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 NRK cell clone (6m2 cells) infected with ts110 Moloney murine sarcoma virus (MuSV) produce a gag-mos protein, P85gag-mos, and a truncated gag protein of Mr 58,000d termed P58gag. The gag-mos protein is produced from a 3.5-kb mRNA whereas the gag protein is made from a 4.0-kb mRNA. It has been proposed that the 3.5-kb RNA is produced from the 4.0-kb RNA by a splicing mechanism (R. P. Junghans, E. C. Murphy, Jr., and R. B. Arlinghaus (1982) J. Mol. Biol. 161, 229-255). The results presented here provide further support for this model. The expression of the 3.5-kb RNA and the gag-mos protein increased as the temperature at which 6m2 cells were maintained was lowered from 39 to 28 degrees. This increase coincided with a decrease in both the 4.0-kb RNA and its product P58gag. The optimum temperature for syntheses of both the gag-mos mRNA and its protein was found to be 28 degrees. Consistent with the increase in the level of the gag-mos protein is the increase in the protein kinase activity associated with P85gag-mos and the degree of morphological transformation of 6m2 cells. Thus, the level of P85gag-mos within 6m2 cells is directly proportional to the degree of cell transformation and the amount of the kinase activity associated with the gag-mos protein, providing convincing evidence that P85gag-mos plays a direct role in the neoplastic transformation of these cells.
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PMID:The gag-mos hybrid protein of ts110 Moloney murine sarcoma virus: variation of gene expression with temperature. 609 31

By double indirect immunofluorescence, using primary rabbit antibodies to tubulin and guinea pig antibodies to vimentin, we have simultaneously labeled microtubules and intermediate filaments in several types of cultured normal fibroblasts. With well-spread interphase cells there was an extensive but not complete correspondence of the labeling patterns for the two filamentous structures out to the cell periphery. This correspondence existed both at a gross level, where parallel but not coincident arrays of thickly labeled strands of the two types of filaments were observed, and at a fine level, where thinly labeled strands of the two were superimposed. The results suggest that there may be some type(s) of molecular linkages between microtubules and vimentin intermediate filaments that is under metabolic control. With NRK fibroblasts infected with a temperature-sensitive mutant (LA23) of Rous sarcoma virus, cells grown at the nonpermissive temperature (39 degrees C) showed the correspondence of the distributions of the microtubules and intermediate filaments characteristic of the normal phenotype but within 1 hr after a shift to the permissive temperature (33 degrees C) there was an extensive retraction of the intermediate filaments around the cell nucleus whereas the microtubules remained dispersed into the cell periphery. These results suggest that one of the functions carried out by p60src, the protein kinase responsible for transformation by Rous sarcoma virus, may be to modify the component(s) involved in the putative linkages between microtubules and intermediate filaments in the normal cells.
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PMID:Association of microtubules and intermediate filaments in normal fibroblasts and its disruption upon transformation by a temperature-sensitive mutant of Rous sarcoma virus. 627

A nontransformed line of Chinese hamster ovary (CHO) cells (Pollard and Stanners, 1979) has been transformed by the Schmidt-Ruppin subgroup D strain of Rous sarcoma virus (SR-RSV). SR-RSV transformed CHO cells are shown to differ from spontaneously transformed cells in that the virally transformed cells are more resistant to growth inhibition or changes in cell shape by 8-Br-cyclic AMP or cholera toxin. SR-RSV transformed rat (NRK) cells also have a reduced sensitivity to growth inhibition by 8-Br-cyclic AMP. Cyclic AMP-dependent protein kinase was examined in SR-RSV transformed CHO cells, but no differences in enzyme level, activation by cyclic AMP, chromatographic behavior, or its ability to phosphorylate endogenous proteins in whole cells could be detected. It is concluded that transformation of CHO and NRK cells by SR-RSV alters the cells in a manner different from spontaneous transformation, and that this alteration does not affect cAMP-dependent protein kinase activity.
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PMID:Rous sarcoma virus transformed cells are resistant to cyclic AMP. 628 4

We developed a specific antibody to the catalytic subunit (C-subunit) of cyclic AMP-dependent protein kinase and used it to localize C-subunit in cultured cells. C-subunit antigen was purified from bovine cardiac muscle and cross-linked to hemocyanin with glutaraldehyde. Immunized goat serum showed a low titer of antibody after boosting; it was enriched 100-fold by affinity chromatography on catalytic subunit-Sepharose. The antibody immunoprecipitated C-subunit from type I and type II holoenzyme and depleted enzymatic activity from solution. At 12.5 nM antigen, 1 microgram antibody immunoprecipitated 10 ng of C-subunit. Immunoprecipitation of 35S-labeled cell extracts and 125I-antibody detection on nitrocellulose paper revealed that the antibody specifically reacts with C-subunit in Chinese hamster ovary (CHO) whole cell extracts. Using indirect immunofluorescence to localize C-subunit, we found a pattern of diffuse staining in the cytoplasm of CHO cells with little or no nuclear staining. A similar distribution of the enzyme was observed in Swiss 3T3 cells, bovine endothelial tracheal cells, human lung fibroblasts and NRK cells. Treatment of CHO cells with 8-bromo-cyclic AMP produced no change in the pattern or intensity of immunofluorescence. We conclude that the majority of C-subunit is localized in cytoplasm and that in cultured fibroblasts exposure to cyclic AMP analogues causes no apparent redistribution of catalytic subunit.
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PMID:Localization of the catalytic subunit of cyclic AMP-dependent. Protein kinase in cultured cells using a specific antibody. 675 45

Transforming growth factor beta 1 (TGF beta 1) is a cytokine capable of inhibiting or stimulating cell growth, depending on the nature of the target cell. Inhibition of cell growth by TGF beta 1 is thought to be mediated by TGF beta 1-induced changes in the expression and activity of cell cycle regulatory proteins like cyclin-dependent kinase (cdk) 2 and cdk4. Here we show that adenovirus E1A blocks growth inhibition by TGF beta 1. The activity of cdk2 was strongly inhibited by TGF beta 1 in control cells but not in E1A-expressing cells. Similarly, an early event in TGF beta 1 signaling, junB induction, was significantly reduced in E1A-expressing cells. E1A also interferes with growth stimulation of NRK cells by TGF beta 1, both in monolayer and in soft agar. In these cells, E1A also interferes with junB induction by TGF beta 1. Moreover, E1A abrogates TGF beta 1-induced production of an autocrine-acting platelet-derived growth factor-like activity. These results show that E1A can interfere with TGF beta 1-induced growth-inhibiting as well as growth-promoting signals.
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PMID:Adenovirus E1A antagonizes both negative and positive growth signals elicited by transforming growth factor beta 1. 764 36

We have investigated the levels of calmodulin protein and calmodulin mRNA species during proliferative activation of NRK cells. Cells activated to proliferate from quiescence started to replicate DNA at 15 h, reaching a maximum at 20 h after serum addition. The maximum of mitosis was observed at 24 h. Quiescent cells showed a calmodulin concentration of 1.5 ng/micrograms of protein. At 10 h after serum addition the amount of calmodulin started to increase, reaching values of 3.0 ng/micrograms of protein at 24 h. NRK cells expressed predominantly 3 species of calmodulin transcripts: the 1.7 kb from CaM I, the 1.4 kb from CaM II and the 2.3 kb from CaM III. The amount of all the 3 transcripts was low in quiescent cells and 10 h after activation the levels were already high, reaching a maximum around 20 h. At the latter time the amount of the 3 calmodulin mRNAs was 5-10-fold higher than in serum starved cells. Run-on experiments showed that at 20 h after activation the transcription rates of the 3 calmodulin genes were higher than in quiescent cells. The addition of protein kinase C inhibitors to the cultures blocked the increase of the calmodulin transcripts while inhibitors of protein kinase A did not have any effect. Moreover, the addition of submitogenic doses of phorbol 12-tetradecanoate induced the increase of all 3 calmodulin transcripts. These results indicate that protein kinase C regulates calmodulin expression when NRK cells are activated to proliferate.
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PMID:Protein kinase C regulates calmodulin expression in NRK cells activated to proliferate from quiescence. 771 38

RCR cells are NRK clones in which Raf-1 production is blocked by the expression of an antisense RNA, and consequently they are refractory to transformation by various oncogenes. In RCR cells, MAP kinases (ERK1 and ERK2) were activated to an extent and in a time course similar to those of the original NRK cells, irrespective of whether the stimulus was oncogenic or non-oncogenic. Moreover, there was no significant elevation of ERK activities in oncogene-transformed NRK cells. These results indicate that Raf-1 kinase is not the major upstream activator of ERK's in NRK cells and that neither ERK1 nor ERK2 are likely to mediate oncogenic signals from Raf-1 kinase.
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PMID:Raf-1 is not a major upstream regulator of MAP kinases in rat fibroblasts. 826 40

The rat fibroblast NRK cells are transformed reversibly by a combination of growth factors. When stimulated with serum, NRK cells rely on cyclin-dependent kinase 4 (Cdk4) for their S phase entry. However, when stimulated with serum containing oncogenic growth factors, they come to rely on either Cdk4 or Cdk6, and their S phase entry cannot be blocked unless both Cdk4 and Cdk6 are immunodepleted. Such change of dependence does not occur in the NRK cell mutants defective in an oncogenic signal pathway and, therefore, deficient in anchorage-independent cell cycle start ability, correlating Cdk6 dependence with this remarkable, cancer-associated phenotype. However, both Cdk4 and Cdk6 are activated upon serum stimulation, and neither the amounts of Cdk6, Cdk4, cyclin D1, and cyclin-dependent kinase inhibitors nor the activities or subcellular localization of Cdk6 and Cdk4 are significantly influenced by oncogenic stimulation. Thus, oncogenic stimulation invokes Cdk6 to participate in a critical step of the cell cycle start in a rat fibroblast, but by a mechanism seemingly unrelated to the regulation of the kinase. Given that many hematopoietic cells employ predominantly Cdk6 for the cell cycle start and perform anchorage-independent growth by nature, our results raise the possibility that the oncogenic stimulation-induced anchorage-independent cell cycle start of NRK is elicited by a mechanism similar to the one used for hematopoietic cell proliferation.
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PMID:Oncogenic stimulation recruits cyclin-dependent kinase in the cell cycle start in rat fibroblast. 1055 97

The c-Jun N-terminal kinase (JNK) signaling pathway plays a crucial role in cellular responses stimulated by stress-inducing agents and proinflammatory cytokines. The group I germinal center kinase family members selectively activate the JNK pathway. In this study, we have isolated a mouse cDNA encoding a protein kinase homologous to Nck-interacting kinase (NIK), a member of the group I germinal center kinase family. This protein kinase is expressed during the late stages of embryogenesis, but not in adult tissues, and thus named NESK (NIK-like embryo-specific kinase). NESK selectively activated the JNK pathway when overexpressed in HEK 293 cells but did not stimulate the p38 kinase or extracellular signal-regulated kinase (ERK) pathways. NESK-induced JNK activation was inhibited by the dominant negative mutants of MEKK1 and MKK4. Tumor necrosis factor (TNF)-alpha or TNF receptor-associated factor 2 (TRAF2) stimulated the NESK activity. Furthermore, the dominant negative NESK mutant inhibited the JNK activation induced by TNF-alpha or TRAF2. These results suggest that NESK, a novel activator of the JNK pathway, functions in coupling TRAF2 to the MEKK1 --> MKK4 --> JNK kinase cascade during the late stages of mammalian embryogenesis.
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PMID:NESK, a member of the germinal center kinase family that activates the c-Jun N-terminal kinase pathway and is expressed during the late stages of embryogenesis. 1080 98

To test the hypothesis that there is cross-talk between the protein kinase C (PKC) and protein kinase A (PKA) pathways in the regulation of the Na,K-ATPase, we measured its phosphorylation in mammalian cell cultures. Phosphorylation of the PKC site, Ser-18, appeared to be due to the activation of the alpha isoform of the kinase. In NRK-52E and L6 cells, this phosphorylation was reduced by prior activation of a cAMP-dependent signaling pathway with forskolin. In principle this would be consistent with direct interaction between the two phosphorylation sites, but further investigation suggested a more indirect mechanism. First, phosphorylation of Ser-938, the PKA site, could not be detected despite the presence of active PKA. Second, there was a major reduction in the phosphorylation of unrelated phosphoproteins as a consequence of elevation of cAMP, suggesting generalized reduction of kinase activity or activation of phosphatase activity. In NRK-52E and L6, phosphorylation of the Na, K-ATPase at Ser-18 paralleled this global change. In C6 cells, in contrast, there was no cAMP effect on Na,K-ATPase phosphorylation at Ser-18 and no global cAMP effect on other phosphoproteins. The cross-talk is evidently mediated by events occurring at the cellular level.
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PMID:Interaction of protein kinase C and cAMP-dependent pathways in the phosphorylation of the Na,K-ATPase. 1094 Mar 9


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