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

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Published: 4 June 2021
Last updated: 1 February 2022

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Kato, M., M. Hagiwara, and H. Hidaka. "Identification of a 80 kDa calmodulin-binding protein as a new Ca2+/calmodulin-dependent kinase by renaturation blotting assay (RBA)." Biochemical Journal 281, no. 2 (January 15, 1992): 339–42. http://dx.doi.org/10.1042/bj2810339.

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We surveyed rabbit brain cytosol for a new Ca2+/calmodulin (CaM)-dependent kinase. The renaturation blotting assay (RBA) exploits the ability of blotted SDS-denatured proteins to regain enzymic activity after guanidine treatment. Using RBA, we found that the eluate of rabbit brain cytosol from a CaM affinity column contains at least four electrophoretically distinct protein kinase bands which were autophosphorylated in a Ca2+/CaM-dependent manner. The 49 kDa band and the 60 kDa band were alpha and beta subunit of CaM kinase II, and the 42 kDa band was presumed to be CaM kinase I, but the 80 kDa band could not be attributed to any reported Ca2+/CaM-dependent protein kinases. The 80 kDa protein kinase was isolated by three-step chromatography. We examined the phosphorylation of exogenous substrates by 80 kDa protein kinase, and histone IIIs and myosin light chain were phosphorylated in a Ca2+/CaM-dependent manner. W-7, a specific inhibitor for calmodulin, inhibited this kinase activity, but KN-62, a specific inhibitor for CaM kinase II, had no effect on this protein kinase activity. Autoradiography using boiled rabbit brain homogenate as substrate showed three intrinsic substrates (80 kDa, 60 kDa and 42 kDa), which were phosphorylated in a Ca2+/CaM-dependent manner. These findings suggest that a new Ca2+/CaM-dependent protein kinase could be identified by the RBA.
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12

Scott-Woo, G. C., C. Sutherland, and M. P. Walsh. "Kinase activity associated with caldesmon is Ca2+/calmodulin-dependent kinase II." Biochemical Journal 268, no. 2 (June 1, 1990): 367–70. http://dx.doi.org/10.1042/bj2680367.

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The relationship of the kinase which co-purifies with caldesmon to Ca2+/calmodulin-dependent protein kinase II (CaM-kinase II) was investigated by studying the phosphorylation of bovine brain synapsin I, as well-characterized substrate of CaM-kinase II. Synapsin I is a very good substrate (Km = 90 nM) of the co-purifying kinase, which phosphorylates two sites in synapsin I, both of which are distinct from the single site phosphorylated by cyclic-AMP-dependent protein kinase. Phosphorylation of synapsin I is Ca2(+)- and calmodulin-dependent: half-maximal activation occurs at 0.13 microM-Ca2+ and maximal activity at 0.4 microM-Ca2+. Phosphorylation of the co-purifying kinase slightly enhances the rate, but does not alter the stoichiometry, of subsequent synapsin I phosphorylation; it does, however, circumvent the requirement for Ca2+ and calmodulin. The properties of this kinase therefore closely resemble those of CaM-kinase II, and we conclude that it is probably a smooth-muscle isoenzyme of CaM-kinase II.
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13

Kitani, T., S. Okuno, and H. Fujisawa. "Regulation of Ca2+/Calmodulin-Dependent Protein Kinase Kinase by cAMP-Dependent Protein Kinase: II. Mutational Analysis." Journal of Biochemistry 130, no. 4 (October 1, 2001): 515–25. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a003014.

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14

Colbran, R. J. "Protein Phosphatases and Calcium/Calmodulin-Dependent Protein Kinase II-Dependent Synaptic Plasticity." Journal of Neuroscience 24, no. 39 (September 29, 2004): 8404–9. http://dx.doi.org/10.1523/jneurosci.3602-04.2004.

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15

Bartelt, D. C., D. J. Wolff, and G. A. Scheele. "Calmodulin-binding proteins and calmodulin-regulated enzymes in dog pancreas." Biochemical Journal 240, no. 3 (December 15, 1986): 753–63. http://dx.doi.org/10.1042/bj2400753.

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Calmodulin was isolated and purified to homogeneity from dog pancreas. Highly purified subcellular fractions were prepared from dog pancreas by zonal sucrose-density ultracentrifugation and assayed for their ability to bind 125I-calmodulin in vitro. Proteins contained in these fractions were also examined for binding of 125I-calmodulin after their separation by polyacrylamide-gel electrophoresis in SDS. Calmodulin-binding proteins were detected in all subcellular fractions except the zymogen granule and zymogen-granule membrane fractions. One calmodulin-binding protein (Mr 240,000), observed in a washed smooth-microsomal fraction, has properties similar to those of alpha-fodrin. The postribosomal-supernatant fraction contained three prominent calmodulin-binding proteins, with apparent Mr values of 62,000, 50,000 and 40,000. Calmodulin-binding proteins, prepared from a postmicrosomal-supernatant fraction by Ca2+-dependent affinity chromatography on immobilized calmodulin, exhibited calmodulin-dependent phosphodiesterase, protein phosphatase and protein kinase activities. In the presence of Ca2+ and calmodulin, phosphorylation of smooth-muscle myosin light chain and brain synapsin and autophosphorylation of a Mr-50,000 protein were observed. Analysis of the protein composition of the preparation by SDS/polyacrylamide-gel electrophoresis revealed a major protein of Mr 50,000 which bound 125I-calmodulin. This protein shares characteristics with the calmodulin-dependent multifunctional protein kinase (kinase II) recently observed to have a widespread distribution. The possible role of calmodulin-binding proteins and calmodulin-regulated enzymes in the regulation of exocrine pancreatic protein synthesis and secretion is discussed.
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16

Katoh, T., and H. Fujisawa. "Autoactivation of calmodulin-dependent protein kinase II by autophosphorylation." Journal of Biological Chemistry 266, no. 5 (February 1991): 3039–44. http://dx.doi.org/10.1016/s0021-9258(18)49951-6.

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17

Gupta, Ram P., Daniel M. Lapadula, and Mohamed B. Abou-Donia. "Ca2+/calmodulin-dependent protein kinase II from hen brain." Biochemical Pharmacology 43, no. 9 (May 1992): 1975–88. http://dx.doi.org/10.1016/0006-2952(92)90641-u.

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18

Schulman, Howard, and Mark E. Anderson. "Ca2+/calmodulin-dependent protein kinase II in heart failure." Drug Discovery Today: Disease Mechanisms 7, no. 2 (June 2010): e117-e122. http://dx.doi.org/10.1016/j.ddmec.2010.07.005.

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19

Colbran, R. J., M. K. Smith, C. M. Schworer, Y. L. Fong, and T. R. Soderling. "Regulatory Domain of Calcium/Calmodulin-dependent Protein Kinase II." Journal of Biological Chemistry 264, no. 9 (March 1989): 4800–4804. http://dx.doi.org/10.1016/s0021-9258(18)83661-4.

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20

Bass, Martha, Harish C. Pant, Harold Gainer, and Thomas R. Soderling. "Calcium/Calmodulin-Dependent Protein Kinase II in Squid Synaptosomes." Journal of Neurochemistry 49, no. 4 (October 1987): 1116–23. http://dx.doi.org/10.1111/j.1471-4159.1987.tb10001.x.

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21

Lu, Haiqin, Hung-Tat Leung, Ning Wang, William L. Pak, and Bih-Hwa Shieh. "Role of Ca2+/calmodulin-dependent protein kinase II inDrosophilaphotoreceptors." Journal of Biological Chemistry 284, no. 23 (May 29, 2009): 16060.4–16060. http://dx.doi.org/10.1074/jbc.a806956200.

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22

Lu, Haiqin, Hung-Tat Leung, Ning Wang, William L. Pak, and Bih-Hwa Shieh. "Role of Ca2+/Calmodulin-dependent Protein Kinase II inDrosophilaPhotoreceptors." Journal of Biological Chemistry 284, no. 17 (March 2, 2009): 11100–11109. http://dx.doi.org/10.1074/jbc.m806956200.

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23

Yamagata, Yoko, and Kunihiko Obata. "Ca2+/calmodulin-dependent protein kinase II in septal kindling." Neuroscience Research Supplements 19 (January 1994): S168. http://dx.doi.org/10.1016/0921-8696(94)92741-3.

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24

Colbran, Roger J., and Abigail M. Brown. "Calcium/calmodulin-dependent protein kinase II and synaptic plasticity." Current Opinion in Neurobiology 14, no. 3 (June 2004): 318–27. http://dx.doi.org/10.1016/j.conb.2004.05.008.

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25

Zhang, Xuejing, Jaclyn Connelly, Edwin S. Levitan, Dandan Sun, and Jane Q. Wang. "Calcium/Calmodulin–Dependent Protein Kinase II in Cerebrovascular Diseases." Translational Stroke Research 12, no. 4 (March 13, 2021): 513–29. http://dx.doi.org/10.1007/s12975-021-00901-9.

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AbstractCerebrovascular disease is the most common life-threatening and debilitating condition that often leads to stroke. The multifunctional calcium/calmodulin-dependent protein kinase II (CaMKII) is a key Ca2+ sensor and an important signaling protein in a variety of biological systems within the brain, heart, and vasculature. In the brain, past stroke-related studies have been mainly focused on the role of CaMKII in ischemic stroke in neurons and established CaMKII as a major mediator of neuronal cell death induced by glutamate excitotoxicity and oxidative stress following ischemic stroke. However, with growing understanding of the importance of neurovascular interactions in cerebrovascular diseases, there are clearly gaps in our understanding of how CaMKII functions in the complex neurovascular biological processes and its contributions to cerebrovascular diseases. Additionally, emerging evidence demonstrates novel regulatory mechanisms of CaMKII and potential roles of the less-studied CaMKII isoforms in the ischemic brain, which has sparked renewed interests in this dynamic kinase family. This review discusses past findings and emerging evidence on CaMKII in several major cerebrovascular dysfunctions including ischemic stroke, hemorrhagic stroke, and vascular dementia, focusing on the unique roles played by CaMKII in the underlying biological processes of neuronal cell death, neuroinflammation, and endothelial barrier dysfunction triggered by stroke. We also highlight exciting new findings, promising therapeutic agents, and future perspectives for CaMKII in cerebrovascular systems.
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26

Wicks, Stephen J., Stephen Lui, Nadia Abdel-Wahab, Roger M. Mason, and Andrew Chantry. "Inactivation of Smad-Transforming Growth Factor β Signaling by Ca2+-Calmodulin-Dependent Protein Kinase II." Molecular and Cellular Biology 20, no. 21 (November 1, 2000): 8103–11. http://dx.doi.org/10.1128/mcb.20.21.8103-8111.2000.

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ABSTRACT Members of the transforming growth factor β (TGF-β) family transduce signals through Smad proteins. Smad signaling can be regulated by the Ras/Erk/mitogen-activated protein pathway in response to receptor tyrosine kinase activation and the gamma interferon pathway and also by the functional interaction of Smad2 with Ca2+-calmodulin. Here we report that Smad–TGF-β-dependent transcriptional responses are prevented by expression of a constitutively activated Ca2+-calmodulin-dependent protein kinase II (Cam kinase II). Smad2 is a target substrate for Cam kinase II in vitro at serine-110, -240, and -260. Cam kinase II induces in vivo phosphorylation of Smad2 and Smad4 and, to a lesser extent, Smad3. A phosphopeptide antiserum raised against Smad2 phosphoserine-240 reacted with Smad2 in vivo when coexpressed with Cam kinase II and by activation of the platelet-derived growth factor receptor, the epidermal growth factor receptor, HER2 (c-erbB2), and the TGF-β receptor. Furthermore, Cam kinase II blocked nuclear accumulation of a Smad2 and induced Smad2-Smad4 hetero-oligomerization independently of TGF-β receptor activation, while preventing TGF-β-dependent Smad2-Smad3 interactions. These findings provide a novel cross-talk mechanism by which Ca2+-dependent kinases activated downstream of multiple growth factor receptors antagonize cell responses to TGF-β.
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27

Singla, Sheela I., Andy Hudmon, Jonathan M. Goldberg, Janet L. Smith, and Howard Schulman. "Molecular Characterization of Calmodulin Trapping by Calcium/Calmodulin-dependent Protein Kinase II." Journal of Biological Chemistry 276, no. 31 (May 30, 2001): 29353–60. http://dx.doi.org/10.1074/jbc.m101744200.

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28

Li, Huan, and >Rotimi E. Aluko. "Structural modulation of calmodulin and calmodulin-dependent protein kinase II by pea protein hydrolysates." International Journal of Food Sciences and Nutrition 57, no. 3-4 (January 2006): 178–89. http://dx.doi.org/10.1080/09637480600659144.

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Ginnan, Roman, and Harold A. Singer. "CaM kinase II-dependent activation of tyrosine kinases and ERK1/2 in vascular smooth muscle." American Journal of Physiology-Cell Physiology 282, no. 4 (April 1, 2002): C754—C761. http://dx.doi.org/10.1152/ajpcell.00335.2001.

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In vascular smooth muscle (VSM) and many other cells, G protein receptor-coupled activation of mitogen-activated protein kinases has been linked, in part, to increases in free intracellular Ca2+. Previously, we demonstrated that ionomycin-, angiotensin II-, and thrombin-induced activation of extracellular signal-regulated kinase (ERK)1/2 in VSM cells was attenuated by pretreatment with KN-93, a selective inhibitor of the multifunctional Ca2+/calmodulin-dependent protein kinase (CaM kinase II). In the present study, we show that the Ca2+-dependent pathway leading to activation of ERK1/2 is preceded by nonreceptor proline-rich tyrosine kinase (PYK2) activation and epidermal growth factor (EGF) receptor tyrosine phosphorylation and is attenuated by inhibitors of src family kinases or the EGF receptor tyrosine kinase. Furthermore, we demonstrate that pretreatment with KN-93 or a CaM kinase II inhibitor peptide inhibits Ca2+-dependent PYK2 activation and EGF receptor tyrosine phosphorylation in response to ionomycin, ATP, and platelet-derived growth factor but has no effect on phorbol 12,13-dibutyrate- or EGF-induced responses. The results implicate CaM kinase II as an intermediate in the Ca2+/calmodulin-dependent activation of PYK2.
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Schulman, H. "Activity-Dependent Regulation of Calcium/Calmodulin-Dependent Protein Kinase II Localization." Journal of Neuroscience 24, no. 39 (September 29, 2004): 8399–403. http://dx.doi.org/10.1523/jneurosci.3606-04.2004.

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31

Chenglong, Liu, Liu Haihua, Zhang Fei, Zheng Jie, and Wei Fang. "Scutellarin Mitigates Cancer-Induced Bone Pain by Suppressing CaMKII/CREB Pathway in Rat Models." Current Topics in Nutraceutical Research 17, no. 3 (April 1, 2019): 249–53. http://dx.doi.org/10.37290/ctnr2641-452x.17:249-253.

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Cancer-induced bone pain is a severe and complex pain caused by metastases to bone in cancer patients. The aim of this study was to investigate the analgesic effect of scutellarin on cancer-induced bone pain in rat models by intrathecal injection of Walker 256 carcinoma cells. Mechanical allodynia was determined by paw withdrawal threshold in response to mechanical stimulus, and thermal hyperalgesia was indicated by paw withdrawal latency in response to noxious thermal stimulus. The paw withdrawal threshold and paw withdrawal latencies were significantly decreased after inoculation of tumor cells, whereas administration of scutellarin significantly attenuated tumor cell inoculation-induced mechanical and heat hyperalgesia. Tumor cell inoculation-induced tumor growth was also significantly abrogated by scutellarin. Ca2+/calmodulin-dependent protein kinase II is a multifunctional kinase with up-regulated activity in bone pain models. The activation of Ca2+/calmodulin-dependent protein kinase II triggers phosphorylation of cAMP-response element binding protein. Scutellarin significantly reduced the expression of phosphorylated-Ca2+/calmodulin-dependent protein kinase II and phosphorylated-cAMP-response element binding protein in cancer-induced bone pain rats. Collectively, our study demonstrated that scutellarin attenuated tumor cell inoculation-induced bone pain by down-regulating the expression of phosphorylated-Ca2+/calmodulin-dependent protein kinase II and phosphorylated-cAMP-response element binding protein. The suppressive effect of scutellarin on phosphorylated-Ca2+/calmodulin-dependent protein kinase II/phosphorylated-cAMP-response element binding protein activation may serve as a novel therapeutic strategy for CIBP management.
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32

Pfitzer, Gabriele. "Invited Review: Regulation of myosin phosphorylation in smooth muscle." Journal of Applied Physiology 91, no. 1 (July 1, 2001): 497–503. http://dx.doi.org/10.1152/jappl.2001.91.1.497.

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Phosphorylation of the regulatory light chains of myosin II (rMLC) by the Ca2+/calmodulin-dependent myosin light-chain kinase (MLCK) and dephosphorylation by a type 1 phosphatase (MLCP), which is targeted to myosin by a regulatory subunit (MYPT1), are the predominant mechanisms of regulation of smooth muscle tone. The activities of both enzymes are modulated by several protein kinases. MLCK is inhibited by the Ca2+/calmodulin-dependent protein kinase II, whereas the activity of MLCP is increased by cGMP and perhaps also cAMP-dependent protein kinases. In either case, this results in a decrease in the Ca2+ sensitivity of rMLC phosphorylation and force production. The activity of MLCP is inhibited by Rho-associated kinase, one of the effectors of the monomeric GTPase Rho, and protein kinase C, leading to an increase in Ca2+sensitivity. Hence, smooth muscle tone appears to be regulated by a network of activating and inactivating intracellular signaling cascades.
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33

Yamamoto, Hideyuki, Nobuaki Maeda, Michio Niinobe, Eishichi Miyamoto, and Katsuhiko Mikoshiba. "Phosphorylation of P400Protein by Cyclic AMP-Dependent Protein Kinase and Ca2+/Calmodulin-Dependent Protein Kinase II." Journal of Neurochemistry 53, no. 3 (September 1989): 917–23. http://dx.doi.org/10.1111/j.1471-4159.1989.tb11792.x.

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34

Konstantopoulos, Nicky, Seb Marcuccio, Stella Kyi, Violet Stoichevska, Laura A. Castelli, Colin W. Ward, and S. Lance Macaulay. "A Purine Analog Kinase Inhibitor, Calcium/Calmodulin-Dependent Protein Kinase II Inhibitor 59, Reveals a Role for Calcium/Calmodulin-Dependent Protein Kinase II in Insulin-Stimulated Glucose Transport." Endocrinology 148, no. 1 (January 1, 2007): 374–85. http://dx.doi.org/10.1210/en.2006-0446.

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Olomoucine is known as a cyclin-dependent kinase inhibitor. We found that olomoucine blocked insulin’s ability to stimulate glucose transport. It did so without affecting the activity of known insulin signaling proteins. To identify the olomoucine-sensitive kinase(s), we prepared analogs that could be immobilized to an affinity resin to isolate binding proteins. One of the generated analogs inhibited insulin-stimulated glucose uptake with increased sensitivity compared with olomoucine. The IC50 for inhibition of insulin-stimulated glucose uptake occurred at analog concentrations as low as 0.1 μm. To identify proteins binding to the analog, [35S]-labeled cell lysates prepared from 3T3-L1 adipocytes were incubated with analog chemically cross-linked to a resin support and binding proteins analyzed by SDS-PAGE. The major binding species was a doublet at 50–60 kDa, which was identified as calcium/calmodulin-dependent protein kinase II (CaMKII) by N-terminal peptide analysis and confirmed by matrix-assisted laser desorption ionization-mass spectrometry as the δ- and β-like isoforms. To investigate CaMKII involvement in insulin-stimulated glucose uptake, 3T3-L1 adipocytes were infected with retrovirus encoding green fluorescent protein (GFP)-hemagluttinin tag (HA)-tagged CaMKII wild-type or the ATP binding mutant, K42M. GFP-HA-CaMKII K42M cells had less kinase activity than cells expressing wild-type GFP-HA-CaMKII. Insulin-stimulated glucose transport was significantly decreased (∼80%) in GFP-HA-CaMKII K42M cells, compared with nontransfected cells, and cells expressing either GFP-HA-CaMKII or GFP-HA. There was not a concomitant decrease in insulin-stimulated GLUT4 translocation in GFP-HA-CaMKII K42M cells when compared with GFP-HA alone. However, insulin-stimulated GLUT4 translocation in GFP-HA-CaMKII cells was significantly higher, compared with either GFP-HA or GFP-HA-CaMKII K42M cells. Our results implicate the involvement of CaMKII in glucose transport in a permissive role.
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35

Hughes, S. J., H. Smith, and S. J. H. Ashcroft. "Characterization of Ca2+/calmodulin-dependent protein kinase in rat pancreatic islets." Biochemical Journal 289, no. 3 (February 1, 1993): 795–800. http://dx.doi.org/10.1042/bj2890795.

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We have attempted to identify islet Ca2+/calmodulin-dependent protein kinase (CaM kinase) by comparing its activity with purified brain CaM kinase II. Islet CaM kinase, in the presence of calmodulin and Ca2+, phosphorylated major endogenous substrates of 102, 57 and 53 kDa and also exogenous glycogen synthase; brain CaM kinase II phosphorylated glycogen synthase and peptides of 57 and 53 kDa. Alloxan (1 mM) inhibited the phosphorylation of glycogen synthase and the 102, 57 and 53 kDa islet peptides by islet CaM kinase; the phosphorylation of glycogen synthase and the 57 and 53 kDa substrates by brain CaM kinase II was also inhibited by alloxan. The Ca2+ and calmodulin-dependencies of phosphorylation of the endogenous islet substrates differed. In the presence of 400 nM calmodulin, half-maximal phosphorylation was attained at Ca2+ concentrations of 80 +/- 9, 401 +/- 61 and 459 +/- 59 nM for the 102, 57 and 53 kDa substrates respectively. In the presence of 10 microM Ca2+, half-maximal phosphorylation was attained at calmodulin concentrations of 9 +/- 2, 38 +/- 2.5 and 37 +/- 2 nM for the 102, 57 and 53 kDa substrates respectively. Differential centrifugation located the 102 kDa substrate in the post-100,000 g supernatant and the 57 and 53 kDa substrates in the particulate fraction. These data suggest that islet CaM kinase is similar to, if not identical with, brain CaM kinase II, but that phosphorylation of the endogenous 102 kDa substrate occurs by a distinct kinase which shows different sensitivities to Ca2+ and calmodulin. This kinase probably corresponds to CaM kinase III and the 102 kDa peptide to elongation factor 2 (EF-2), since the 102 kDa peptide was shown to undergo ADP-ribosylation in the presence of diphtheria toxin and NAD+.
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36

Yanagihara, Nobuyuki, Yumiko Toyohira, Hideyuki Yamamoto, Yasutaka Ohta, Eishichi Miyamoto, and Futoshi Izumi. "Ca /calmodulin-dependent protein kinase II and calmodulin-binding proteins in bovine adrenal medullary cells." Japanese Journal of Pharmacology 55 (1991): 93. http://dx.doi.org/10.1016/s0021-5198(19)38289-7.

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37

Lickteig, R., S. Shenolikar, L. Denner, and P. T. Kelly. "Regulation of Ca2+/calmodulin-dependent protein kinase II by Ca2+/calmodulin-independent autophosphorylation." Journal of Biological Chemistry 263, no. 35 (December 1988): 19232–39. http://dx.doi.org/10.1016/s0021-9258(18)37414-3.

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38

Putkey, John A., and M. Neal Waxham. "A Peptide Model for Calmodulin Trapping by Calcium/Calmodulin-dependent Protein Kinase II." Journal of Biological Chemistry 271, no. 47 (November 22, 1996): 29619–23. http://dx.doi.org/10.1074/jbc.271.47.29619.

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39

Lorenz, Jillinda M., Marilyn H. Riddervold, Elizabeth A. H. Beckett, Salah A. Baker, and Brian A. Perrino. "Differential autophosphorylation of CaM kinase II from phasic and tonic smooth muscle tissues." American Journal of Physiology-Cell Physiology 283, no. 5 (November 1, 2002): C1399—C1413. http://dx.doi.org/10.1152/ajpcell.00020.2002.

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Ca+/calmodulin-dependent protein kinase II (CaM kinase II) is regulated by calcium oscillations, autophosphorylation, and its subunit composition. All four subunit isoforms were detected in gastric fundus and proximal colon smooth muscles by RT-PCR, but only the γ and δ isoforms are expressed in myocytes. Relative γ and δ message levels were quantitated by real-time PCR. CaM kinase II protein and Ca2+/calmodulin-stimulated (total) activity levels are higher in proximal colon smooth muscle lysates than in fundus lysates, but Ca2+/calmodulin-independent (autonomous) activity is higher in fundus lysates. CaM kinase II in fundus lysates is relatively unresponsive to Ca2+/calmodulin. Alkaline phosphatase decreased CaM kinase II autonomous activity in fundus lysates and restored its responsiveness to Ca2+/calmodulin. Acetylcholine (ACh) increased autonomous CaM kinase II activity in fundus and proximal colon smooth muscles in a time- and dose-dependent manner. KN-93 enhanced ACh-induced fundus contractions but inhibited proximal colon contractions. The different properties of CaM kinase II from fundus and proximal colon smooth muscles suggest differential regulation of its autophosphorylation and activity in tonic and phasic gastrointestinal smooth muscles.
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40

Sato, Hirokazu, Takashi Yamauchi, and Hi toshi Fujisawa. "Purification and Characterization of Calmodulin-Dependent Protein Kinase II from Rat Spleen: A New Type of Calmodulin-Dependent Protein Kinase II1." Journal of Biochemistry 107, no. 6 (June 1990): 802–9. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a123129.

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41

Scott, C. W., C. B. Caputo, and A. I. Salama. "Properties of a microtubule-associated cofactor-independent protein kinase from pig brain." Biochemical Journal 263, no. 1 (October 1, 1989): 207–14. http://dx.doi.org/10.1042/bj2630207.

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A protein kinase activity was identified in pig brain that co-purified with microtubules through repeated cycles of temperature-dependent assembly and disassembly. The microtubule-associated protein kinase (MTAK) phosphorylated histone H1; this activity was not stimulated by cyclic nucleotides. Ca2+ plus calmodulin, phospholipids or polyamines. MTAK did not phosphorylate synthetic peptides which are substrates for cyclic AMP-dependent protein kinase, cyclic GMP-dependent protein kinase. Ca2+/calmodulin-dependent protein kinase II, protein kinase C or casein kinase II. MTAK activity was inhibited by trifluoperazine [IC50 (median inhibitory concn.) = 600 microM] in a Ca2+-independent fashion. Ca2+ alone was inhibitory [IC50 = 4 mM). MTAK was not inhibited by heparin, a potent inhibitor of casein kinase II, nor a synthetic peptide inhibitor of cyclic AMP-dependent protein kinase. MTAK demonstrated a broad pH maximum (7.5-8.5) and an apparent Km for ATP of 45 microM. Mg2+ was required for enzyme activity and could not be replaced by Mn2+. MTAK phosphorylated serine and threonine residues on histone H1. MTAK is a unique cofactor-independent protein kinase that binds to microtubule structures.
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42

Nanba, Kazutaka, Andrew Chen, Koshiro Nishimoto, and William E. Rainey. "Role of Ca2+/Calmodulin-Dependent Protein Kinase Kinase in Adrenal Aldosterone Production." Endocrinology 156, no. 5 (February 13, 2015): 1750–56. http://dx.doi.org/10.1210/en.2014-1782.

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There is considerable evidence supporting the role of calcium signaling in adrenal regulation of both aldosterone synthase (CYP11B2) and aldosterone production. However, there have been no studies that investigated the role played by the Ca2+/calmodulin-dependent protein kinase kinase (CaMKK) in adrenal cells. In this study we investigated the role of CaMKK in adrenal cell aldosterone production. To determine the role of CaMKK, we used a selective CaMKK inhibitor (STO-609) in the HAC15 human adrenal cell line. Cells were treated with angiotensin II (Ang II) or K+ and evaluated for the expression of steroidogenic acute regulatory protein and CYP11B2 (mRNA/protein) as well as aldosterone production. We also transduced HAC15 cells with lentiviral short hairpin RNAs of CaMKK1 and CaMKK2 to determine which CaMKK plays a more important role in adrenal cell regulation of the calcium signaling cascade. The CaMKK inhibitor, STO-609, decreased aldosterone production in cells treated with Ang II or K+ in a dose-dependent manner. STO-609 (20μM) also inhibited steroidogenic acute regulatory protein and CYP11B2 mRNA/protein induction. CaMKK2 knockdown cells showed significant reduction of CYP11B2 mRNA induction and aldosterone production in cells treated with Ang II, although there was no obvious effect in CaMKK1 knockdown cells. In immunohistochemical analysis, CaMKK2 protein was highly expressed in human adrenal zona glomerulosa with lower expression in the zona fasciculata. In conclusion, the present study suggests that CaMKK2 plays a pivotal role in the calcium signaling cascade regulating adrenal aldosterone production.
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43

Waxham, M. Neal, and Jaroslaw Aronowski. "Calcium/calmodulin-dependent protein kinase II is phosphorylated by protein kinase C in vitro." Biochemistry 32, no. 11 (March 23, 1993): 2923–30. http://dx.doi.org/10.1021/bi00062a024.

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44

Wright, Susan C., Ute Schellenberger, Li Ji, g. Wang, and James W. Larrick. "Calmodulin‐dependent protein kinase II mediates signal transduction in apoptosis." FASEB Journal 11, no. 11 (September 1997): 843–49. http://dx.doi.org/10.1096/fasebj.11.11.9285482.

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45

Wagner, Stefan, Nataliya Dybkova, Eva C. L. Rasenack, Claudius Jacobshagen, Larissa Fabritz, Paulus Kirchhof, Sebastian K. G. Maier, et al. "Ca2+/calmodulin-dependent protein kinase II regulates cardiac Na+ channels." Journal of Clinical Investigation 116, no. 12 (December 1, 2006): 3127–38. http://dx.doi.org/10.1172/jci26620.

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46

Swaminathan, Paari Dominic, Anil Purohit, Thomas J. Hund, and Mark E. Anderson. "Calmodulin-Dependent Protein Kinase II: Linking Heart Failure and Arrhythmias." Circulation Research 110, no. 12 (June 8, 2012): 1661–77. http://dx.doi.org/10.1161/circresaha.111.243956.

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47

Bland, M. M., O. B. Mcdonald, and A. C. Carrera. "p56LCK Phosphorylation by Ca2+/Calmodulin-Dependent Protein-Kinase Type II." Biochemical and Biophysical Research Communications 198, no. 1 (January 1994): 67–73. http://dx.doi.org/10.1006/bbrc.1994.1010.

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48

Mayer, Peter, Matthias Möhlig, Helmut Schatz, and Andreas Pfeiffer. "New isoforms of multifunctional calcium/calmodulin-dependent protein kinase II." FEBS Letters 333, no. 3 (November 1, 1993): 315–18. http://dx.doi.org/10.1016/0014-5793(93)80678-n.

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49

Kato, M., T. Sasaki, K. Imazumi, K. Takahashi, K. Araki, H. Shirataki, Y. Matsuura, A. Ishida, H. Fujisawa, and Y. Takai. "Phosphorylation of Rabphilin-3A by Calmodulin-Dependent Protein Kinase II." Biochemical and Biophysical Research Communications 205, no. 3 (December 1994): 1776–84. http://dx.doi.org/10.1006/bbrc.1994.2875.

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50

Singer, Harold A. "Ca2+/calmodulin-dependent protein kinase II function in vascular remodelling." Journal of Physiology 590, no. 6 (March 2012): 1349–56. http://dx.doi.org/10.1113/jphysiol.2011.222232.

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