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1

Regulation of nuclear phospholipase C activity

100%
Manzoli L., Billi A. M., Martelli A. M., Cocco L.
Acta Biochimica Polonica
|
2004
|
tom 51
|
nr 2
A body of evidence, linking inositide-specific phospholipase C (PI-PLC) to the nu­cleus, is quite extensive. The main isoform in the nucleus is PI-PLQCß1, whose activity is up-regulated in response to insulin-like growth factor-1 (IGF-1) or insulin stimula­tion. Whilst at the plasma membrane this PI-PLC is activated and regulated by Gaq/a11 and Gßy subunits, there is yet no evidence that qa/a11 is present within the nuclear compartment, neither GTP-y-S nor AlF4 can stimulate PI-PLCß1 activity in isolated nuclei. Here we review the evidence that upon occupancy of type 1 IGF re­ceptor there is translocation to the nucleus of phosphorylated mitogen-activated pro­tein kinase (MAPK) which phosphorylates nuclear PI-PLCß1 and triggers its signal­ling, hinting at a separate pathway of regulation depending on the subcellular loca­tion of PI-PLCß1. The difference in the regulation of the activity of PI-PLCß1 mirrors the evidence that nuclear and cytoplasmatic inositides can differ markedly in their signalling capability. Indeed, we do know that agonists which affect nuclear inositol lipid cycle at the nucleus do not stimulate the one at the plasma membrane.
2
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Differentiation of Listeria monocytogenes on the basis of hemolytic and phosphatidylinositol specific phospholipase C activity and by PCR method

100%
Kotlowski R., Kaczmarek M., Kur J., Rudnicka W.
Polish Journal of Food and Nutrition Sciences
|
1996
|
tom 05
|
nr 3
The possibility of differentiation of L.monocytogenes from other Listeria species on the basis of hemolytic activity, the production of phosphatidylinositol-specific phospholipase C (PI-PLC) and the polymerase chain reaction (PCR) for the amplification of a DNA fragment of listeriolysine O (hly A) gene was compared. The screening of Listeria colonies for PI-PLC activity allowed to distinguish the pathogenic for humans L.monocytogenes bacteria from the majority of non-pathogenic Listeria spp. The amplification of DNA from Listeria lysates with two primers selected in area of the hly A gene made possible the differentiation of L.monocytogenes from other Listeria species, including hemolytic L.ivanovii and L.seeligeri bacteria as well as hemolytic or PI-PLC positive L.innocua strains.
3

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

100%
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
|
1998
|
tom 03
|
nr 3
4

Isozymes delta of phosphoinositide-specific phospholipase C

100%
Pawelczyk T.
Acta Biochimica Polonica
|
1999
|
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.
5

Accumulation of inositol phosphates in human lymphocytes after cholinergic stimulation

100%
Laskowska-Bozek H., Bany U., Stokarska G., Ryzewski J.
Acta Biochimica Polonica
|
1993
|
tom 40
|
nr 1
6

Gastrin activates tyrosine kinase and phospholipase C in isolated rat colonocytes

84%
Malecka-Panas E., Tureaud J., Majumdar A. P. N.
Acta Biochimica Polonica
|
1996
|
tom 43
|
nr 3
Postreceptor regulation of the trophic action of gastrin is not fully elucidated. Tyrosine kinase (Tyr-kinase) has been associated with receptors of a number of growth factors and plays an important role in regulation of cellular growth within the gastrointestinal tract. The aim of this study was to determine, whether Tyr-kinase plays a role in mediating the growth promoting action of gastrin and whether phos­pholipase C (PLC) is involved in the signal transduction pathway. Colonocytes isolated from Fischer 344 rats were incubated for 2 min with gastrin (10-8 M) and assayed for Tyr-kinase and PLC activities. Incubations with gastrin resulted in 60%-70% rise in Tyr-kinase and 150%-200% rise in PLC activities over the corresponding basal levels. When processed separately, in proximal colon Tyr-kinase activation by gastrin was 15%-20%, while in distal colon 70%-80% as compared to the buffer control. Gastrin activation of both Tyr-kinase and PLC was abolished by Tyr-kinase inhibitor, tyrphostin-25 (3.2 nM) and was not affected by staurosporine (20 ng/ml). We conclude that Tyr-kinase is involved in the mechanism of trophic action of gastrin, and PLC activation appears to be the next step in the signal transduction pathway.
7

Intraperitoneal fluid accumulation induced by Clostridium perfringens alpha-toxin [phospholipase C]

84%
Maegawa T., Wang X., Karasawa T., Zuka M., Kita H., Nakamura S.
Acta Microbiologica Polonica
|
2002
|
tom 51
|
nr 4
8

Molecular aspects of Listeria monocytogenes infection

84%
Krawczyk-Balska A., Bielecki J.
Polish Journal of Microbiology
|
2004
|
tom 53
|
nr Suppl.
Listeria monocytogenes, a food-borne intracellular animal and human pathogen, interacts with infected host cells both prior to entry and during the intracellular phase of infection. This review is focused on the role of secreted proteins including listeriolysin O and two distinct phospholipases C, in modulating the signal transduction of infected cells.
9

Cross-talk between the ATP and ADP nucleotide receptor signalling pathways in glioma C6 cells

84%
Czajkowski R., Baranska J.
Acta Biochimica Polonica
|
2002
|
tom 49
|
nr 4
In this review we summarize the present status of our knowledge on the enzymes in­volved in the extracellular metabolism of nucleotides and the receptors involved in nucleotide signalling. We focus on the mechanism of the ATP and ADP signalling path­ways in glioma C6, representative of the type of nonexcitable cells. In these cells, ATP acts on the P2Y2 receptor coupled to phospholipase C, whereas ADP on two distinct P2Y receptors: P2Y1 and P2Y12. The former is linked to phospholipase C and the lat­ter is negatively coupled to adenylyl cyclase. The possible cross-talk between the ATP-, ADP- and adenosine-induced pathways, leading to simultaneous regulation of inositol 1,4,5-trisphosphate and cAMP mediated signalling, is discussed.
10

Sphingosine modulates Ca2 signals via phospholipase C dependent pathway in glioma C6 cells

84%
Czajkowski R., Sabala P., Baranska J.
Acta Neurobiologiae Experimentalis
|
1997
|
tom 57
|
nr 4
11

Expression, purification and kinetic properties of human recombinant phospholipase C delta3

67%
Pawelczyk T., Matecki A.
Acta Biochimica Polonica
|
1997
|
tom 44
|
nr 2
To obtain sufficient quantities of pure phospholipase C delta 3 (PLC delta 3) necessary for structural and kinetic studies, cDNA of human fibroblast PLC delta 3 was cloned in the pPROEX-1 vector, expressed in E. coli cells as a (6 x His) fusion protein and purified to homogeneity. From 1 L of E. coli culture 8 mg of pure PLC delta 3 was obtained by a two step purification procedure, which includes phosphocellulose and Mono S cation exchange chromatography. The presence of His tag did not affect the catalytic and regulatory properties of PLC delta 3. The K(app) for PIP2 was 142 +/- 11 and 156 +/- 12 microM for His.PLC delta 3 and PLC delta 3, respectively. Recombinant PLC delta 3 showed an absolute requirement for Ca2+. Increasing the free Ca2+ concentration from 0.2 to 0.5 microM resulted in a sharp increase in enzyme activity. In comparison with human recombinant PLC delta 1 the delta 3 isoenzyme was more sensitive to low Ca2+ concentration. The Ca2+ concentration yielding maximal activation of PLC delta 1 and PLC delta 3 was 10 and 1 microM, respectively. The activity of PLC delta 3 was stimulated by polyamines and by basic proteins such as protamine, histone and mellitin. PLC delta 3 was activated most effectively by spermine and histone but the extent of this activation was lower than for PLC delta 1. The data presented indicate that the expression of PLC delta 3 in E. coli cells permits to obtain active enzyme. The catalytic and regulatory properties of PLC delta 3 are similar to those of PLC delta 1.
12

Acute hypoxia modulates arachidonic acid metabolism in cat carotid bodies. Role of dopamine

67%
Strosznajder R. P.
Acta Neurobiologiae Experimentalis
|
1996
|
tom 56
|
nr 2
13

Effect of estradiol and progesterone on growth of porcine myometrial smooth muscle cells and phospholipase C and adenylate cyclase signalling systems in vitro

67%
Kisielewska J., Zezula-Szpyra A., Bilinska B., Flint A. P. F., Ziecik A. J.
Folia Histochemica et Cytobiologica
|
1997
|
tom 35
|
nr 3
14

Increased activity of phospholipase C in aortas of spontaneously hypertensive rats correlates with decreased sphingomyelin: total phospholipid ratio

67%
Gryckiewicz E., Dettlaff A., Pawelczyk T.
Cellular and Molecular Biology Letters
|
1998
|
tom 03
|
nr 1
The activity of phospholipase C (PLC) in the aortas of spontaneously hypertensive rats (SHR) was higher than in the aortas of age-matched normotensive Wistar-Kyoto rats (WKY). This was associated with the higher level of inositol 1,4,5-trisphosphate and diacylglycerol in aortas of SHR compared to the level of these compounds found in aortas of WKY. Observed changes in PLC activity correlates with changes in phospholipid composition of SHR aortas. The sphingomyelin (SM) to total phospholipid ratio decreased significantly in aortas of SHR compared to WKY. Since, SM was proposed to be the major PLC δ inhibitor in vivo (Arch. Biochem. Biophys. 297 (1992) 328-333) it might be possible that observed higher activity of PLC in aortas of SHR results from decreased content of this phospholipid.
15
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ATP activates phospholipase C in the cat carotid body in vitro

67%
Pokorski M., Strosznajder R.
Journal of Physiology and Pharmacology
|
1997
|
tom 48
|
nr 3
16

Regulation of wound-responsive calcium-dependent protein kinase from maize (ZmCPK11) by phosphatidic acid

59%
Klimecka M., Szczegielniak J., Godecka L., Lewandowska-Gnatowska E., Dobrowolska G., Muszynska G.
Acta Biochimica Polonica
|
2011
|
tom 58
|
nr 4
In plant cells, phospholipids are not only membrane components but also act as second messengers interacting with various proteins and regulating diverse cellular processes, including stress signal transduction. Here, we report studies on the effects of various phospholipids on the activity and expression of maize wound-responsive calcium-dependent protein kinase (ZmCPK11). Our results revealed that in leaves treated with n-butanol, a potent inhibitor of phosphatidic acid (PA) synthesis catalyzed by phospholipase D, a significant decrease of ZmCPK11 activity was observed, indicating contribution of PA in the kinase activation. Using lipid binding assays, we demonstrate that among various phospholipids only saturated acyl species (16 : 0 and 18 : 0) of phosphatidic acid are able to bind to ZmCPK11. Saturated acyl species of PA are also able to stimulate phosphorylation of exogenous substrates by ZmCPK11 and autophosphorylation of the kinase. The level of ZmCPK11 autophosphorylation is correlated with its enzymatic activity. RT-PCR analysis showed that transcript level of ZmCPK11 in maize leaves increased in response to PA treatment. The influence of PA on the activity and transcript level of ZmCPK11 suggests an involvement of this kinase in a PA-mediated wound signal transduction pathway.
17

Jak atakuje Helicobacter pylori?

59%
Lekowska-Kochaniak A.
Żywność, Żywienie a Zdrowie
|
1995
|
tom 04
|
nr 1-4
44-48
18

ATP a potent regulator of inositol phospholipids-phospholipase C and lipid mediators in brain cortex

59%
Strosznajder J., Strosznajder R. P.
Acta Neurobiologiae Experimentalis
|
1996
|
tom 56
|
nr 2
19

Epidermal growth factor signalling in rat pancreatic acinar cells

59%
Stryjek-Kaminska D.
Journal of Physiology and Pharmacology. Supplement
|
1998
|
tom 49
|
nr 1
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