Wyniki wyszukiwania

1

In vitro phosphorylation of alfa-preprotachykinin by protein kinase C

100%

Hrabec E., Hrabec Z., Lachowicz L., Greger J., Plucienniczak G., Plucienniczak A.

Acta Biochimica Polonica

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1994

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tom 41

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nr 2

2

Diacylglycerol signalling: targeting protein kinase C isozymes and 'non-kinase' diacylglycerol effectors

100%

Kazanietz M. G.

Cellular and Molecular Biology Letters

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2005

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tom 10

|

nr Suppl.2

3

The potential therapeutic value of protein kinase C

88%

Parker P. J.

Cellular and Molecular Biology Letters

|

1998

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tom 03

|

nr 3

4

Promoting phorbol-ester-TPA enhances migration of C3H 10T1-2 cells. The role of protein kinase C and its relation to carcinogenesis

88%

Janik P., Szaniawska B., Kowalczyk D., Maternicka K.

Folia Biologica

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1995

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tom 43

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nr 3-4

5

Exogenous sphingosine 1-phosphate and sphingosylphosphorylcholine do not stimulate phospholipase D in C6 glioma cells

88%

Dygas A., Sidorko M., Bobeszko M., Baranska J.

Acta Biochimica Polonica

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1999

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tom 46

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nr 1

In the present study we investigate the effect of exogenous sphingosine, sphingosine 1-phosphate and sphingosylphosphorylcholine on phospholipase D (PLD) activity in glioma C6 cells. The cells were prelabeled with [1-14C]palmitic acid and PLD-mediated synthesis of [14C]phosphatidylethanol was measured. Sphingosine 1-phosphate and sphingosylphosphorylcholine did not stimulate [14C]phosphatidyl-ethanol formation either at low (0.1-10 μM) or high (25-100 μM) concentrations. On the other hand, sphingosine at concentrations of 100-250 μM strongly stimulated PLD activity as compared to the effect of phorbol ester, 12-O-tetradecanoylphorbol 13-acetate (TPA), known as a PLD activator. The effect of TPA on PLD is linked to the activation of protein kinase C. The present study also shows that sphingosine additively enhances TPA-mediated PLD activity. This is in contrast to the postulated role of sphingosine as a protein kinase C inhibitor. These results demonstrate that in glioma C6 cells sphingosine not only affects PLD independently of its effect on protein kinase C, but also is unable to block TPA-mediated PLD activity.

6

Mechanism of inhibition of the protein kinase C by nonstructure protein 3 of hepatitis C virus

88%

Hartjen P., Reinholz M., Baier A., Borowski P.

Cellular and Molecular Biology Letters

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2005

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tom 10

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nr Suppl.2

7

Poly(ADP-ribose) polymerase-1 is a novel nuclear target for cholinergic receptor signaling in the hippocampus

75%

Strosznajder R. P., Jesko H., Adamczyk A.

Journal of Physiology and Pharmacology. Supplement

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2005

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tom 56

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nr 4

209-213

Poly(ADP-ribose) polymerase-1 (PARP-1) is a nuclear enzyme involved in DNA repair and transcription regulation. The aim of this study was to investigate the role of PARP-1 in muscarinic cholinergic receptor signaling. Our data indicate that activation of muscarinic cholinergic receptors by carbachol (1mM) in the presence of GTPS evoked a significant enhancement of PARP activity in the adult rat hippocampus. Moreover, TMB-8 (10µM), an antagonist of inositol 1, 4, 5 trisphosphate (IP3) receptor prevented the activation of PARP-1, which indicates that IP3 /Ca2+ signaling is involved in this pathway. The diacylglycerol (DAG)-regulated protein kinase C (PKC) inhibitor (GF109203X) (1µM) only slightly enhanced PARP activity in hippocampal nuclear fractions, which suggests that DAG/ PKC is not involved in PARP activation.

8

12-O-tetradecanoylphorbol-1,3-acetate induces the negative regulation of protein kinase B by protein kinase Calpha during gastric cancer cell apoptosis

75%

Zhang B., Xia C.

Cellular and Molecular Biology Letters

|

2010

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tom 15

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nr 3

377-394

The PKB signaling pathway is essential for cell survival and the inhibition of apoptosis, but its functional mechanisms have not been fully explored. Previously, we reported that TPA effectively inhibited PKB activity and caused PKB degradation, which was correlated with the repression of PKB phosphorylation at Ser473. In this study, we focus on how PKB is regulated by TPA in gastric cancer cells. One of the TPA targets, PKCα, was found to mediate the inhibition of PKB phosphorylation and degredation caused by TPA. Furthermore, TPA induced the import of PKCα into the nucleus, where PKCα exerted an inhibitory effect on PKB expression and phosphorylation. As a result, cancer cell proliferation was arrested. Our study characterizes a novel function of PKCα in mediating the negative regulation of PKB by TPA, and suggests a potential application in the clinical treatment of gastric cancer.

9

Epac1 is involved in cell cycle progression in lung cancer through PKC and Cx43 regulation

75%

Sun Q., Wang D., Ai G., Tian L., Zhao L., Chen R., Wang K., Guo D., Yao Y., Liu W., Kong X., Chen X., Zhang Y.

Folia Histochemica et Cytobiologica

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2018

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tom 56

|

nr 1

10

Latest aspects of aldosterone actions on the heart muscle

75%

Kritis A. A., Gouta C. P., Liaretidou E. I., Kallaras K. I.

Journal of Physiology and Pharmacology

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2016

|

tom 67

|

nr 1

11

Modulation of CD40L antigen expression in Jurkat cells: involvement of protein kinase C activity

75%

Lisowska K., Bryl E., Soroczynska M., Witkowski J. M.

Folia Histochemica et Cytobiologica

|

2003

|

tom 41

|

nr 4

12

The inhibition of protein kinase C by hepatitis C virus non-structural protein 3 depends on its conformational status

75%

Borowski P., Hartjen P.

Cellular and Molecular Biology Letters

|

2003

|

tom 08

|

nr 2A

13

Decrease of PKCalpha translocation to the erythrocyte membrane in patients with chronic renal failure [CRF]

75%

Kaczmarek J., Komorowska G., Rybczynska M.

Cellular and Molecular Biology Letters

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1998

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tom 03

|

nr 2

14

Pituitary adenylate cyclase-activating polypeptide [PACAP] stimulates phosphoinositide metabolism and translocation of protein kinase C in chick cerebral cortex

75%

Nowak J. Z., Dejda A., Pigulowska A., Kuba K., Zawilska J. B.

Acta Neurobiologiae Experimentalis

|

2001

|

tom 61

|

nr 4

15

The transition from a pharmacophore-guided approach to a receptor-guided approach in the design of potent protein kinase C ligands

75%

Marquez V. E., Nacro K., Benzaria S., Lee J., Milne G. W., Bienfait B., Wang S., Lewin N., Blumberg P. M.

Cellular and Molecular Biology Letters

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1998

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tom 03

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nr 3

16

Isozymes delta of phosphoinositide-specific phospholipase C

75%

Pawelczyk T.

Acta Biochimica Polonica

|

1999

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tom 46

|

nr 1

Phospholipase C (PLC, EC 3.1.4.11) is the major starting point in the phosphatidylinositol pathway, which generates intracellular signals that regulate protein kinase C and intracellular calcium concentration. To date, three major types of phosphoinositide-specific PLC species named β, γ and δ, have been characterized. This article reviews recent studies on isozymes delta of PLC. Four such isozymes have been cloned and termed δ1-4. Their structural organization, regulation of activity and the interaction with membrane lipid are considered. The intracellular localization of delta isozymes and distribution in various tissues are presented. Attention is given to the pathological conditions in which an abnormal protein level of PLC d or its activity have been observed.

17

The ultraviolet studies on protein-lipid interaction of a protein kinase C-gamma phorbol-binding domain

75%

Kowara R., Gryckiewicz E., Matecki A., Pawelczyk T.

Acta Biochimica Polonica

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1999

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tom 46

|

nr 2

Family of protein kinase C (PKC) isozymes play a key role in transducing a vast number of signals into the cells. The members of classical PKC family are activated by binding of various lipid ligands to one of the several cysteine-rich domains of the enzyme. Second cysteine-rich (Cys2) domain of PKC-γ was expressed in Escherichia coli as a fusion protein with glutathione-S-transferase (GST) using the cDNA sequence from rat brain. The Cys2 protein after cleavage from GST was purified to homogeneity using glutathione-agarose and Mono-S cation exchanger column. In order to investigate the interaction of lipids and calcium with Cys2 protein we used UV spectroscopy. The UV spectrum of Cys2 protein exhibited a maximum at 205 nm. Exposition of Cys2 protein to phosphatidylserine (PS) vesicles resulted in significant decrease in the absorbance in the 210 nm region. Changes in UV spectrum of Cys2 protein induced by phorbol 12,13-dibutyrate (PDB) were smaller than those induced by PS, and addition of PDB with PS had no effect on the PS induced changes in UV spectrum of Cys2. Neither phosphatidylcholine (PC) nor phosphatidylethanolamine (PE) affected UV spectrum of Cys2 but in the presence of phosphatidylinositol 4,5-bisphosphate (PIP2) or phosphatidylinositol 4-phosphate (PIP) vesicles some changes were observed. Calcium ions alone or in the presence of PS had no effect on the UV spectrum of Cys2 protein. These data indicate that PS comparing to PDB, interacts with a larger area of Cys2 protein, and that the binding sites for these two molecules are at least overlapping. The site of PIP and PIP2 interaction with PKC-γ is distinct from that of phorbol ester binding site.

18

Contribution of protein kinase A and protein kinase C signalling pathways to the regulation of HSD11B2 expression and proliferation of MCF-7 cells

75%

Rubis B., Grodecka-Gazdecka S., Lecybyl R., Ociepa M., Krozowski Z., Trzeciak W. H.

Acta Biochimica Polonica

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2004

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tom 51

|

nr 4

Contribution of the protein kinase A (PKA) and protein kinase C (PKC) signalling pathways to the regulation of 11y3-hydroxysteroid dehydrogenase type II (HSD11B2) gene expression was investigated in human breast cancer cell line MCF-7. Treatment of the cells with an adenylyl cyclase activator, forskolin, known to stimulate the PKA pathway, resulted in an increase in HSD11B2 mRNA content. Semi-quantitative RT-PCR revealed attenuation of the effect of forskolin by phorbol ester, tetra- decanoyl phorbol acetate (TPA), an activator of the PKC pathway. It was also demonstrated that specific inhibitors significantly reduced the effect of activators of the two pathways. Stimulation of the PKA pathway did not affect, whereas stimulation of the PKC pathway significantly reduced MCF-7 cell proliferation in a time-dependent manner. A cell growth inhibitor, dexamethasone, at high concentrations, caused a 40% decrease in proliferation of MCF-7 cells and this effect was abolished under conditions of increased HSD11B2 expression. It was concluded that in MCF-7 cells, stimulation of the PKA signal transduction pathway results in the induction of HSD11B2 expression and that this effect is markedly reduced by activation of the PKC pathway. Activation of the PKC pathway also resulted in inhibition of cell proliferation, while activation of the PKA pathway abolished the antiproliferative effect of dexamethasone. These effects might be due to oxidation of dexamethasone by the PKA-inducible HSD11B2.

19

CD3 receptor modulation in Jurkat leukemic cell line

75%

Jozwik A., Soroczynska M., Witkowski J. M., Bryl E.

Folia Histochemica et Cytobiologica

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2004

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tom 42

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nr 1

20

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Induction of ornithine decarboxylase in normal and protein kinase C - depleted human colon carcinoma cells

75%

Ostrowski J., Szczepiorkowski Z., Trzeciak L., Rochowska M., Skurzak H., Butruk E.

Journal of Physiology and Pharmacology

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1992

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tom 43

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nr 4

To examine the role of protein kinase С (PKC) in induction of human colon adenocarcinoma cell line, DETA/W, by polypeptide growth- promoting factors, ornithine decarboxylase activity (ODC) and DNA synthesis were determined in cells depleted of PKC. PKC depletion was achieved by prolonged cultivation (more than 30 passages) with 10⁻⁶ M phorbol 12-myristate 13-acelate. Lack of PKC in studied cells was proved by measurements of PKC activity and immunoreactivity. Although ODC activities and DNA syntheses in PKC-depleted cells were decreased by about 40-50% compared to normal DETA/W cells, the percentage increase of these mitogen-responsive reactions was quantitatively similar in both cell sublines. These results raise the possibility that not all of the biological responses to growth factors are connected with the activation of calcium-dependent PKC.

Ograniczanie wyników

In vitro phosphorylation of alfa-preprotachykinin by protein kinase C

Diacylglycerol signalling: targeting protein kinase C isozymes and 'non-kinase' diacylglycerol effectors

The potential therapeutic value of protein kinase C

Promoting phorbol-ester-TPA enhances migration of C3H 10T1-2 cells. The role of protein kinase C and its relation to carcinogenesis

Exogenous sphingosine 1-phosphate and sphingosylphosphorylcholine do not stimulate phospholipase D in C6 glioma cells

Mechanism of inhibition of the protein kinase C by nonstructure protein 3 of hepatitis C virus

Poly(ADP-ribose) polymerase-1 is a novel nuclear target for cholinergic receptor signaling in the hippocampus

12-O-tetradecanoylphorbol-1,3-acetate induces the negative regulation of protein kinase B by protein kinase Calpha during gastric cancer cell apoptosis

Epac1 is involved in cell cycle progression in lung cancer through PKC and Cx43 regulation

Latest aspects of aldosterone actions on the heart muscle

Modulation of CD40L antigen expression in Jurkat cells: involvement of protein kinase C activity

The inhibition of protein kinase C by hepatitis C virus non-structural protein 3 depends on its conformational status

Decrease of PKCalpha translocation to the erythrocyte membrane in patients with chronic renal failure [CRF]

Pituitary adenylate cyclase-activating polypeptide [PACAP] stimulates phosphoinositide metabolism and translocation of protein kinase C in chick cerebral cortex

The transition from a pharmacophore-guided approach to a receptor-guided approach in the design of potent protein kinase C ligands

Isozymes delta of phosphoinositide-specific phospholipase C

The ultraviolet studies on protein-lipid interaction of a protein kinase C-gamma phorbol-binding domain