
Xenopus Laevis Oocytes ◽  
Kinase C ◽  
Protein Kinase C Zeta

A number of studies have demonstrated the activation of phospholipase C-mediated hydrolysis of phosphatidylcholine (PC-PLC) both by growth factors and by the product of the ras oncogene, p21ras. Evidence has been presented indicating that the stimulation of this phospholipid degradative pathway is sufficient to activate mitogenesis in fibroblasts as well as that it is sufficient and necessary for induction of maturation in Xenopus laevis oocytes. However, the mechanism whereby PC-PLC transduces mitogenic signals triggered by growth factors or oncogenes remains to be elucidated. In this study, data are presented that show the involvement of protein kinase C zeta subspecies in the channelling of the mitogenic signal activated by insulin-p21ras-PC-PLC in Xenopus oocytes as well as the lack of a critical role of protein kinase C isotypes alpha, beta, gamma, delta, and epsilon in these pathways.

scholarly journals Local anaesthetics inhibit signalling of human NMDA receptors recombinantly expressed in Xenopus laevis oocytes: role of protein kinase C

2006 ◽  
Vol 96 (1) ◽  
pp. 77-87 ◽  
Author(s):  
K Hahnenkamp ◽  
M.E. Durieux ◽  
A Hahnenkamp ◽  
S.K. Schauerte ◽  
C.W. Hoenemann ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Xenopus Laevis ◽  
Nmda Receptors ◽  
Local Anaesthetics ◽  
Xenopus Laevis Oocytes ◽  
Kinase C

Evidence for a role of protein kinase C zeta subspecies in maturation of Xenopus laevis oocytes

1992 ◽  
Vol 12 (9) ◽  
pp. 3776-3783
Author(s):  
I Dominguez ◽  
M T Diaz-Meco ◽  
M M Municio ◽  
E Berra ◽  
A García de Herreros ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Growth Factors ◽  
Protein Kinase ◽  
Xenopus Laevis ◽  
Critical Role ◽  
Study Data ◽  
Xenopus Laevis Oocytes ◽  
Kinase C ◽  
Protein Kinase C Zeta

A number of studies have demonstrated the activation of phospholipase C-mediated hydrolysis of phosphatidylcholine (PC-PLC) both by growth factors and by the product of the ras oncogene, p21ras. Evidence has been presented indicating that the stimulation of this phospholipid degradative pathway is sufficient to activate mitogenesis in fibroblasts as well as that it is sufficient and necessary for induction of maturation in Xenopus laevis oocytes. However, the mechanism whereby PC-PLC transduces mitogenic signals triggered by growth factors or oncogenes remains to be elucidated. In this study, data are presented that show the involvement of protein kinase C zeta subspecies in the channelling of the mitogenic signal activated by insulin-p21ras-PC-PLC in Xenopus oocytes as well as the lack of a critical role of protein kinase C isotypes alpha, beta, gamma, delta, and epsilon in these pathways.

Inhibition of protein kinase C zeta subspecies blocks the activation of an NF-kappa B-like activity in Xenopus laevis oocytes

1993 ◽  
Vol 13 (2) ◽  
pp. 1290-1295
Author(s):  
I Dominguez ◽  
L Sanz ◽  
F Arenzana-Seisdedos ◽  
M T Diaz-Meco ◽  
J L Virelizier ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Xenopus Laevis ◽  
Critical Role ◽  
Xenopus Laevis Oocytes ◽  
Nuclear Factor ◽  
Nf Kappa B ◽  
Kinase C ◽  
Ras P21 ◽  
Protein Kinase C Zeta

Nuclear factor kappa B (NF-kappa B) plays a critical role in the regulation of a large variety of cellular genes. However, the mechanism whereby this nuclear factor is activated remains to be determined. In this report, we present evidence that in oocytes from Xenopus laevis, (i) ras p21- and phospholipase C (PLC)-mediated phosphatidylcholine (PC) hydrolysis activates NF-kappa B and (ii) protein kinase C zeta subspecies is involved in the activation of NF-kappa B in response to insulin/ras p21/PC-PLC. Thus, the microinjection of either ras p21 or PC-PLC, or the exposure of oocytes to insulin, promotes a significant translocation to the nucleus of an NF-kappa B-like activity. This effect is not observed when oocytes are incubated with phorbol myristate acetate or progesterone, both of which utilize a ras p21-independent pathway for oocyte activation. These data strongly suggest a critical role of the insulin/ras p21/PC-PLC/protein kinase C zeta pathway in the control of NF-kappa B activation.

Modulation of the Arabidopsis KAT1 channel by an activator of protein kinase C in Xenopus laevis oocytes

FEBS Journal ◽  
2010 ◽  
Vol 277 (10) ◽  
pp. 2318-2328 ◽  
Author(s):  
Aiko Sato ◽  
Franco Gambale ◽  
Ingo Dreyer ◽  
Nobuyuki Uozumi
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Xenopus Laevis ◽  
Xenopus Laevis Oocytes ◽  
Kinase C

scholarly journals Inhibition of protein kinase C zeta subspecies blocks the activation of an NF-kappa B-like activity in Xenopus laevis oocytes.

1993 ◽  
Vol 13 (2) ◽  
pp. 1290-1295 ◽  
Author(s):  
I Dominguez ◽  
L Sanz ◽  
F Arenzana-Seisdedos ◽  
M T Diaz-Meco ◽  
J L Virelizier ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Xenopus Laevis ◽  
Critical Role ◽  
Xenopus Laevis Oocytes ◽  
Nuclear Factor ◽  
Nf Kappa B ◽  
Kinase C ◽  
Ras P21 ◽  
Protein Kinase C Zeta

Nuclear factor kappa B (NF-kappa B) plays a critical role in the regulation of a large variety of cellular genes. However, the mechanism whereby this nuclear factor is activated remains to be determined. In this report, we present evidence that in oocytes from Xenopus laevis, (i) ras p21- and phospholipase C (PLC)-mediated phosphatidylcholine (PC) hydrolysis activates NF-kappa B and (ii) protein kinase C zeta subspecies is involved in the activation of NF-kappa B in response to insulin/ras p21/PC-PLC. Thus, the microinjection of either ras p21 or PC-PLC, or the exposure of oocytes to insulin, promotes a significant translocation to the nucleus of an NF-kappa B-like activity. This effect is not observed when oocytes are incubated with phorbol myristate acetate or progesterone, both of which utilize a ras p21-independent pathway for oocyte activation. These data strongly suggest a critical role of the insulin/ras p21/PC-PLC/protein kinase C zeta pathway in the control of NF-kappa B activation.

scholarly journals Protein kinase C acts downstream of calcium at entry into the first mitotic interphase of Xenopus laevis.

1990 ◽  
Vol 1 (3) ◽  
pp. 315-326 ◽  
Author(s):  
W M Bement ◽  
D G Capco
Keyword(s):  
Cell Cycle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Xenopus Laevis ◽  
Mitotic Cell ◽  
Cortical Granule ◽  
Mitotic Cell Cycle ◽  
Cleavage Furrow ◽  
Kinase C ◽  
Cortical Granule Exocytosis

Transit into interphase of the first mitotic cell cycle in amphibian eggs is a process referred to as activation and is accompanied by an increase in intracellular free calcium [( Ca2+]i), which may be transduced into cytoplasmic events characteristic of interphase by protein kinase C (PKC). To investigate the respective roles of [Ca2+]i and PKC in Xenopus laevis egg activation, the calcium signal was blocked by microinjection of the calcium chelator BAPTA, or the activity of PKC was blocked by PKC inhibitors sphingosine or H7. Eggs were then challenged for activation by treatment with either calcium ionophore A23187 or the PKC activator PMA. BAPTA prevented cortical contraction, cortical granule exocytosis, and cleavage furrow formation in eggs challenged with A23187 but not with PMA. In contrast, sphingosine and H7 inhibited cortical granule exocytosis, cortical contraction, and cleavage furrow formation in eggs challenged with either A23187 or PMA. Measurement of egg [Ca2+]i with calcium-sensitive electrodes demonstrated that PMA treatment does not increase egg [Ca2+]i in BAPTA-injected eggs. Further, PMA does not increase [Ca2+]i in eggs that have not been injected with BAPTA. These results show that PKC acts downstream of the [Ca2+]i increase to induce cytoplasmic events of the first Xenopus mitotic cell cycle.

scholarly journals Protein kinase C activation antagonizes melatonin-induced pigment aggregation in Xenopus laevis melanophores.

1992 ◽  
Vol 119 (6) ◽  
pp. 1515-1521 ◽  
Author(s):  
D Sugden ◽  
S J Rowe
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Xenopus Laevis ◽  
Pigment Granule ◽  
Melatonin Receptors ◽  
Kinase C ◽  
Pigment Granules ◽  
Slow Aggregation ◽  
Pigment Aggregation ◽  
Induced Aggregation

The pineal hormone, melatonin (5-methoxy N-acetyltryptamine) induces a rapid aggregation of melanin-containing pigment granules in isolated melanophores of Xenopus laevis. Treatment of melanophores with activators of protein kinase C (PKC), including phorbol esters, mezerein and a synthetic diacylglycerol, did not affect pigment granule distribution but did prevent and reverse melatonin-induced pigment aggregation. This effect was blocked by an inhibitor of PKC, Ro 31-8220. The inhibitory effect was not a direct effect on melatonin receptors, per se, as the slow aggregation induced by a high concentration of an inhibitor of cyclic AMP-dependent protein kinase (PKA), adenosine 3',5'-cyclic monophosphothioate, Rp-diastereomer (Rp-cAMPS), was also reversed by PKC activation. Presumably activation of PKC, like PKA activation, stimulates the intracellular machinery involved in the centrifugal translocation of pigment granules along microtubules. alpha-Melanocyte stimulating hormone (alpha-MSH), like PKC activators, overcame melatonin-induced aggregation but this response was not blocked by the PKC inhibitor, Ro 31-8220. This data indicates that centrifugal translocation (dispersion) of pigment granules in Xenopus melanophores can be triggered by activation of either PKA, as occurs after alpha-MSH treatment, or PKC. The very slow aggregation in response to inhibition of PKA with high concentrations of Rp-cAMPS, suggests that the rapid aggregation in response to melatonin may involve multiple intracellular signals in addition to the documented Gi-mediated inhibition of adenylate cyclase.

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