Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:2.7.11.1 (protein kinase)
81,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A protein kinase and an acidic phosphoprotein phosphatase were purified from Tetrahymena pyriformis which phosphorylate and dephosphorylate the purified ornithine decarboxylase (ODC) of this microorganism. The protein kinase and the phosphoprotein phosphatase are copurified with ODC and can be separated in three distinct peaks only by a hydrophobic column of phenyl-Sepharose. The purified kinase is not dependent on cAMP, requires Mg2+ for its catalytic activity and has a molecule mass of 45 kDa. Incubation of [32P]ODC with the purified phosphoprotein phosphatase results in a complete loss of 32P and its catalytic activity. Phosphorylation of the inactive phosphatase-treated ODC by endogenous kinase or rat liver casein kinase-2 results in 100 or 40% reactivation of the initial untreated ODC activity, respectively.
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PMID:Interconversion of Tetrahymena pyriformis ornithine decarboxylase from inactive to active form by phosphorylation. 250 Jan 53

Purine analogues were used in this study to dissect specific steps in the mechanism of action of nerve growth factor (NGF). Protein kinase N (PKN) is an NGF-activated serine protein kinase that is active in the presence of Mn++. The activity of PKN was inhibited in vitro by purine analogues, the most effective of which was 6-thioguanine (apparent Ki = 6 microM). Several different criteria indicated that 6-thioguanine is not a general inhibitor of protein kinases and that it is relatively specific for PKN. For instance, it did not affect protein kinases A or C and was without effect on the overall level and pattern of protein phosphorylation by either intact or broken PC12 cells. Since purine analogues rapidly and effectively enter cells, they were also assessed for their actions on both transcription-dependent and -independent responses of PC12 cells to NGF. NGF-promoted neurite regeneration was reversibly suppressed by the analogues and at concentrations very similar to those that inhibit PKN. Comparable concentrations of the analogues also blocked NGF-stimulated induction of ornithine decarboxylase activity. In contrast to its inhibition of neurite regeneration and ornithine decarboxylase induction, 6-thioguanine did not suppress NGF-dependent induction of c-fos mRNA expression. Thus, purine analogues such as 6-thioguanine appear capable of differentially suppressing some, but not other actions of NGF. These findings suggest the presence of multiple pathways in the NGF mechanism and that these can be dissected with purine analogues. Moreover, these data are compatible with a role for protein kinase N in certain of these pathways.
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PMID:Differential inhibition of nerve growth factor responses by purine analogues: correlation with inhibition of a nerve growth factor-activated protein kinase. 255 45

Casein kinase II from a virally-transformed macrophage cell line (RAW264) was purified by a sequential DEAE, Procion Red, phosvitin-Sepharose and heparin-Sepharose chromatography. With [tau-32P]GTP as a phosphate donor and casein as a substrate, the kinase was stimulated by polyamines and inhibited by heparin. The purified kinase had a specific activity of 1137 nmol/min/mg protein and exhibited three major protein bands of 40 K, 35 K, and 25 K. Under non-denaturing conditions in 50 mM Tris-50 mM NaCl the enzyme was eluted as a single peak with molecular weight of 110 K. Incubation of kinase in the presence of [tau-32P]GTP and Mg2+ resulted in phosphorylation of the 25 K protein band of the enzyme. In the presence of [tau-32P]GTP and Mg2+ the kinase was able to phosphorylate 55 K protein band in purified ornithine decarboxylase preparation from RAW264 cells and the rat-type II regulatory subunit of the cyclic AMP-dependent protein kinase.
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PMID:Characterization of casein kinase II from a virally transformed macrophage-like cell line, RAW264. 262 1

The polypeptide hormones governing the proliferation and differentiation of the mature immune system and hematopoiesis are collectively referred to as lymphokines. We have examined a number of biochemical and molecular events stimulated by several unique lymphokines which exhibit proliferative activity on lymphoid and myeloid cell lines. Interleukin-2 (IL-2) and several members of the colony-stimulating factors (IL-3, G-CSF, and GM-CSF) stimulate similar patterns of cellular phosphorylation including the prominent phosphorylation of a 68-kDa substrate present in numerous distinct lineage cell lines. The 68-kDa substrate is phosphorylated by protein kinase C on threonine residues and is primarily cytosolic. Another kinase system activated by either physiological ligand or synthetic diacylglycerol phosphorylated the 40S ribosomal protein in a dose-dependent manner. The increased phosphorylation of S6 protein was associated with enhanced chain elongation in vitro. The kinase responsible for the in situ phosphorylation, however, was not protein kinase-C (PK-C) but another physicochemically distinct Mg2+-dependent enzyme (termed S6 kinase). These studies suggested that, although PK-C was activated by diacylglycerol, another kinase, S6 kinase, was the effector enzyme involved in the phosphorylation of the 40S protein. IL-2 and all other CSFs tested stimulated the transcription of the nuclear protooncogenes c-fos, c-myc, and c-myb. In addition, ornithine decarboxylase mRNA accumulation was also stimulated. Phorbol esters also stimulated similar gene expression; however, cyclic AMP analog inhibited phorbol ester or ligand-induced c-myc expression and ODC mRNA accumulation. Cyclic AMP agonists are antiproliferative to all the growth factors tested. We have constructed complementary oligonucleotides, "antisense", against c-fos, c-myc, and other structural genes induced by the growth factors. Such antisense oligomers were capable of selectively deleting protein expression of the respective gene products and inhibited the biological action of the growth factors.
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PMID:The molecular basis of immune cytokine action. 265 49

In cultured NG 108-15 neuroblastoma x glioma cells, opiates decreased cellular cyclic AMP and polyamine levels. This decrease was related to the inhibition of ornithine decarboxylase and cyclic AMP-dependent protein kinase activities during the acute exposure of the cells to the drugs. Growing the cells in the presence of opiates for several days led to drug addiction. In the tolerant-addicted cells, polyamine and cyclic AMP levels were close to normal values as were the activities of ornithine decarboxylase and cyclic AMP-dependent protein kinase. Removal of the opiate from 'addicted' cells, by either washing or by adding the antagonist naloxone, resulted in an increase in cyclic AMP and polyamine levels and the activities of ornithine decarboxylase and cyclic AMP-dependent protein kinase. The effect of opiates was closely related to their biological activities. Inactive enantiomorphs did not affect cyclic AMP or polyamine levels; neither did they decrease ornithine decarboxylase and cyclic AMP-dependent protein kinase activities.
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PMID:Opiates and cultured neuroblastoma x glioma cells. Effect on cyclic AMP and polyamine levels and on ornithine decarboxylase and protein kinase activities. 298 99

When guinea pig lymphocytes were cultured with 1-oleoyl-2-acetyl-glycerol (OAG), A23187, and cholera toxin, ornithine decarboxylase activity was induced synergistically, peaking at 6 h. Addition of 12-O-tetradecanoyl-phorbol 13-acetate (TPA), A23187, and dibutyryl cAMP caused the same kind of induction. Cholera toxin potentiated the ability of A23187 to induce ornithine decarboxylase, but not that of OAG. Dibutyryl cAMP augmented the induction caused by A23187 but not by TPA. These results suggest that both the activation of Ca++-sensitive, phospholipid-dependent protein kinase (protein kinase C) and the increase in intracellular levels of Ca++ and cAMP are necessary for this induction. cAMP may potentiate the induction by modulating a Ca++ messenger system other than that for protein kinase C activation.
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PMID:Synergistic induction of ornithine decarboxylase by diacylglycerol, A23187, and cholera toxin in guinea pig lymphocytes. 299 66

Ornithine decarboxylase, the rate-limiting enzyme in polyamine biosynthesis, has been shown to be regulated in thyroid by thyrotropin both in vivo and in vitro. Little, however, is known of the role of polyamines in thyroid cell function. Since studies in other tissues suggest that polyamines may influence protein phosphorylation, we studied the effect of the polyamines on various protein kinase activities in rat thyroid. Putrescine, spermidine, and spermine inhibit cyclic-AMP-dependent histone H1 kinase activity when measured in the cytosol fraction of rat thyroid; this effect is largely reproduced by NaCl concentrations of equivalent ionic strength. Both spermidine and spermine effect a 1.6-2.4-fold increase in cytosolic cyclic-AMP-independent (messenger-independent) casein kinase activity; stimulation by both polyamines is maximal at 5mM. A similar profile of stimulation is observed for messenger-independent casein kinase activity in crude nuclear preparations. Sodium chloride fails to stimulate both cytosolic and nuclear messenger-independent casein kinase activities at ionic strength equivalent to the spermine concentrations used. Spermine, but not putrescine, spermidine, or sodium chloride, inhibits calcium/phospholipid-dependent protein kinase C activity in cytosol extracts partially purified by DEAE chromatography. These findings suggest that regulation of protein kinase(s) by polyamines may represent a proximal locus (i) of action of thyrotropin-regulated ornithine decarboxylase activity in thyroid.
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PMID:Differential effects of polyamines on rat thyroid protein kinase activities. 299 43

Cyclosporine (CsA), a potent immunosuppressant for the prevention of transplant rejection, modulates T lymphocyte activation by blocking antigen stimulation and the production of interleukin-2. The mode of action by which CsA generates this immunosuppressive effect is unknown. We have studied two early intracellular enzymes associated with mitogen activation. They include calcium/phospholipid-dependent protein kinase (C-kinase) and cAMP-dependent protein kinase (cAMPd PK). Changes in protein kinase activation were correlated with the immunosuppression of polyamine and DNA synthesis measured by ornithine decarboxylase (ODC) induction and 3H-thymidine incorporation, respectively. These studies utilized murine T cell tumor lines sensitive to the effects of CsA. Similar to the mitogen activation of human peripheral blood lymphocytes, CsA was capable of inhibiting the induction of ODC and 3H-thymidine uptake of T cell tumor lines cultured with either fresh serum or mitogen. In contrast, C-kinase and cAMPd PK activation stimulated by the addition of fresh serum was not affected by CsA. Further, CsA did not inhibit the direct activation of C-kinase with phorbol esters or the activation of cAMPd PK with exogenous cAMP. We conclude that CsA does not affect the activation of either C-kinase or cAMPd PK in T cell tumor lines when activated by either fresh serum or when stimulated with chemical agents. The suppression of ODC induction and 3H-thymidine incorporation associated with CsA treatment cannot be accounted for with changes in C-kinase and cAMPd PK activation.
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PMID:Protein kinase activation and the immunosuppressant cyclosporine. 300 75

The intracisternal injection of either all-trans-retinoic acid or [alpha]-difluoromethylornithine (DFMO) into the brain of 9-day-old mice blocked (greater than 90%) phorbol ester-induced ornithine decarboxylase (ODC, EC 4.1.1.17) activity in a concentration-dependent fashion; this inhibition was not evident with the use of the biologically impotent furyl analog of retinoic acid. In a similar manner, retinoic acid reduced the soluble protein kinase-C (PK-C) activity by 60% as well as total EGTA-sensitive kinase activity (66%) associated with the plasma membrane. Sixty-six percent of the retinoic acid-induced loss of PK-C activity in the soluble fraction could be accounted for by the translocation of PK-C to the plasma membrane as measured by the specific binding of 12-O-[3H]tetradecanylphorbol-13-acetate (TPA). DFMO and furyl-retinoic acid were not effective in altering PK-C activity or TPA binding to PK-C. In the presence of retinoic acid, however, there was a 2.3-fold increase in specific [3H]TPA binding in the plasma membrane fraction, which was 3.4-fold greater than that lost from the cytosol. Because retinoids do not directly affect TPA binding to PK-C, the data suggest that (i) the presence of retinoic acid results in the exposure of heretofore cryptic TPA-binding sites in the membrane, where this binding is most likely related to the alteration of membrane structure and (ii) de novo ODC induction is not required for retinoid-dependent inhibition of PK-C, although the TPA induction of PK-C appears to be necessary with regard to ODC induction.
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PMID:The in vivo inhibition of mouse brain protein kinase-C by retinoic acid. 300 83

To elucidate the biological mechanisms of 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced phenotypic changes in HTLV-I virus-infected human T-cell line KH-2Lo cells, inhibitors of TPA-induced ornithine decarboxylase (ODC), protein kinases and calmodulin were examined for their effects on TPA-induced multinucleated cell formation and HTLV-I p19 antigen expression. Among the inhibitors of TPA-induced ODC activity, alpha-difluoromethyl ornithine (DFMO), 1,25(OH)2D3 and its analogues, and retinoic acid were tested. As inhibitors of protein kinases, 1-(5-isoquinolinyl-sulfonyl)-2-methylpiperazine (H-7), N-[2-(methylamino)ethyl]-5-isoquinoline-sulfonamide (H-8) and 1,(5-isoquinolynylsulfonyl)-2,3-dimethylpiperazine (H-5) were used. In addition, a calmodulin inhibitor, N-(4-aminobutyl)-5-chlor-2-naphthalenesulfonamide (W13) and its inactive analogue, N-(4-aminobutyl)-2-naphthalenesulfonamide (W12) were also tested. 1,25(OH)2D3 and its active analogues inhibited both TPA-induced HTLV-I p19 antigen expression and multinucleated cell formation after 4 days of culture with TPA. On the other hand, an inhibitor of ODC, DFMO, the protein kinase inhibitors, the calmodulin inhibitor and retinoic acid suppressed TPA-induced HTLV-I p19 expression but did not suppress multinucleated cell formation.
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PMID:Inhibitors of 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced multinucleated cell formation and HTLV-I p19 antigen expression in HTLV-I-infected T-cell line KH-2Lo. 301 86


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