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Wyszukujesz frazę "protein kinase A" wg kryterium: Temat


Wyświetlanie 1-4 z 4
Tytuł:
PP2A phosphatase interacts with CPK kinase and regulates pathogenesis responses triggered by intracellular ROS signals
Autorzy:
Kangasjarvi, S.
Denessiouk, K.
Trotta, A.
Konert, G.
Rahikainen, M.
Li, S.
Mhamdi, A.
Noctor, G.
Powiązania:
https://bibliotekanauki.pl/articles/80995.pdf
Data publikacji:
2013
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
conference
protein phosphatase 2A
calcium-dependent protein kinase
reactive oxygen species
organelle
protein kinase
plant immunity
Arabidopsis
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 2
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The expression profile of miR-222b-5p/MAPK10 in spleens of SPF chickens infected with REV-SNV at 28-42 dpi
Autorzy:
Jiang, H.
Gao, S.
Mao, M.
Diao, Y.
Tang, Y.
Hu, J.
Powiązania:
https://bibliotekanauki.pl/articles/2087117.pdf
Data publikacji:
2021
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
reticuloendotheliosis virus strain SNV
RLRs signaling pathway
gga-miR-222b-5p
mitogen-activated protein kinase 10
a dual-luciferase reporter gene experiment
Źródło:
Polish Journal of Veterinary Sciences; 2021, 24, 3; 439-443
1505-1773
Pojawia się w:
Polish Journal of Veterinary Sciences
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The involvement of protein kinase A in the immune response of Galleria mellonella larvae to bacteria
Autorzy:
Cytryńska, Małgorzata
Zdybicka-Barabas, Agnieszka
Jakubowicz, Teresa
Powiązania:
https://bibliotekanauki.pl/articles/1041132.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
antibacterial activity
protein kinase A
Rp-8-Br-cAMPS
lysozyme
Galleria mellonella
Opis:
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.
Źródło:
Acta Biochimica Polonica; 2007, 54, 1; 167-174
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Regulation of renal Na+,K+ -ATPase and ouabain-sensitive H+,K+ -ATPase by the cyclic AMP-protein kinase A signal transduction pathway.
Autorzy:
Bełtowski, Jerzy
Marciniak, Andrzej
Wójcicka, Grażyna
Górny, Dionizy
Powiązania:
https://bibliotekanauki.pl/articles/1043651.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
kidney
cyclic AMP
protein kinase A
cytochrome P450-dependent arachidonate metabolites
Na+,K+ -ATPase
H+,K+ -ATPase
Opis:
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 10-17 mol/kg per min and 10-6 mol/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 10-6 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.
Źródło:
Acta Biochimica Polonica; 2003, 50, 1; 103-114
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-4 z 4

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