Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników

Znaleziono wyników: 14

Liczba wyników na stronie
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników

Wyniki wyszukiwania

Wyszukiwano:
w słowach kluczowych:  protein kinase A
help Sortuj według:

help Ogranicz wyniki do:
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
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.
An active form of p38 protein kinase, belonging to the mitogen-activated protein kinases subfamily, has been designed based on crystallographically known structures of two other kinases, an active form of protein kinase A (PKA) and an inactive form of extracellular signal-regulated kinase 2 (ERK2). The modelling procedure is described. Its general scheme can also be applied to other kinases. The structure of the active forms of p38 and PKA is very similar in the region which binds the substrate. The ATP-binding mode is very similar in the active forms of all the three studied kinases. Models of the active forms allow for further studies on transphosphorylation processes at the molecular level, and modelling of inhibitors competitive with ATP and/or substrates.
We investigated the effect of the cyclic AMP-protein kinase A (PKA) signalling path­way on renal Na+ ,K+ -ATPase and ouabain-sensitive H+ ,K+ -ATPase. Male Wistar rats were anaesthetized and catheter was inserted through the femoral artery into the ab­dominal aorta proximally to the renal arteries for infusion of the investigated sub­stances. Na+ ,K+ -ATPase activity was measured in the presence of Sch 28080 to block ouabain-sensitive H+ ,K+ -ATPase and improve specificity of the assay. Dibutyryl-cyclic AMP (db-cAMP) administered at a dose of 10-7 mol/kg per min and 10 -6mol/kg per min increased Na+ ,K+ -ATPase activity in the renal cortex by 34% and 42%, respec­tively, and decreased it in the renal medulla by 30% and 44%, respectively. db-cAMP infused at 10- mol/kg per min increased the activity of cortical ouabain-sensitive H+,K+ -ATPase by 33%, and medullary ouabain-sensitive H+,K+ -ATPase by 30%. All the effects of db-cAMP were abolished by a specific inhibitor of protein kinase A, KT 5720. The stimulatory effect on ouabain-sensitive H+ ,K+ -ATPase and on cortical Na+ ,K+ -ATPase was also abolished by brefeldin A which inhibits the insertion of pro­teins into the plasma membranes, whereas the inhibitory effect on medullary Na+ ,K+ -ATPase was partially attenuated by 17-octadecynoic acid, an inhibitor of cytochrome P450-dependent arachidonate metabolism. We conclude that the cAMP-PKA pathway stimulates Na+ ,K+ -ATPase in the renal cortex as well as ouabain-sensitive H+ ,K+ -ATPase in the cortex and medulla by a mechanism requiring insertion of proteins into the plasma membrane. In contrast, medullary Na+ ,K+ -ATPase is inhibited by cAMP through a mechanism involving cytochrome P450-dependent arachidonate metabolites.
Shaker-related Kv1.3 channels are the most prevalent and widely studied ion channels in normal human T Lymphocytes (TL) as well as in certain T cell lines, such as Jurkat cells. This review focuses on modulatoty effects of intracellular cAMP on the activity of the channels. Available data provide evidence that: 1) intracellular cAMP directly activates a novel class of charybdotoxin-insensitive voltage-independent cAMP-gated K+ channels, but not the Kv1.3 channels both in quiescent and activated human T Lymphocytes, 2) intracellular cAMP reduces the Kv1.3 channel activity by protein kinase A - dependent channel phosphorylation in Jurkat TL cell line, 3) intracellular cAMP does not affect the activity of Kv1.3 channels in normal human T Lymphocytes. The apparently different effects of intracellular cAMP on Kv1.3 channels expressed in normal and Jurkat TL may reflect differences in the biochemical microenvironment as well as in an expression of auxiliary channel subunits in both cell types. A more complete biochemical characterisation of the Kv1.3 channel microenvironment and the channel-associated subunits in different T cell subtypes will be necessary to further elucidate this problem.
The gene SPI1, of Saccharomyces cerevisiae, encodes a cell wall protein that is induced in several stress conditions, particularly in the postdiauxic and stationary phases of growth. It has a paralogue, SED1, which shows some common features in expression regulation and in the null mutant phenotype. In this work we have identified homologues in other species of yeasts and filamentous fungi, and we have also elucidated some aspects of the origin of SPI1, by duplication and diversification of SED1. In terms of regulation, we have found that the expression in the post-diauxic phase is regulated by genes related to the PKA pathway and stress response (MSN2/4, YAK1, POP2, SOK2, PHD1, and PHO84) and by genes involved in the PKC pathway (WSC2, PKC1, and MPK1).
The role of protein kinase A (PKA) in the humoral immune response of the greater wax moth Galleria mellonella larvae to live Gram-positive bacteria Micrococcus lysodeikticus and Gram-negative bacteria Escherichia coli was investigated. The immune challenge of larvae with both kinds of bacteria caused an increase in fat body PKA activity depending on the injected bacteria. Gram-positive M. lysodeikticus was a much better inducer of the enzyme activity than Gram-negative E. coli. The PKA activity was increased about 2.5-fold and 1.5-fold, after M. lysodeikticus and E. coli injection, respectively. The in vivo inhibition of the enzyme activity by a cell permeable selective PKA inhibitor, Rp-8-Br-cAMPS, was correlated with considerable changes of fat body lysozyme content and hemolymph antimicrobial activity in bacteria-challenged insects. The kinetics of changes were different and dependent on the bacteria used for the immune challenge of G. mellonella larvae.
The nuclear matrices of plant cell nuclei display intrinsic nuclease activity which consists in nicking supercoiled DNA. A cDNA encoding a 32 kDa endonuclease has been cloned and sequenced. The nucleotide and deduced amino-acid sequences show high homology to known 14-3-3 protein sequences from other sources. The amino-acid sequence shows agreement with consensus sequences for potential phosphorylation by protein kinase A and C and for calcium, lipid and membrane-binding sites. The nucleotide-binding site is also present within the conserved part of the sequence. By Northern blot analysis, the differential expression of the corresponding mRNA was detected; it was the strongest in sink tissues. The endonuclease activity found on DNA-polyacrylamide gel electrophoresis coincided with mRNA content and was the highest in tuber.
It was found that wild type yeast Pichia pastoris can tolerate vanadate concentration as high as 25 mM in the growth medium. Moreover, four vanadate-resistant P. pastoris strains designated JC100/1, JC100/3, JC100/9 and JC100/15 exhibiting tol­erance up to 150 mM vanadate were selected. Growth of P. pastoris was correlated with vanadate to vanadyl reduction and its accumulation in the growth medium. In two selected strains, JC100/9 and JC100/15, protein kinase A activity was much higher in comparison to the wild type strain even without vanadate addition to the growth medium. Moreover, in the presence of vanadate, protein kinase A activity was significantly increased in the wild type and the vanadate-resistant JC100/1 and JC100/3 strains. It was also found that phosphorylation of a 40 kDa protein associ­ated with ribosomes occured in all vanadate-resistant strains from the logarithmic, while in the wild type strain from the stationary growth phase. From the presented re­sults it can be concluded that a protein kinase A signalling pathway(s) might be in­volved in the mechanism of P. pastoris vanadate resistance. The results also indicate a possible role of the 40 kDa protein in protection of P. pastoris against vanadate toxicity.
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.