Bidirectional control of phospholipase A2 activity by Ca2+/calmodulin-dependent protein kinase II, cAMP-dependent protein kinase, and casein kinase II.

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Bidirectional control of phospholipase A2 activity by Ca2+/calmodulin-dependent protein kinase II, cAMP-dependent protein kinase, and casein kinase II.

In preparations of synaptic terminals (synaptosomes) isolated from rat brain, the activity of phospholipase A2 (PLA2), a phospholipid hydrolase that serves a central function in signal transduction, was inhibited in a Ca(2+)-dependent manner by incubation with 60 mM K+ or with the Ca(2+)-selective ionophore ionomycin. Reversal by alkaline phosphatase treatment suggested that this inhibitory eff...

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THE EFFECT OF THEOPHYLLINE ON THE KINETICS OF cAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT, cAMP, PROTEIN KINASE INHIBITOR AND THEIR RELATIONSHIP IN LUNG TISSUE

We have investigated the effect of theophylline on the kinetics of the catalytic subunit of protein kinase and related factors in lung tissue. The results show that the point of highest concentration of the C subunit of protein kinase which is active in casein phosphorylation is at 3h of incubation time, but in the presence of 100 Ilg/ InL and 10µg/mL theophylline, this is shifted to I.S an...

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Subcellular Localization of the Type II CAMP-Dependent Protein Kinase

Hormone-receptor interactions generate signals that trigger protein kinase-catalyzed phosphorylation events (12). The action of 30 or more catecholamine and peptide hormones, as well as some prostaglandins, proceeds through parallel pathways that elevate intracellular adenosine 3’,5’-cyclic monophosphate (CAMP) and lead to activation of the CAMP-dependent protein kinase (PKA). An apparent parad...

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the effect of theophylline on the kinetics of camp-dependent protein kinase catalytic subunit, camp, protein kinase inhibitor and their relationship in lung tissue

we have investigated the effect of theophylline on the kinetics of the catalytic subunit of protein kinase and related factors in lung tissue. the results show that the point of highest concentration of the c subunit of protein kinase which is active in casein phosphorylation is at 3h of incubation time, but in the presence of 100 ilg/ inl and 10µg/ml theophylline, this is shifted to i.s and 2....

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Induced interchain disulfide bonding in cAMP-dependent protein kinase II.

Cupric phenanthroline was used to catalyze the formation of disulfide bonds in cAMP-dependent protein kinase II. Incubation of holoenzyme alone with cupric phenanthroline resulted in no disulfide bond formation. In contrast, when holoenzyme was preincubated with cAMP prior to treatment with cupric phenanthroline, specific interchain disulfide bonding was found between the regulatory (R) and cat...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 1991

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.88.15.6770