Relevant bibliographies by topics / Calmodulin-dependent protein kinase II

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Calmodulin-dependent protein kinase II'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Calmodulin-dependent protein kinase II"

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Kelly, Paul T. "Calmodulin-dependent protein kinase II." Molecular Neurobiology 5, no. 2-4 (June 1991): 153–77. http://dx.doi.org/10.1007/bf02935544.

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Fujisawa, Hitoshi. "Calmodulin-dependent protein kinase II." BioEssays 12, no. 1 (January 1990): 27–29. http://dx.doi.org/10.1002/bies.950120106.

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Moriya, M., C. Katagiri, M. Ikebe, and K. Yagi. "Immunohistochemical detection of calmodulin and calmodulin-dependent protein kinase II in the mouse testis." Zygote 8, no. 4 (November 2000): 303–14. http://dx.doi.org/10.1017/s0967199400001106.

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We reported previously that in mouse testis calmodulin-dependent protein phosphatase (calcineurin) is localised in the nuclei of round and elongating spermatids (Cell Tissue Res. 1995; 281: 273-81). In this study, we studied the immunohistochemical localisation of calcium/calmodulin-dependent protein kinase (CaM kinase II) using antibodies against CaM kinase IIγ from chicken gizzard and specific antibodies raised against the amino acid sequence Ileu480–Ala493 of this enzyme, and compared it with the distribution of calmodulin. Indirect immunofluorescence was most concentrated in early spermatocytes and localised in the outermost layer of seminiferous tubules where the calmodulin level was relatively low. Measurements of immuno-gold particle densities on electron micrographs revealed that CaM kinase II is transiently increased in the nucleus of zygotene spermatocytes. These observations suggest the involvement of CaM kinase II in the meiotic chromosomal pairing process. An extremely high concentration of calmodulin in spermatogenic cells undergoing meiosis may not be directly related to activation of calmodulin-dependent kinases and phosphatases.
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Griffith, L. C. "Calcium/Calmodulin-Dependent Protein Kinase II: An Unforgettable Kinase." Journal of Neuroscience 24, no. 39 (September 29, 2004): 8391–93. http://dx.doi.org/10.1523/jneurosci.2888-04.2004.

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COLBRAN, Roger J. "Targeting of calcium/calmodulin-dependent protein kinase II." Biochemical Journal 378, no. 1 (February 15, 2004): 1–16. http://dx.doi.org/10.1042/bj20031547.

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Calcium/calmodulin-dependent protein kinase II (CaMKII) has diverse roles in virtually all cell types and it is regulated by a plethora of mechanisms. Local changes in Ca2+ concentration drive calmodulin binding and CaMKII activation. Activity is controlled further by autophosphorylation at multiple sites, which can generate an autonomously active form of the kinase (Thr286) or can block Ca2+/calmodulin binding (Thr305/306). The regulated actions of protein phosphatases at these sites also modulate downstream signalling from CaMKII. In addition, CaMKII targeting to specific subcellular microdomains appears to be necessary to account for the known signalling specificity, and targeting is regulated by Ca2+/calmodulin and autophosphorylation. The present review focuses on recent studies revealing the diversity of CaMKII interactions with proteins localized to neuronal dendrites. Interactions with various subunits of the NMDA (N-methyl-d-aspartate) subtype of glutamate receptor have attracted the most attention, but binding of CaMKII to cytoskeletal and several other regulatory proteins has also been reported. Recent reports describing the molecular basis of each interaction and their potential role in the normal regulation of synaptic transmission and in pathological situations are discussed. These studies have revealed fundamental regulatory mechanisms that are probably important for controlling CaMKII functions in many cell types.
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Kameshita, Isamu, Atsuhiko Ishida, and Hitoshi Fujisawa. "Phosphorylation and activation of Ca2+ /calmodulin-dependent protein kinase phosphatase by Ca2+ /calmodulin-dependent protein kinase II." FEBS Letters 456, no. 2 (August 4, 1999): 249–52. http://dx.doi.org/10.1016/s0014-5793(99)00958-8.

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Luise, M., C. Presotto, L. Senter, R. Betto, S. Ceoldo, S. Furlan, S. Salvatori, R. A. Sabbadini, and G. Salviati. "Dystrophin is phosphorylated by endogenous protein kinases." Biochemical Journal 293, no. 1 (July 1, 1993): 243–47. http://dx.doi.org/10.1042/bj2930243.

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Dystrophin, the protein coded by the gene missing in Duchenne muscular dystrophy, is assumed to be a component of the membrane cytoskeleton of skeletal muscle. Like other cytoskeletal proteins in different cell types, dystrophin bound to sarcolemma membranes was found to be phosphorylated by endogenous protein kinases. The phosphorylation of dystrophin was activated by cyclic AMP, cyclic GMP, calcium and calmodulin, and was inhibited by cyclic AMP-dependent protein kinase peptide inhibitor, mastoparan and heparin. These results suggest that membrane-bound dystrophin is a substrate of endogenous cyclic AMP- and cyclic GMP-dependent protein kinases, calcium/calmodulin-dependent kinase and casein kinase II. The possibility that dystrophin could be phosphorylated by protein kinase C is suggested by the inhibition of phosphorylation by staurosporin. On the other hand dystrophin seems not to be a substrate for protein tyrosine kinases, as shown by the lack of reaction of phosphorylated dystrophin with a monoclonal antiphosphotyrosine antibody. Sequence analysis indicates that dystrophin contains seven potential phosphorylation sites for cyclic AMP- and cyclic GMP-dependent protein kinases (all localized in the central rod domain of the molecule) as well as several sites for protein kinase C and casein kinase II. Interestingly, potential sites of phosphorylation by protein kinase C and casein kinase II are located in the proximity of the actin-binding site. These results suggest, by analogy with what has been demonstrated in the case of other cytoskeletal proteins, that the phosphorylation of dystrophin by endogenous protein kinases may modulate both self assembly and interaction of dystrophin with other cytoskeletal proteins in vivo.
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Mayer, P., M. Möhlig, U. Seidler, H. Rochlitz, M. Fährmann, H. Schatz, H. Hidaka, and A. Pfeiffer. "Characterization of γ- and δ-subunits of Ca2+/calmodulin-dependent protein kinase II in rat gastric mucosal cell populations." Biochemical Journal 297, no. 1 (January 1, 1994): 157–62. http://dx.doi.org/10.1042/bj2970157.

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We searched for the occurrence of a Ca2+/calmodulin-dependent protein kinase in rat gastric cell types as a likely member in the chain of gastrin- and muscarinic-receptor-mediated signal transmission. A Ca(2+)- and calmodulin-dependent phosphorylation of major 50, 60 and 100 kDa substrates was observed in parietal cell cytosol and a major 60 and 61 kDa protein doublet was found to bind 125I-calmodulin in 125I-calmodulin-gel overlays. A specific substrate of the multifunctional Ca2+/calmodulin-dependent protein kinase II, autocamtide II, was phosphorylated in a calmodulin-dependent manner. The specific inhibitor of this enzyme, KN-62, antagonized protein kinase activity. RNA extracted from gastric mucosal cells was shown to contain sequences of the gamma- and delta- but not alpha- and beta-subunits of the calmodulin-dependent kinase II, and mRNA of both subtypes was demonstrated in highly purified parietal, chief and mucous cells. A calmodulin-dependent kinase II composed of gamma- and delta-subunits is a likely mediator of Ca(2+)-dependent signal transmission in these populations of gastric cells.
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Kato, M., M. Hagiwara, Y. Nimura, S. Shionoya, and H. Hidaka. "Purification and characterization of calcium-calmodulin kinase II from human parathyroid glands." Journal of Endocrinology 131, no. 1 (October 1991): 155–62. http://dx.doi.org/10.1677/joe.0.1310155.

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ABSTRACT Calmodulin has been identified in parathyroid cells and is thought to play an important role in the production or secretion of parathyroid hormone. However, a detailed investigation of calmodulinbinding proteins in parathyroid glands has not been conducted. In this study, we attempted to determine the presence of calmodulin-binding protein in human parathyroid adenoma by affinity chromatography. The eluted protein from a calmodulin-coupled Sepharose 4B column with EGTA was analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis which revealed a major protein band of Mr 50 000. A Ca2+/calmodulin-dependent protein kinase activity was detected at the protein peak using dephosphorylated casein as a substrate. The 50 kDa band was identified as calcium/calmodulin-dependent protein kinase II (CaM-kinase II) by immunoblotting. The substrate specificity, pH dependency and affinity for calmodulin of this enzyme were identical to those of CaM-kinase II from rat brain. Also, the kinase activity was sensitive to KN-62, a specific inhibitor of CaM-kinase II. In total, 0·48 mg of this kinase was purified from 3 g human parathyroid adenoma. Journal of Endocrinology (1991) 131, 155–162
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NEVALAINEN, Leena T., Takashi AOYAMA, Mitsuhiko IKURA, Anna CRIVICI, Hong YAN, Nam-Hai CHUA, and Angus C. NAIRN. "Characterization of novel calmodulin-binding peptides with distinct inhibitory effects on calmodulin-dependent enzymes." Biochemical Journal 321, no. 1 (January 1, 1997): 107–15. http://dx.doi.org/10.1042/bj3210107.

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We describe the isolation and interaction with calmodulin (CaM) of two 10-amino-acid peptides (termed peptides 1 and 2; AWDTVRISFG and AWPSLQAIRG respectively) derived from a phage random peptide display library. Both peptides are shorter than previously described CaM-binding peptides and lack certain features found in the sequences of CaM-binding domains present in CaM-activated enzymes. However, 1H NMR spectroscopy and fluorimetry indicate that both peptides interact with CaM in the presence of Ca2+. The two peptides differentially inhibited CaM-dependent kinases I and II (CaM kinases I and II) but did not affect CaM-dependent phosphodiesterase. Peptide 1 inhibited CaM kinase I but not CaM kinase II, whereas peptide 2 inhibited CaM kinase II, but only partially inhibited CaM kinase I at a more than 10-fold higher concentration. Peptide 1 also inhibited a plant calcium-dependent protein kinase, whereas peptide 2 did not. The ability of peptides 1 and 2 to differentially inhibit CaM-dependent kinases and CaM-dependent phosphodiesterase suggests that they may bind to distinct regions of CaM that are specifically responsible for activation of different CaM-dependent enzymes.
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Dissertations / Theses on the topic "Calmodulin-dependent protein kinase II"

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Whelan, Helen A. "Calmodulin Dependent Protein Kinase II - A Sulfhydryl Chemistry Study /." The Ohio State University, 1995. http://rave.ohiolink.edu/etdc/view?acc_num=osu148793151262033.

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Saeedi, Shahriar. "Targeting of calcium/calmodulin-dependent protein kinase II to membranes." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2001. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/MQ57789.pdf.

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Tzortzopoulos, Athanasios. "Activation mechanism of a-Ca²+/calmodulin-dependent protein kinase II." Thesis, St George's, University of London, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.252397.

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Saeedi, Shahriar Carleton University Dissertation Biology. "Targeting of calcium/calmodulin-dependent protein kinase II to membranes." Ottawa, 2000.

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Jama, Abdirahman Mohamud. "Functional regulation of kisspeptin receptor by calmodulin and Ca2+/calmodulin-dependent protein kinase II." Thesis, University of Edinburgh, 2015. http://hdl.handle.net/1842/15914.

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The kisspeptin receptor (KISS1R), functioning as a metastasis suppressor and gatekeeper of GnRH neurons, is a potent activator of intracellular Ca2+. The surge in cytoplasmic Ca2+ mediates the exocytosis of GnRH from GnRH neurons. However, the regulatory processes which enable KISS1R to sense increasing intracellular Ca2+ and avoid Ca2+ excitotoxicity via a signalling off-switch mechanism remain unclear. This thesis provides evidence for the interaction between KISS1R and the Ca2+ regulated proteins of calmodulin (CaM), and αCa2+/CaM-dependent-protein kinase II (α-CaMKII). Binding of CaM to KISS1R was shown with three independent approaches. Firstly, cell-free spectrofluorimeter assays showed that CaM selectively binds to intracellular loop (IL) 2 and IL3 of the KISS1R. Secondly, KISS1R co-immunoprecipitation experiments identified ligand/Ca2+-dependent binding of KISS1R to HEK-293 endogenous CaM. Thirdly, confocal experiments showed CFPCaM co-localises with YFP-KISS1R. The functional relevance of CaM binding was examined with alanine substitution of critical residues of the CaM binding motifs in IL2 and IL3 of KISS1R. This approach revealed that the receptor activity (relative maximum responsiveness) was increased in the mutated residues of the juxtamembrane regions of IL3 and the N-terminus of IL2 relative to wild-type KISS1R. The Ca2+/CaM regulated αCaMKII was also found to interact with KISS1R by selectively phosphorylating T77 of IL1. Phosphomimetic mutations of T77 into E or D created a receptor that was unable to elicit inositol phosphate production upon ligand stimulation. Finally, in vivo studies using ovariectomised rats that were intracerebroventricularly administered with a cell-permeable αCaMKII inhibitor augmented the effects of kisspeptin ligand stimulation of plasma luteinizing hormone levels. Taken together, this thesis demonstrates that the KISS1R-G protein coupling is regulated by Ca2+-dependent CaM binding and αCaMKII-mediated KISS1R phosphorylation.
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He, Beixin Julie. "Calcium and calmodulin dependent protein kinase II hyperactivity in cardiac remodeling." Diss., University of Iowa, 2012. https://ir.uiowa.edu/etd/2516.

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The multifunctional calcium and calmodulin dependent protein kinase II (CaMKII) is implicated in both animal models and human forms of cardiovascular disease. CaMKII is activated by elevated neurohormonal signals including enhanced â-adrenergic stimulation and angiotensin II signaling, whereas CaMKII inhibition is cardioprotective from these pathologic triggers. In addition to â-blockers and angiotensin II inhibitors, aldosterone antagonist drugs are the third and most recent class of pharmacologic agents comprising the frontline therapy for heart disease patients. Here, I show that CaMKII activation is important for cardiac aldosterone signaling in the post-myocardial infarction (MI) mouse model. Aldosterone infusion to MI mice increases cardiac rupture, a lethal and nearly untreatable clinical problem. CaMKII inhibition protects from aldosterone enhanced post-MI rupture. We previously reported microarray analysis of genes upregulated after MI but downregulated in the presence of cardiac CaMKII inhibition. Surprisingly, a number of these genes are involved in extracellular matrix remodeling. Here, I validated the microarray findings for matrix metalloproteinase 9 (MMP9), an extracellular matrix remodeling enzyme known to contribute to the rupture phenotype. My results support a sequence where aldosterone infusion after MI recruits NADPH oxidase-derived reactive oxygen species to enhance CaMKII oxidation and subsequent myocyte enhancer factor 2 driven increases in MMP9 expression in myocytes. I found that oxidative activation of CaMKII is critical for this rupture phenotype through a new transgenic mouse model that overexpresses methionine sulfoxide reductase A, which modulates CaMKII oxidation and therefore activation. These results implicate CaMKII activation in cardiac aldosterone signaling and reinforce the importance of CaMKII hyperactivity in acute cardiac remodeling after MI. Overall, this work supports myocardial CaMKII as a novel mediator of cardiac aldosterone stimulation of post-MI matrix remodeling and suggests potential efficacy for molecularly targeted anti-oxidant therapy in the treatment of patients after acute MI.
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Kwiatkowski, Ann Phyllis. "Structure, function, and regulation of type II calmodulin dependent protein kinase /." The Ohio State University, 1988. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487596807822769.

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Takeuchi-Suzuki, Erika. "Structure, function, and regulation of type II calmodulin-dependent protein kinase /." The Ohio State University, 1993. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487846885779386.

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Choo, Hyeran. "Ca²⁺/calmodulin-dependent protein kinase II regulates the growth of human osteosarcoma cells in vivo." Thesis, Birmingham, Ala. : University of Alabama at Birmingham, 2007. http://www.mhsl.uab.edu/dt/2007m/choo.pdf.

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Zhou, Zhihong Lucy. "Molecular cloning and characterization of novel isoforms of calmodulin-dependent protein kinase II." Case Western Reserve University School of Graduate Studies / OhioLINK, 1995. http://rave.ohiolink.edu/etdc/view?acc_num=case1057945686.

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Books on the topic "Calmodulin-dependent protein kinase II"

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Asher, Valerie Anne. Protein phosphorylation and dephosphorylation in the parietal cell: The role of the regulatory subunit of type II cAMP-dependent protein kinase in histamine-stimulated acid secretion. [New Haven: s.n.], 1990.

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Means, Anthony R. Calcium regulation of cellular function. New York: Raven Press, 1995.

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Schizophrenia: Elevated mRNA for calcium/calmodulin-dependent protein kinase II[Beta] in frontal cortex. Ottawa: National Library of Canada, 2001.

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Stevens, Ilse. Identification of Cyk, a Cyclin B2 Kinase As a Novel Calcium, Calmodulin-Dependent Protein Kinase II and Its Role During Xenopus Laevis Oocyte. Coronet Books Inc, 1999.

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Wang, Zengquan. Molecular and biochemical aspects of calmodulin and calmodulin-dependent protein kinase in signal transduction in plants. 1991.

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D, Takezawa, Poovaiah B. W, and United States. National Aeronautics and Space Administration., eds. Chimeric plant calcium/calmodulin-dependent protein kinase gene with a neural visinin-like calcium-binding domain. [Washington, DC: National Aeronautics and Space Administration, 1995.

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Book chapters on the topic "Calmodulin-dependent protein kinase II"

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Coultrap, Steven J., and K. Ulrich Bayer. "Ca2+/Calmodulin-Dependent Protein Kinase II (CaMKII)." In Protein Kinase Technologies, 49–72. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-824-5_4.

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Soderling, Thomas R. "Calcium/calmodulin-dependent protein kinase II: role in learning and memory." In Reversible Protein Phosphorylation in Cell Regulation, 93–101. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2600-1_8.

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Maier, Lars S. "Ca2+/Calmodulin-Dependent Protein Kinase II (CaMKII) in the Heart." In Advances in Experimental Medicine and Biology, 685–702. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-2888-2_30.

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Okamoto, Hiroshi, and Kazuhisa Ichikawa. "Autophosphorylation Versus Dephosphorylation of Ca2+/Calmodulin-Dependent Protein Kinase II." In Computational Neuroscience, 23–28. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4757-9800-5_5.

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House, Suzanne J., Melissa M. Zachar, Roman G. Ginnan, Dee Van Riper, and Harold A. Singer. "Ca2+/Calmodulin-Dependent Protein Kinase II Signaling in Vascular Smooth Muscle." In Signal Transduction in the Cardiovascular System in Health and Disease, 339–55. Boston, MA: Springer US, 2008. http://dx.doi.org/10.1007/978-0-387-09552-3_18.

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Fujimoto, K., M. Sakurai, and S. Katoh. "Determination of Residues of Sepiapterin Reductase Phosphorylated by Ca2+/Calmodulin-Dependent Protein Kinase II." In Chemistry and Biology of Pteridines and Folates, 181–85. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4615-0945-5_30.

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Urquidi, Virginia, and Stephen J. H. Ashcroft. "Molecular Cloning of the cDNA Encoding β-Cell Calcium/Calmodulin-Dependent Protein Kinase II." In Advances in Experimental Medicine and Biology, 91–96. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4899-1819-2_12.

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Poovaiah, B. W., A. S. N. Reddy, G. An, Y. J. Choi, and Z. Q. Wang. "Calmodulin gene expression and Ca2+/calmodulindependent protein kinase II in plants." In Progress in Plant Growth Regulation, 691–702. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2458-4_84.

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Ohba, Takashi, Yasutaka Ohta, Kohji Miyazaki, Hitoshi Okamura, and Eishichi Miyamoto. "Fetal Calf Serum: Eliciting Phosphorylation of Ca++/Calmodulin-Dependent Protein Kinase II in Cultured Rat Granulosa Cells." In Signaling Mechanisms and Gene Expression in the Ovary, 218–24. New York, NY: Springer New York, 1991. http://dx.doi.org/10.1007/978-1-4612-3200-1_20.

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Benter, Ibrahim F., Jasbir S. Juggi, and Saghir Akhtar. "Role of Ras/GTPase and Calcium/Calmodulin-dependent Protein Kinase II in the Signal Transduction Mechanisms Involved in Hyperthermic Preconditioning." In Pathophysiology of Cardiovascular Disease, 101–7. Boston, MA: Springer US, 2004. http://dx.doi.org/10.1007/978-1-4615-0453-5_8.

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Conference papers on the topic "Calmodulin-dependent protein kinase II"

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Liu, Huanling, Kuanquan Wang, Jieyun Bai, Suyu Dong, and Henggui Zhang. "Calcium Calmodulin Dependent Protein Kinase II (CaMKII) Contribute to Arrhythmias after Acidosis:A Simulation Study." In 2016 Computing in Cardiology Conference. Computing in Cardiology, 2016. http://dx.doi.org/10.22489/cinc.2016.274-246.

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Wong, Maria P., Jing Liu, Zhi-Jie Xiao, Si-Qi Wang, and Vicky Pc Tin. "Abstract 3352: Calcium/calmodulin-dependent protein kinase II alpha (CaMK2A) regulates the tumor initiating cell phenotype through SOX2 expression and modulates treatment response to anti-cancer drugs in lung adenocarcinoma." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-3352.

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de Chaffov de Courcelles, D., F. De Clerck, and P. Roevens. "EVALUATION OF THE PROPOSED FUNCTIONS OF PROTEIN KINASE C IN PLATELET SIGNAL TRANSDUCTION BY THE USE OF A DIACYLGLYCEROL KINASE INHIBITOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644632.

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Protein kinase C is suggested to play a major role in propagation as well as in termination of excitatory signal transduction in the platelet. Most of its properties were discovered by the use of synthetic diacylglycerol analogs or phorbol esters that directly stimulate protein kinase C. It is, however, unknown to what extent activation of the protein kinase C by these exogenously added compounds can be compared to that after receptor activation. To evaluate the role of protein kinase C in excitatory signal transduction, we transiently elevated the endogenous diacylglycerol level after receptor activation by the use of a diacylglycerol kinase inhibitor (R 59 949). On addition of the agonist vasopressin to platelets prelabeled with [32P] orthophosphate, 32P-phosphatidic acid (PA) formation was inhibited by R 59 949 in a dose-dependent manner (IC50 α 10−6 M). Vasopressin induced formation of 32P-phosphatidylinositol-4’-phosphate (PIP) and the phosphorylation of the 40 k Da protein (major substrate of the protein kinase C) were increased in the presence of the compound. In platelets prelabeled with [3H]-inositol, the agonist-induced formation of all the water-soluble inositol phosphates was inhibited in the presence of the diacylglycerol kinase inhibitor and Li+. Vasopressin induced increase in intracellular Ca2+ was lower in the presence of R 59 949. The platelet shape change induced by a threshold concentration of vasopressin was reduced by the compound. By contrast, the rate and the maximum of the first-wave aggregation was enhanced in the presence of R 59 949.These data evidence that protein kinase C, stimulated by endogenously generated diacylglycerol after receptor activation, plays a major inhibitory role on the primary steps of signal transduction since its activation reduces i) phospholipase C activity and ii) the increase in intracellular Ca2+ and the concomitant shape change reaction. The inhibitory role of protein kinase C on signal transduction is largely independent of its stimulatory role on platelet aggregation. Our data further confirm that stimulation of protein kinase C induces the formation of PIP but questions the role of the kinase in the breakdown process of inositoltrisphosphate.
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Sakon, M., Y. Uemura, K. Suga, T. Tsujinaka, J. Kambayashi, and T. Mori. "STUDIES ON PHOSPHATASES IN HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644494.

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Activation of platelets by various agonists has been ascribed to be associated with phosphorylation and dephosphorylation of specific proteins such as 20K and 47K polypeptide. Although protein kinases such as myosin light chain kinase and C kinase have been extensively studied, little information is currently available on platelet phosphatases, which may play a crucial role in the regulation of stimulus-linked protein phosphorylation. Thereby, the present study was conducted to know some characters of platelet phosphatases. Glycerol loaded platelets prepared from human platelet concentrates were subjected to osmotic lysis in 20 mM HEPES-NaOH buffer containing 5 mM EDTA, 0.5 mM dithio-threitol and various protease inhibitors and a soluble fraction was obtained by centrifugation, The activity of phosphatase was assayed at pH 7.35, using paranitrophenylphosphate as a substrate. Leupeptin and EDTA were added to the reaction mixture to avoid proteolytic attack to the enzyme. The neutral phosphatase was partially purified from the soluble fraction by a combination of ammonium sulfate fractionation and column chromatographies. Five distinct peaks with neutral phosphatase activity were obtained by a linear gradient elution ( 0−0.5 M KCl ) in DEAE Sepharose CL-6B of 0−60 % ammonium sulfate precipitate. The phosphatase activity of one peak eluted at 0.2M KCl was maximum at pH below 6, which was considered to be acid phosphatase, and the remaining four peaks' optimal pH was between 7.0−7.5. These four peaks were termed as PH-I (passed through fraction), PH-II (0.1M KCl), PH-III (0.25M KCl) and PH-IV (0.3M KCl). The respective peak was eluted as a single peak on Ultrigel AcA 34 and the molecular weight was estmated as follows; I-55K, II-40K, III-55K, IV-37K. PH-I − II were active in the presnce of EDTA and were not affect ed by divalent cations (Mg++ , Mn++ , Ca++ ) , whereas PH-III was highly dependent upon Mg++. The activity of PH-IV was completely dependent on Mn++. From these observations, the following conclusions were obtained; (1) Human platelets contain four species of neutral phosphatases, in addition to acid phosphatase. (2) Each neutral phosphatase is distincive by molecular weight and requirement of divalent cations.
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Ming Wu and Douglas A. Lawrence. "Monotonicity and bistability of calcium/calmodulin-dependent protein kinase-phosphatase activation." In 2010 American Control Conference (ACC 2010). IEEE, 2010. http://dx.doi.org/10.1109/acc.2010.5531229.

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Gocher, Angela M., Gissou Azabdaftari, and Arthur M. Edelman. "Abstract A12: Regulation of ovarian cancer OVCAR-3 cell proliferation and viability by calcium/calmodulin-dependent protein kinase kinase 2." In Abstracts: AACR Special Conference on Advances in Ovarian Cancer Research: From Concept to Clinic; September 18-21, 2013; Miami, FL. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1078-0432.ovca13-a12.

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Gocher, Angela M., Thomas F. Franke, Gissou Azabdaftari, Loukia G. Karacosta, and Arthur M. Edelman. "Abstract B13: Regulation of Akt activity, cell proliferation, and viability in ovarian cancer cells by calcium/calmodulin-dependent protein kinase kinase 2." In Abstracts: AACR Special Conference: Targeting the PI3K-mTOR Network in Cancer; September 14-17, 2014; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-8514.pi3k14-b13.

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Daniel, J. L., and M. Rigmaiden. "Evidence for Ca2+-independent phosphorylation of human platelet myosin." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644527.

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Phosphorylation of platelet myosin is thought to be required for activation of the contractile events occurring during platelet activation. At present the only known mechanism for Onitiating myosin phosphorylation is through a Ca2+-calmodulin-dependent activation of myosin light chain kinase. However, our previous studies using the fluorescent Ca2+-indicator quin2 indicated that both platelet shape change and myosin phosphorylation could be induced in an EGTA-containing media in the absence of a measurable change in cytosolic free Ca2+ concentration (Hallam, Daniel, Kendrick-Jones & Rink. Biochem. J. 232 (1985) 373). In order to confirm this finding, we fyave investigated the regulation of myosin phosphorylation usin^+a preparation of electrically-permeabilized platelets and Ca2+ buffers to control the internal Ca2+ concentration. Fifty percent myosin phosphorylation was obtained at 700 nM Ca2+. When thrombin (5 U/ml) was added to this system, this curve shifted both to the left and upward; 50% myosin phosphorylation was obtained at 400 nM Ca2+.A synthetic inhibitor of protein kinase C, H7, had no effect on myosin phosphorylation in the absence of agonist but did inhibit the thrombin-induced shift to left suggesting that protein kinase C may modulate myosin phosphorylation. We also compared the effects of H7 agonist-induced myosin phosphorylation and shape change in control and an quin2 loaded platelets. Comparable inhibition of both phosphorylation and the rate of shape change was observed with both quin2 and H7. Addition of H7 to quin2-loaded platelets resulted in complete inhibition of both agonist-induced shape change and myosin phosphorylation. These results indicate that both protein kinase C and Ca2+-dependent reactions are involved in complete expression of myosin phosphorylation in human platelets.
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Wu, Hsien-Ming, Angel Chao, Tzu-Hao Wang, Hsin-Shih Wang, Hong-Yuan Huang, Chyi-Long Lee, Yung-Kuei Soong, and Peter C. K. Leung. "Abstract 3018: Gonadotropin-releasing hormone type II (GnRH-II) agonist regulates the invasiveness of endometrial cancer cells through GnRH-I receptor and mitogen-activated protein kinases (MAPKs)-dependent activation of matrix metalloproteinase (MMP)-2." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3018.

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SIMON, M. F., H. CHAP, and L. DOUSTE-BLAZY. "EFFECTS OF SIN 1 ON PLATELET ACTIVATION INDUCED BY THROMBIN IN HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643423.

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The mechanism of platelet activation is well known. The interaction of agonist such as thrombin, on specific membrane receptor induces phosphatidylinositol-specific phospholipase C activation, with a concomitant formation of two second messengers (from PIP2): inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). IP3 is able to induce a rapid discharge of Ca2+ from internal stores and Ca2+ influx through plasma membrane by unidentified Ca2+ channels linked to receptor activation. The increase of cytoplasmic free calcium concentration leads to the activation of the calcium calmodulin dependent myosine light chain kinase which phosphoryla-tes 20 kD proteins (myosine light chain). DAG is a potent activator of protein kinase C, which phosphorylates 40 kD proteins. These different pathways act in synergism.Sin 1 is a platelet aggregating inhibitor. This compound is an active metabolite of molsidomine, which activates platelet guany-late cyclase, inducing a rapid rise in cyclic GMP level. The precise role of cyclic GMP in platelet activation is not yet known. In order to study the mechanism of action of this drug, we tried to determine the effect of Sin 1 on the different steps described above. We measured Ca2+ fluxes and phospholipase C activation in thrombin (0,5 U/ml) stimulated platelets in the presence of different doses of Sin 1 (10™7-10™3M). Serotonin secretion was inhibited by 30 % with Sin 1 (10™4M-10™5m). A parallel inhibition of phospholipase C was detected by measurement of [32P)-PA level. Platelets loaded with Quin 2 and stimulated by thrombin showed a 70 % inhibition of external Ca2+ influx as soon as a concentration of 10™7M of Sin 1 was added. A study on platelet loaded with [45Ca2+) and Quin 2 confirmed these results. On the contrary, discharge of internal Ca2+ store seemed to be unaffected.In conclusion, the major effect of Sin 1 on platelet phospholipase C pathway is an inhibition of Ca2+ influx through plasma membrane. Some further experiments are necessary to shown whether this inhibition is correlated with cyclic GMP formation (the major effect of Sin 1) and try to establish a relation between this inhibition and that exerted on phospholipase C.Sin 1 was a generous gift of Hoechst.
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