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Wyszukujesz frazę "AMP" wg kryterium: Temat

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    Wyświetlanie 1-5 z 5
    Tytuł:
    AMP-deaminase from hen stomach smooth muscle - physico-chemical properties of the enzyme.
    Autorzy:
    Swieca, Anna
    Rybakowska, Iwona
    Koryziak, Anna
    Klimek, Jerzy
    Kaletha, Krystian
    Powiązania:
    https://bibliotekanauki.pl/articles/1043348.pdf
    Data publikacji:
    2004
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    AMP-deaminase
    smooth muscle
    Opis:
    AMP-deaminase from hen stomach smooth muscle was isolated and physico-chemical properties of the purified enzyme were investigated. The enzyme had an activity optimum at pH 6.5, and poorly deaminated the substrate analogues tested. At optimum pH (6.5), in the absence of regulatory ligands (control conditions), the enzyme manifested hyperbolic substrate-saturation kinetics with half-saturation constant (S0.5) of about 4.5 mM. Additions of adenine nucleotide effectors (ATP, ADP) activated the enzyme strongly at all the concentrations tested, diminishing significantly the value of S0.5 constant. In contrast, the regulatory effect of orthophosphate was variable, and depended on the orthophosphate concentration used. The molecular mass of the enzyme subunit determined in SDS/PAG electrophoresis was about of 37 kDa. The obtained results suggest that in different types of hen muscle, similarly as in humans and rats, expression of AMP-deaminase is under the control of independent genes.
    Źródło:
    Acta Biochimica Polonica; 2004, 51, 1; 213-218
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Rabbit muscle fructose-1,6-bisphosphatase is phosphorylated in vivo.
    Autorzy:
    Rakus, Dariusz
    Zarzycki, Marek
    Dzugaj, Andrzej
    Powiązania:
    https://bibliotekanauki.pl/articles/1043652.pdf
    Data publikacji:
    2003
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    aldolase
    muscle
    phosphorylation
    AMP
    fructose-1,6-bisphosphatase
    Opis:
    Phosphorylated fructose-1,6-bisphosphatase (FBPase) was isolated from rabbit muscle in an SDS/PAGE homogeneous form. Its dephosphorylation with alkaline phosphatase revealed 2.8 moles of inorganic phosphate per mole of FBPase. The phosphorylated FBPase (P-FBPase) differs from the dephosphorylated enzyme in terms of its kinetic properties like Km and kcat, which are two times higher for the phosphorylated FBPase, and in the affinity for aldolase, which is three times lower for the dephosphorylated enzyme. ephosphorylated FBPase can be a substrate for protein kinase A and the amount of phosphate incorporated per FBPase monomer can reach 2-3 molecules. Since interaction of muscle aldolase with muscle FBPase results in desensitisation of the latter toward AMP inhibition (Rakus & Dzugaj, 2000, Biochem. Biophys. Res. Commun. 275, 611-616), phosphorylation may be considered as a way of muscle FBPase activity regulation.
    Źródło:
    Acta Biochimica Polonica; 2003, 50, 1; 115-121
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Metformin reduces NAD(P)H oxidase activity in mouse cultured podocytes through purinergic dependent mechanism by increasing extracellular ATP concentration
    Autorzy:
    Piwkowska, Agnieszka
    Rogacka, Dorota
    Jankowski, Maciej
    Angielski, Stefan
    Powiązania:
    https://bibliotekanauki.pl/articles/1039452.pdf
    Data publikacji:
    2013
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    AMP-activated kinase
    free radicals
    metformin
    NAD(P)H oxidase
    podocytes
    purinoceptors
    Opis:
    Hyperglycemia affects the functioning numbers of podocytes and leads to a gradual decline of renal function. The normalization of glucose level is a principle therapeutic goal in diabetic patients and metformin is a popular hypoglycemic drug used in type 2 diabetes mellitus. Metformin activates AMP-activated kinase (AMPK) and decreases NAD(P)H oxidase activity in podocytes leading to reduction of free radical generation. Similar effects are observed after activation of P2 receptors. Therefore, we investigated whether metformin increases extracellular ATP concentration and affects the activities of NAD(P)H oxidase and AMPK through P2 receptors. Experiments were performed on cultured mouse podocytes. NAD(P)H oxidase activity was measured by chemiluminescence and changes in AMPK activity were estimated by immunoblotting against AMPKα-Thr172-P. Metformin increased extracellular ATP concentration by reduction of ecto-ATPase activity, decreased NAD(P)H oxidase activity and increased AMPK phosphorylation. A P2 receptor antagonist, suramin (300 µM), prevented metformin action on NAD(P)H oxidase and AMPK phosphorylation. The data suggests a novel mechanism of metformin action, at least in podocytes. Metformin, which increases extracellular ATP concentration leads to activation of P2 receptors and consequent modulation of the podocytes' metabolism through AMPK and NAD(P)H oxidase which, in turn, may affect podocyte functioning.
    Źródło:
    Acta Biochimica Polonica; 2013, 60, 4; 607-612
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Ganoderma lucidum extract stimulates glucose uptake in L6 rat skeletal muscle cells
    Autorzy:
    Jung, Kyung
    Ha, Eunyoung
    Kim, Mi-Ja
    Uhm, Yoon
    Kim, Hye
    Hong, Seung-Jae
    Chung, Joo-Ho
    Yim, Sung-Vin
    Powiązania:
    https://bibliotekanauki.pl/articles/1041224.pdf
    Data publikacji:
    2006
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Ganoderma lucidum extract
    skeletal muscle
    phosphatidylinositol 3-kinase
    AMP-activated protein kinase
    glucose uptake
    Opis:
    The effect of Ganoderma lucidum extract on glucose uptake was studied in L6 rat skeletal muscle cells. G. lucidum extract increased glucose uptake about 2-fold compared to control. The extract stimulated the activity of phosphatidylinositol (PI) 3-kinase which is a major regulatory molecule in the glucose uptake pathway. About 7-fold increased activity of a PI 3-kinase was observed after treatment with G. lucidum extract, whereas PI 3-kinase inhibitor, LY294002, blocked the G. lucidum extract-stimulated PI 3-kinase activity in L6 skeletal muscle cells. Protein kinase B, a downstream mediator of PI 3-kinase, was also activated by G. lucidum extract. We then assessed the activity of AMP-activated protein kinase (AMPK), another regulatory molecule in the glucose uptake pathway. G. lucidum extract increased the phosphorylation level of both AMPK α1 and α2. Activity of p38 MAPK, a downstream mediator of AMPK, was also increased by G. lucidum extract. Taken together, these results suggest that G. lucidum extract may stimulate glucose uptake, through both PI 3-kinase and AMPK in L6 skeletal muscle cells thereby contributing to glucose homeostasis.
    Źródło:
    Acta Biochimica Polonica; 2006, 53, 3; 597-601
    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 1-5 z 5

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