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)

Protein kinase CKII (i.e. casein kinase II, CKII, NII) is expressed at a higher level in rapidly proliferating tissues and in solid human tumours (e.g. colorectal carcinomas) when compared to the corresponding non-neoplastic colorectal mucosa. This could be shown by (a) Western blotting of cellular extracts from solid tumours followed by immunostaining with an anti-CKII polyclonal antibody, (b) immunohistochemical staining of cells from tissue sections and (c) by activity measurements using the CKII-specific synthetic peptide (RRRDDDSDDD). The maximum observed activity in the colorectal carcinomas investigated was up to eightfold higher in the tumour specimens than in the non-neoplastic tissue (i.e. colorectal mucosa). The activity range was between 33-350 U/mg protein and in the case of colorectal mucosa 13-106 U/mg protein. The amount of CKII determined in the individual tumours was in the range 0.4-1.6 nmol/g tissue.
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PMID:Casein kinase II is elevated in solid human tumours and rapidly proliferating non-neoplastic tissue. 215 76

Protein kinase FA (an activating factor of ATP.Mg-dependent protein phosphatase) has been characterized to exist in two forms in the purified brain myelin. One form of kinase FA is spontaneously active and trypsin-labile, whereas the other form of kinase FA is inactive and trypsin-resistant, suggesting a different membrane topography with active FA exposed on the outer face of the myelin membrane and inactive FA buried within the myelin membrane. When myelin was solubilized in 1% Triton X-100, all kinase FA became active and trypsin-labile. Phospholipid reconstitution studies further indicated that when kinase FA was reconstituted in acidic phospholipids, such as phosphatidylinositol and phosphatidylserine, the enzyme activity was inhibited in a dose-dependent manner, suggesting that kinase FA interacts with acidic phospholipids which inhibit its activity. Furthermore, when myelin was incubated with exogenous phospholipase C, the inactive/trypsin-resistant FA could be converted to the active/trypsin-labile FA in a time- and dose-dependent manner. Taken together, it is concluded that membrane phospholipids play an important role in modulating the activity of kinase FA in the brain myelin. It is suggested that phospholipase C may mediate the activation-sequestration of inactive/trypsin-resistant kinase FA in the brain myelin through the phospholipase C-catalyzed degradation of acidic membrane phospholipids. The activation-sequestration of protein kinase FA may represent one mode of control modulating the activity of kinase FA in the central nervous system myelin.
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PMID:On the mechanism of activation of protein kinase FA (an activating factor of ATP.Mg-dependent protein phosphatase) in brain myelin. 216 Feb 45

Fractions containing myelin of varying degrees of compaction were prepared from human white matter. Protein kinase activity in these fractions was measured by using both endogenous and exogenous myelin basic protein (MBP) as substrates. In both cases, less compact myelin fractions possessed higher levels of protein kinase activity than the compact myelin fraction. In addition, the specific activity of phosphorylated basic protein was greater in the loosely compacted fractions than in compact multilamellar myelin. When basic protein in compact myelin or the myelin fractions was phosphorylated by the endogenous kinase, approximately 70% of the [32P]phosphate was incorporated at a single site, identified as Ser-102. The remaining 30% was found in three other minor sites. Electron microscopy of less compact myelin showed it was composed of fewer lamellae which correlated with a relative decrease in the proportion of cationic charge isomers (microheteromers) when MBP was subjected to gel electrophoresis at alkaline pH. The shift in charge microheterogeneity of basic protein to the less cationic isomers in the less compact myelin fractions correlated with an increase in protein kinase activity and a greater specific activity of phosphorylated basic protein.
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PMID:Endogenous phosphorylation of basic protein in myelin of varying degrees of compaction. 246 8

Protein kinase activities were detected in cell-free extracts of the B385 derivative of Streptomyces coelicolor A3(2); at least 12 polypeptides, ranging in Mr from 6,000 to 98,000, were detectably phosphorylated, probably as O-monoesters, after incubation with gamma [32P]ATP. The culture stage of the mycelia used for production of the cell-free extracts determined the profile of phosphorylated polypeptides. Phosphoenol pyruvate acted as a potent modulator of the apparent degree of protein kinase activity. In addition Ca2+ ions, verapamil, chlorpromazine and anti-calmodulin antiserum had specific effects on the profile of phosphopolypeptides observed.
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PMID:Protein kinase activities in cell-free extracts of Streptomyces coelicolor A3(2). 251 2

Fertilization of the sea urchin egg initiates or accelerates a number of metabolic activities, which have been causally linked to a rise in cytoplasmic pH due to increased Na+-H+ antiport. Two possible regulatory pathways linking sperm-egg fusion to the activity of the antiporter are activation of protein kinase C (PKC) and Ca2+, calmodulin (CaM)-dependent kinase. This report presents the effects of protein kinase inhibitors on antiporter activation during fertilization and treatment with PKC agonists, dioctanoylglycerol or phorbol diester. Protein kinase inhibitors, K252a and H-7 blocked the action of PKC agonists, without inhibiting cytoplasmic alkalinization during fertilization. In contrast, W-7 blocked fertilization-induced rise in cytoplasmic pH, without altering the actions of PKC agonists. These results suggest that the Na+-H+ antiporter may be regulated by PKC or Ca2+, CaM-dependent kinase activities, but activation of the antiporter during fertilization is Ca2+, CaM-dependent, despite production of diacylglycerols by hydrolysis of phosphatidylinositols.
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PMID:Na+-H+ antiport during fertilization of the sea urchin egg is blocked by W-7 but is insensitive to K252a and H-7. 254 96

The cause and effect relationship between mutations in cAMP-dependent protein kinase activity and resistance of adrenocortical tumor cells to ACTH and cAMP was evaluated by transfection with cloned cDNAs encoding subunits of the mouse cAMP-dependent protein kinase. Protein kinase defective, Kin 8 adrenocortical tumor cells were transfected with pRev [an expression vector encoding the regulatory subunit of the type 1 cAMP-dependent protein kinase (RI)] or with pC alpha ev [an expression vector encoding the catalytic subunit of cAMP-dependent protein kinase (C)]. The pC alpha ev transformant recovered cAMP responsive protein kinase activity, whereas the pRev transformant recovered cAMP-binding activity, but did not recover cAMP responsive protein kinase activity. The pC alpha ev transformant concomitantly recovered steroidogenic and morphologic responsiveness to ACTH- and 8-bromo-cAMP, whereas the pRev transformant remained resistant to these effects of the hormone and cyclic nucleotide. Since Kin 8 cells recovered their responsiveness to ACTH and 8-bromo-cAMP following transfection with pC alpha ev we suggest that the defect in cAMP-dependent protein kinase activity is directly responsible for the ACTH- and cAMP-resistant phenotype of the Kin 8 mutant.
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PMID:Recovery of responsiveness to ACTH and cAMP in a protein kinase-defective adrenal cell mutant following transfection with a protein kinase gene. 254 99

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

The HXK2 gene product has an important role in controlling carbon catabolite repression in Saccharomyces cerevisiae. We have raised specific antibodies against the hexokinase PII protein and have demonstrated that it is a 58 kDa phosphoprotein with protein kinase activity. The predicted amino acid sequence of the HXK2 gene product has significant homology to the conserved catalytic domain of mammalian and yeast protein kinases. Protein kinase activity was located in a different domain of the protein from the hexose-phosphorylating activity. The hexokinase PII protein level remained unchanged in P2T22D mutant cells (hxk1 HXK2 glk1) growing in a complex medium with glucose. The protein kinase activity of hexokinase PII is regulated by the glucose concentration of the culture medium. Exit from the carbon catabolite repression phase and entry into derepression phase may be controlled, in part, by modulation of the 58 kDa protein kinase activity by changes in cyclic AMP concentration.
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PMID:The hexokinase isoenzyme PII of Saccharomyces cerevisiae ia a protein kinase. 255 46

Adrenaline, cAMP and cAMP-dependent protein kinase modulate the slow inward Ca current by the same basic mechanism, presumably a phosphorylation of membrane proteins. Protein kinase also seems to play a role in the regulation of K outward currents, but not for the transient inward current.
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PMID:Cardiac membrane currents and energetic state. 258 42

The cell-cycle timing of mitosis in fission yeast is determined by the cdc25+ gene product activating the p34cdc2 protein kinase leading to mitotic initiation. Protein kinase activity remains high in metaphase and then declines during anaphase. Activation of the protein kinase also requires the cyclin homolog p56cdc13, which also functions post activation at a later stage of mitosis. The continuing function of p56cdc13 during mitosis is consistent with its high level until the metaphase/anaphase transition. At anaphase the p56cdc13 level falls dramatically just before the decline in p34cdc2 protein kinase activity. The behavior of p56cdc13 is similar to that observed for cyclins in oocytes. p13suc1 interacts closely with p34cdc2; it is required during the process of mitosis and may play a role in the inactivation of the p34cdc2 protein kinase. Therefore, the cdc25+, cdc13+, and suc1+ gene products are important for regulating p34cdc2 protein kinase activity during entry into, progress through, and exit from mitosis.
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PMID:Regulation of p34cdc2 protein kinase during mitosis. 266 44


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