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)

Superspiralized coiled plasmide DNA were found in cells E. coli CK. One of plasmides pEco CK-1 had a size 21.2 micron that corresponded to molecular mass 43.7 megadaltons, another plasmide pEco CK-2 with the size 14.2 micron had a molecular weight 29.2 megadaltons. Effective restriction was observed in cross titration using phage PBV-I.CK for E. coli strains carrying R II plasmide and phage PBV-I.R II for E. coli CK cells. The data obtained suggest that the Eco CK type with DNA of host specificity is distinct from hsp II type due to presence of R II and N-15 plasmides.
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PMID:[Detection of plasmids in the cells of E. coli CK]. 38 26

The genetic basis of isozyme phenotypes of creatine kinase (CK) from extracts of skeletal muscle of salmonids has been resolved through breeding data including double heterozygous crosses and backcrosses of rainbow trout (Salmo gairdneri), and backcrosses of coho salmon (Oncorhynchus kisutch). The two-three-, or four-banded phenotypes of homozygous individuals and all heterozygous and hybrid phenotypes of ten salmonid species are readily explained by the following model: (1) there are no detectable heterodimers either between allelic products at a single locus or between loci: (2) each allele is represented electrophoretically by two bands, presumably a reflection of stable posttranslational modification of a single polypeptide unit; (3) CK of salmonid muscle is encoded by two loci--CK-1 and CK-2. The distance separating the paired bands reflecting each allele provides a basis for two groupings--a broad-spaced group (including all species of Oncorhynchus tested excepting O. masou) and a narrow-spaced group (including all species of Salmo tested and O. masou). The relationships among species suggested by the relative mobilities and spacings of these CK bands are consistent with taxonomic schemes inferred from morphological, cytogenetic, and other isozymic data.
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PMID:Genetic basis of creatine kinase isozymes in skeletal muscle of salmonid fishes. 54 1

The total activity and range of the creatine kinase (CK) isozymes have been studied in the homogenate and subcellular fractions (nuclei, mitochondria, cytoplasm) of the rat brain and heart during postnatal ontogenesis. The total activity of CK in the brain and heart of newborn rats was found to be 4 and 2 times less, resp., than in those of adults. The age patterns were established in the activity of cytoplasmic (CK-1, CK-2 and CK-3) and mitochondrial (CK-4) isozymes. During the whole postnatal development the rat brain contains only one cytoplasmic isozyme, CK-1. In the heart of newborn rats, as compared with adults, the content of CK-1 and CK-2 is much higher and that of CK-3 lower. On the 12-15th day of life the range of the CK isozymes approaches that characteristic of adult animals. The activity of CK-4 was found in the brain on the 5-7th day of life and in the heart on 12-15th day. In the range of the CK isozymes in the adult brain the content of mitochondrial CK amounts to 19.3% and in the heart to 16.5%. The data obtained complement the literary ones suggesting the low level of energy-forming processes in the brain and heart cells at the early stages of the rat postnatal development.
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PMID:[Intracellular distribution of creatine kinase isoenzymes in the brains and hearts of rats at different stages of postnatal development]. 121 11

Granulocyte-colony stimulating factor (G-CSF) is a haemopoietic growth factor produced by mesenchymal cells but not T lymphocytes after stimulation with specific cytokines or mitogens. A 330 bp promoter fragment of the human G-CSF gene induced reporter gene expression in human embryonic lung fibroblasts in response to tumor necrosis factor-alpha (TNF-alpha) or interleukin-1 beta (IL-1 beta). The same promoter fragment was not active in Jurkat T cells nor did it respond to phorbol ester in either cell type. At least three distinct elements, the CK-1 sequence, a decanucleotide present in haemopoietic growth factor genes, an NF-IL-6 consensus sequence and a consensus octamer sequence, were essential in the G-CSF promoter for TNF-alpha and IL-1 beta response. Mutation of any of these sequences abolished promoter function. In contrast, mutation of two other consensus protein binding sequences, i.e. a Pu-1 site and a CK-2-like sequence, did not eliminate promoter function. Both the CK-1 and octamer sequences acted independently as TNF-alpha and IL-1 beta responsive elements upstream of a heterologous promoter. The response of the octamer sequence and the 330 bp promoter but not the CK-1 sequence was greater with IL-1 beta than TNF-alpha reflecting a similar response of the endogenous gene.
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PMID:Three essential promoter elements mediate tumour necrosis factor and interleukin-1 activation of the granulocyte-colony stimulating factor gene. 128 Sep 54

Two yeast casein kinase type-1 species of 45 kDa and 27 kDa (CK1) were purified to apparent homogeneity and used for investigation of their immunological affinity. Antisera against the two kinases were isolated; the antibody against the 45 kDa kinase did not react with the 27 kDa enzyme. The 27 kDa casein kinase was recognized only by its own antibody. The obtained data strongly suggest that the low molecular mass CK-1 is not a proteolytic product of the 45 kDa kinase species.
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PMID:The 45 kDa and 27 kDa yeast's protein kinases are not immunologically related. 144 47

Casein kinase-2 (CK-2) is a ubiquitous Ser/Thr specific protein kinase that recognizes phosphorylatable residues located upstream of acidic determinants, its consensus sequence being Ser(Thr)-Xaa-Xaa-Acidic. Here we show that the phosphotetrapeptide AcSer(P)-Ser(P)-Ser-Ser(P), which is devoid of the canonical consensus sequence, is nevertheless phosphorylated by CK-2 with rates comparable to that of typical peptide substrates Ser-Glu-Glu-Glu-Glu-Glu and Arg-Arg-Arg-Glu-Glu-Glu-Thr-Glu-Glu-Glu routinely employed for assaying CK-2 activity. The phosphopeptide AcSer(P)-Ser-Ser(P) [but not Ac-Ser-Ser(P)-Ser(P) or AcSer(P)-Ser(P)-Ser] is also phosphorylated albeit less efficiently than AcSer(P)-Ser(P)-Ser-Ser(P). Further N-terminal elongation with additional phosphoseryl residues to give the peptides AcSer(P)-Ser(P)-Ser(P)-Ser-Ser(P) and AcSer(P)-Ser(P)-Ser(P)-Ser(P)-Ser-Ser(P) does not improve but rather slightly decreases the phosphorylation efficiency by CK-2. These two peptides are conversely excellent substrates for CK-1, which does not appreciably phosphorylate either AcSer(P)-Ser-Ser(P) or AcSer-(P)-Ser(P)-Ser-Ser(P). Either individual or multiple replacement of the phosphorylated residues with glutamic acid in the peptide AcSer(P)-Ser(P)-Ser-Ser(P) drastically reduces the phosphorylation efficiency by CK-2, the phosphoseryl residue at position -2 playing an especially crucial role which cannot be surrogated by glutamyl residues.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Role of phosphorylated aminoacyl residues in generating atypical consensus sequences which are recognized by casein kinase-2 but not by casein kinase-1. 161 Aug 32

Male Sprague-Dawley rats administered with an acute sublethal dose of carbofuran (1.5 mg/kg, s.c.) developed the signs of peak hypercholinergic activity during 30-60 min. At this time, in hemidiaphragm muscle, a significant decrease in ATP (28%) and phosphocreatine (PC) (29%) occurred without concurrent change in AMP and creatine (CR). A significant decrease in the levels of total adenine nucleotides (ATP + ADP + AMP) (20%) and total creatine compounds (PC + CR) (17%) was evident. The decline in the corresponding ratios of ATP/ADP (26%), ATP/AMP (39%), and PC/CR (20%) was therefore suggestive of greater utilization of ATP and PC in response to their increased demand for high-frequency muscle fasciculations. The energy charge = ATP + 1/2 ADP/(ATP + ADP + AMP), an index of high-energy phosphate adequacy in hemidiaphragm, remained unchanged. A significant (p less than 0.01) increase in serum magnesium with no concurrent change in calcium was also evident. The observed higher activity (152%) of total CK (EC 2.7.3.2) in the serum induced by carbofuran was possibly a reflection of more than a twofold increase in CK-BB isoenzyme (CK-1) and 141% increase in CK-MM isoenzyme (CK-3), which also strengthens our findings of enhanced synthesis of ATP and PC. Increased levels of CK-MM isoenzyme in the brain (253%) and hemidiaphragm (195%); and depletion of CK-BB isoenzyme in the hemidiaphragm (0%), heart (42%), and brain (77%), and of CK-MB isoenzyme (CK-2) in the brain (4%) and hemidiaphragm (14%), appeared to be the major contributory factors leading to enhanced serum CK activity.
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PMID:Carbofuran-induced alterations (in vivo) in high-energy phosphates, creatine kinase (CK) and CK isoenzymes. 195 49

Halogeno benzimidazole and benzimidazole nucleoside analogues have been screened for inhibitory activity vs. purified plant (maize seedling) casein kinases I, IIA and IIB, and the results compared with those previously reported for some of the compounds as inhibitors of the corresponding mammalian CK-1 and CK-2 (Meggio et al. (1990) Eur. J. Biochem. 187, 89-94). One new analogue, the riboside of 5,7-dibromobenzimidazole, which is sterically constrained to the anti conformation about the glycosidic bond, and is a good inhibitor, exhibited appreciable (5-7-fold) discrimination between the type I and type II enzymes. An increase in the number of halogen substituents on the benzene ring of benzimidazole from two to three led to marked enhancement of inhibitory activity, particularly against the type II enzymes, with a decrease in Ki from 24 to 4 microM. The 2-aza analogue of 5,6-dichlorobenzimidazole, i.e. 5,6-dichlorobenzotriazole, as the free base, even more effectively discriminated between the two types of plant casein kinases, with Ki approximately 100 microM for CK-I, and Ki approximately 9 microM for CK-IIA and CK-IIB. Inhibition in all instances was competitive with respect to ATP (for CK-I), and ATP and GTP (for CK-IIA and CK-IIB). The results are compared with those for halogenated isoquinolinesulfonamide inhibitors reported by Chijiwa et al. (J. Biol. Chem. (1989) 264, 4924-4927), leading to proposals for the synthesis of potentially more effective and more discriminating inhibitors. Attention is drawn to the significant role of the halogen substituents in the mechanism(s) of action of the structurally related benzimidazole, benzotriazole and naphthalene and isoquinoline, inhibitors of protein kinases.
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PMID:Benzimidazole nucleoside analogues as inhibitors of plant (maize seedling) casein kinases. 195 29

The phosphopeptide Ser (P)-Ser(P)-Ser-(P)-Glu-Glu-Ser22-Ile-Thr, reproducing the 17-24 segment of beta-casein A2 including the seryl residue (Ser-22) which is targeted by casein kinase-1 was synthesized and used as model substrate for this enzyme. Its phosphorylation efficiency is actually higher than that of intact beta-casein (similar Vmax and 14 microM Km). Conversely the fully dephosphorylated peptide SSSEESIT is not affected by CK-1 to any detectable extent and its glutamyl derivative EEEEESIT displays a more than 50-fold higher Km and a 5-fold lower Vmax as compared to the parent phosphopeptide. The relevance of the individual phosphoseryl residues has been assessed by comparing the phosphorylation efficiencies of the phosphopeptides EESpEESIT, ESpEEESIT and SpEEEESIT: while the first is a substrate almost as good as the tris Ser (P)-peptide (Km = 62 microM), and the third one is almost as poor as EEEEESIT (Km = 1.55 mM), ESpEEESIT displays a intermediate efficiency (Km = 277 microM). These data in conjunction with the finding that the phosphopentapeptide Ser(P)-Ser(P)-Ser(P)-Ser-Ser(P), but neither Ser(P)-Ser(P)-Ser-Ser(P) nor Ser-Ser(P)-Ser(P)-Glu-Glu and Ser-Ala-Ala-Ser(P)-Ser(P), is readily phosphorylated by CK-1, support the concept that CK-1 is a phosphate directed protein kinase recognizing the Ser(P)-X-X-Ser-X and, less efficiently, the Ser(P)-X-X-X-Ser-X motifs.
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PMID:A synthetic beta-casein phosphopeptide and analogues as model substrates for casein kinase-1, a ubiquitous, phosphate directed protein kinase. 204 70

A monoclonal antibody was produced against the nuclear casein kinase II (PK-N2) isolated from rat liver. The antibody was of the IgM class, and showed immunoreactivity towards the higher molecular weight subunit (41K Da) of the protein kinase in Western blots. The antibody was equally reactive towards the PK-N2 isolated from rat ventral prostate indicating that it can recognize the enzyme from different tissues of the rat. The antibody also detected the cytosolic casein kinase II (CK-2) suggesting significant similarity of the antigenic domains in the two forms of this protein kinase. No binding was detected with the nuclear or cytosolic casein kinase I (PK-N1 and CK-1). The antibody did not inhibit the enzyme activity or directly precipitate the enzyme, but when coupled to an affinity matrix and cross-linked with dimethylpimelimidate, it was capable of removing nearly all the PK-N2 activity from solution.
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PMID:Monoclonal antibodies against nuclear casein kinase NII (PK-N2). 207 98


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