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Journal articles on the topic 'Calcium/calmodulin-dependent protein kinase II'

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Published: 4 June 2021

Last updated: 1 February 2022

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

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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12

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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13

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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14

Hoffman, Laurel, Richard A. Stein, Roger J. Colbran, and Hassane S. Mchaourab. "Conformational changes underlying calcium/calmodulin-dependent protein kinase II activation." EMBO Journal 30, no. 7 (February 22, 2011): 1251–62. http://dx.doi.org/10.1038/emboj.2011.40.

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15

Neal Waxham, M., Robert C. Malenka, Paul T. Kelly, and Michael D. Mauk. "Calcium/calmodulin-dependent protein kinase II regulates hippocampal synaptic transmission." Brain Research 609, no. 1-2 (April 1993): 1–8. http://dx.doi.org/10.1016/0006-8993(93)90847-g.

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16

Valentine, M. A., A. J. Czernik, N. Rachie, H. Hidaka, C. L. Fisher, J. C. Cambier, and K. Bomsztyk. "Anti-immunoglobulin M activates nuclear calcium/calmodulin-dependent protein kinase II in human B lymphocytes." Journal of Experimental Medicine 182, no. 6 (December 1, 1995): 1943–49. http://dx.doi.org/10.1084/jem.182.6.1943.

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We and others have previously shown that the nuclear protein, Ets-1, is phosphorylated in a calcium-dependent manner after ligation of immunoglobulin (Ig) M on B lymphocytes. As this phosphorylation was independent of protein kinase C activity, we tested whether a calcium/calmodulin-dependent protein kinase (CaM kinase) might phosphorylate the Ets-1 protein after elevation of intracellular free calcium concentrations. The dephosphorylated form of Ets-1 has been shown to bind to chromatin, suggesting that the operative kinase should be detectable in the nucleus. We prepared nuclear extracts from two human B cell lines in which increased intracellular free calcium levels correlated with increased phosphorylation of the Ets-1 protein. Activity of the CaM kinases was determined using a synthetic peptide substrate both in the absence and presence of an inhibitor specific for the CaM kinase family, KN-62. Stimulation of cells with anti-IgM led to increased activity of a nuclear kinase that could phosphorylate the peptide, and this activity was reduced by 10 microM KN-62. Kinase activity was reduced in lysates preadsorbed using an antibody specific for CaM kinase II. Two-dimensional phosphopeptide maps of the Ets-1 protein from cells incubated with ionomycin or anti-IgM contained two unique phosphopeptides that were absent in untreated cells. Incubation of isolated Ets-1 protein with purified CaM kinase II produced phosphorylation of peptides that migrated identically to those found in cells incubated with either anti-IgM or ionomycin. These data suggest a model of signal transduction by the antigen receptor on B lymphocytes in which increased intracellular free calcium can rapidly activate nuclear CaM kinase II, potentially resulting in phosphorylation and regulation of DNA-binding proteins.

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17

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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18

Zhang, T. "Cardiomyocyte Calcium and Calcium/Calmodulin-dependent Protein Kinase II: Friends or Foes?" Recent Progress in Hormone Research 59, no. 1 (January 1, 2004): 141–68. http://dx.doi.org/10.1210/rp.59.1.141.

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19

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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20

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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21

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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22

Gorelick, F. S., A. Chang, and J. D. Jamieson. "Calcium-calmodulin-stimulated protein kinase in developing pancreas." American Journal of Physiology-Gastrointestinal and Liver Physiology 253, no. 4 (October 1, 1987): G469—G476. http://dx.doi.org/10.1152/ajpgi.1987.253.4.g469.

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To implicate the Ca2+-calmodulin-dependent protein kinase (CDPK) in the secretory response of pancreatic acinar cells to postnatal neurohumoral stimulation, we examined enzymatic protein kinase activity during pancreatic development. CDPK was investigated by measuring the phosphorylation of endogenous proteins and an exogenous substrate, synapsin I. Ca2+-calmodulin (CaM)-stimulated phosphorylation of endogenous proteins as well as synapsin I progressively increased in pancreatic supernatants from rats of increasing age. When compared with embryonic pancreas (1 day before birth), Ca2+-CaM-stimulated protein kinase activity increased two- and sixfold in neonatal (1 day after birth) and adult pancreas (60 days after birth), respectively, when normalized to protein content. To further characterize CDPK activity, soluble fractions prepared from embryonic, neonatal, and adult pancreas were separated by gel filtration chromatography. CDPK activities from embryonic and neonatal pancreas were contained in fractions of relative molecular weights (Mr) less than 200,000. In contrast, kinase activity from adult pancreas was predominantly comprised of a Mr approximately 550,000 species that coeluted with a type II CDPK. Increasing amounts of a Mr = 51,000 CaM-binding protein as a function of increasing age were consistent with the developmental appearance of the CaM-binding subunit of type II Ca2+-CaM-stimulated protein kinase. CaM levels increased in parallel with total Ca2+-CaM-stimulated protein kinase activity. Coordinate enhancement of type II CDPK activity and secretagogue responsiveness during pancreatic maturation may suggest a role for this enzyme in the secretory process.

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23

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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24

Shanker, G., and R. A. Pieringer. "Investigations on myelinogenesis in vitro: II. The occurrence and regulation of protein kinases by thyroid hormone in primary cultures of cells dissociated from embryonic mouse brain." Bioscience Reports 7, no. 2 (February 1, 1987): 159–65. http://dx.doi.org/10.1007/bf01121880.

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The occurrence and regulation by thyroid hormone of four protein kinases (cyclic AMP independent and dependent, calcium/calmodulin stimulated, and calcium/phosphatidyl serine stimulated protein kinases) was studied in primary cultures of cells dissociated from embryonic mouse brain. Serum from a thyroidectomized calf, which contained low levels of L-3,5,3′-triiodothyronine, T3 (<25 ng/100 ml), and thyroxine, T4 (<1 μg/100 ml) was used in the culture medium in place of normal calf-serum (T3, 130 ng/100 ml; T4 5.9 μg/100 ml) to render the cultures responsive to exogenously added T3. Cultures grown in hypothyroid calf-serum containing medium had less cAMP dependent and independent protein kinase activity than control cultures grown in normal calf-serum containing medium. However, this activity was restorable to a considerable degree if the cultures grown in hypothyroid calf serum containing medium were supplemented with L-3,5,3′-triiodothyronine (T3). The presence of calcium/calmodulin stimulated protein kinase was also distinctly observed. In comparison, the activity of calcium/phosphatidyl serine stimulated protein kinase was less than the other protein kinases.

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25

Matovcik, L. M., B. Haimowitz, J. R. Goldenring, A. J. Czernik, and F. S. Gorelick. "Distribution of calcium/calmodulin-dependent protein kinase II in rat ileal enterocytes." American Journal of Physiology-Cell Physiology 264, no. 4 (April 1, 1993): C1029—C1036. http://dx.doi.org/10.1152/ajpcell.1993.264.4.c1029.

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Ca2+/calmodulin (CaM)-dependent protein kinase II is a major effector of the Ca2+ signaling pathway. It has a wide tissue distribution and phosphorylates multiple substrates. Villus enterocytes from rat ileum contain a Ca2+/CaM-dependent kinase activity that phosphorylates the exogenous neural substrate synapsin I. This phosphorylation is blocked by a specific peptide inhibitor. Antibodies made to rat brain Ca2+/CaM-dependent protein kinase II label a single band with a relative molecular mass of approximately 50 kDa in isolated rat enterocytes by immunoblot. Almost one-half of this immunoreactive protein is preferentially found in a particulate compared with a soluble subcellular fraction of the enterocytes. Virtually all of the 50-kDa band in the particulate fraction is insoluble in nonionic detergent, suggesting that the kinase is associated with the enterocyte cytoskeleton. Antibodies to Ca2+/CaM-dependent protein kinase II immunocytochemically detect fibrillar structures concentrated in the terminal web region of intestinal epithelial cells that colocalized with myosin II. This enzyme may have a role in regulating the intestinal epithelial cytoskeleton.

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26

Song, Tao, Naoya Hatano, Toshie Kambe, Yoshiaki Miyamoto, Hideshi Ihara, Hideyuki Yamamoto, Katsuyoshi Sugimoto, et al. "Nitric oxide-mediated modulation of calcium/calmodulin-dependent protein kinase II." Biochemical Journal 412, no. 2 (May 14, 2008): 223–31. http://dx.doi.org/10.1042/bj20071195.

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The mechanisms of NO inhibition of CaMK [Ca2+/CaM (calmodulin)-dependent protein kinase] II activity were studied. In rat pituitary tumour GH3 cells, TRH [thyrotrophin (TSH)-releasing hormone]-stimulated phosphorylation of nNOS [neuronal NOS (NO synthase)] at Ser847 was sensitive to an inhibitor of CaMKs, KN-93, and was enhanced by inhibition of nNOS with 7NI (7-nitroindazole). Enzyme activity of CaMKII following in situ treatment with 7NI was also increased. The in vitro activity of CaMKII was inhibited by co-incubation either with nNOS and L-arginine or with NO donors SNAP (S-nitroso-N-acetyl-DL-penicillamine) and DEA-NONOate [diethylamine-NONOate (diazeniumdiolate)]. Once inhibited by these treatments, CaMKII was observed to undergo full reactivation on the addition of a reducing reagent, DTT (dithiothreitol). In transfected cells expressing CaMKII and nNOS, treatment with the calcium ionophore A23187 further revealed nNOS phosphorylation at Ser847, which was enhanced by 7NI and CaMKII S-nitrosylation. Mutated CaMKII (C6A), in which Cys6 was substituted with an alanine residue, was refractory to 7NI-induced enhancement of nNOS phosphorylation or to CaMKII S-nitrosylation. Furthermore, we could identify Cys6 as a direct target for S-nitrosylation of CaMKII using MS. In addition, treatment with glutamate caused an increase in CaMKII S-nitrosylation in rat hippocampal slices. This glutamate-induced S-nitrosylation was blocked by 7NI. These results suggest that inactivation of CaMKII mediated by S-nitrosylation at Cys6 may contribute to NO-induced neurotoxicity in the brain.

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27

Yamamoto, Hideyuki, Koji Fukunaga, Kevin Lee, and Thomas R. Soderling. "Ischemia-Induced Loss of Brain Calcium/Calmodulin-Dependent Protein Kinase II." Journal of Neurochemistry 58, no. 3 (March 1992): 1110–17. http://dx.doi.org/10.1111/j.1471-4159.1992.tb09369.x.

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28

Mayadevi, M., D. R. Sherin, V. S. Keerthi, K. N. Rajasekharan, and R. V. Omkumar. "Curcumin is an inhibitor of calcium/calmodulin dependent protein kinase II." Bioorganic & Medicinal Chemistry 20, no. 20 (October 2012): 6040–47. http://dx.doi.org/10.1016/j.bmc.2012.08.029.

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29

Colbran, Roger J. "Regulation and role of brain calcium/calmodulin-dependent protein kinase II." Neurochemistry International 21, no. 4 (December 1992): 469–97. http://dx.doi.org/10.1016/0197-0186(92)90080-b.

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30

SODERLING, THOMAS R. "MODULATION OF GLUTAMATE RECEPTORS BY CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE II." Neurochemistry International 28, no. 4 (April 1996): 359–61. http://dx.doi.org/10.1016/0197-0186(95)00098-4.

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31

Soderling, Thomas R. "Calcium/calmodulin-dependent protein kinase II: role in learning and memory." Molecular and Cellular Biochemistry 127-128, no. 1 (November 1993): 93–101. http://dx.doi.org/10.1007/bf01076760.

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32

Payne, M. E., Y. L. Fong, T. Ono, R. J. Colbran, B. E. Kemp, T. R. Soderling, and A. R. Means. "Calcium/calmodulin-dependent protein kinase II. Characterization of distinct calmodulin binding and inhibitory domains." Journal of Biological Chemistry 263, no. 15 (May 1988): 7190–95. http://dx.doi.org/10.1016/s0021-9258(18)68626-0.

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33

McCarron, John G., J. Graham McGeown, Sheila Reardon, Mrtsuo Ikebe, Fredric S. Fay, and John V. Walsh Jr. "Calcium-dependent enhancement of calcium current in smooth muscle by calmodulin-dependent protein kinase II." Nature 357, no. 6373 (May 1992): 74–77. http://dx.doi.org/10.1038/357074a0.

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34

Rokolya, A., M. P. Walsh, and R. S. Moreland. "Calcium-and phorbol ester-dependent calponin phosphorylation in homogenates of swine carotid artery." American Journal of Physiology-Heart and Circulatory Physiology 271, no. 2 (August 1, 1996): H776—H783. http://dx.doi.org/10.1152/ajpheart.1996.271.2.h776.

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Calponin inhibits actin-activated myosin adenosinetriphosphatase (ATPase) activity, and phosphorylation reverses this inhibition. Calponin phosphorylation has been demonstrated in reconstituted contractile protein systems, but studies using intact smooth muscle have produced mixed results. The goal of this study was to determine if vascular smooth muscle contains the necessary biochemical machinery to catalyze calponin phosphorylation. We used swine carotid homogenate, which allows access to the intracellular components and contains all endogenous proteins and enzymes in physiologically relevant concentrations. We demonstrated that calponin is phosphorylated in response to Ca2+ (0.27 +/- 0.04 mol P(i)/mol calponin) and in response to phorbol 12,13-dibutyrate in the presence or absence of Ca2+ (0.48 +/- 0.09 mol P(i)/mol calponin). Calponin phosphorylation was inhibited by the protein kinase C inhibitor staurosporine but not by the Ca(2+)- and calmodulin-dependent protein kinase II inhibitor KN-62. We conclude that Ca(2+)-dependent and -independent isoforms of protein kinase C but not the Ca(2+) -and calmodulin-dependent protein kinase II catalyze calponin phosphorylation in the swine carotid artery.

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Borbiev, Talaibek, Alexander D. Verin, Shu Shi, Feng Liu, and Joe G. N. Garcia. "Regulation of endothelial cell barrier function by calcium/calmodulin-dependent protein kinase II." American Journal of Physiology-Lung Cellular and Molecular Physiology 280, no. 5 (May 1, 2001): L983—L990. http://dx.doi.org/10.1152/ajplung.2001.280.5.l983.

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Thrombin-induced endothelial cell barrier dysfunction is tightly linked to Ca2+-dependent cytoskeletal protein reorganization. In this study, we found that thrombin increased Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) activities in a Ca2+- and time-dependent manner in bovine pulmonary endothelium with maximal activity at 5 min. Pretreatment with KN-93, a specific CaM kinase II inhibitor, attenuated both thrombin-induced increases in monolayer permeability to albumin and decreases in transendothelial electrical resistance (TER). We next explored potential thrombin-induced CaM kinase II cytoskeletal targets and found that thrombin causes translocation and significant phosphorylation of nonmuscle filamin (ABP-280), which was attenuated by KN-93, whereas thrombin-induced myosin light chain phosphorylation was unaffected. Furthermore, a cell-permeable N-myristoylated synthetic filamin peptide (containing the COOH-terminal CaM kinase II phosphorylation site) attenuated both thrombin-induced filamin phosphorylation and decreases in TER. Together, these studies indicate that CaM kinase II activation and filamin phosphorylation may participate in thrombin-induced cytoskeletal reorganization and endothelial barrier dysfunction.

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Shackelford, D. A., R. Y. Yeh, M. Hsu, G. Buzsáki, and J. A. Zivin. "Effect of Cerebral Ischemia on Calcium/Calmodulin-Dependent Protein Kinase II Activity and Phosphorylation." Journal of Cerebral Blood Flow & Metabolism 15, no. 3 (May 1995): 450–61. http://dx.doi.org/10.1038/jcbfm.1995.56.

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The effects of cerebral ischemia on calcium/calmodulin-dependent kinase II (CaM kinase II) were investigated using the rat four-vessel occlusion model. In agreement with previous results using rat or gerbil models of cerebral ischemia or a rabbit model of spinal cord ischemia, this report demonstrates that transient forebrain ischemia leads to a reduction in CaM kinase II activity within 5 min of occlusion onset. Loss of activity from the cytosol fractions of homogenates from the neocortex, striatum, and hippocampus correlated with a decrease in the amount of CaM kinase α and β isoforms detected by immunoblotting. In contrast, there was an apparent increase in the amount of CaM kinase α and β in the particulate fractions. The decrease in the amount of CaM kinase isoforms from the cytosol but not the particulate fractions was confirmed by autophosphorylation of CaM kinase II after denaturation and renaturation in situ of the blotted proteins. These results indicate that ischemia causes a rapid inhibition of CaM kinase II activity and a change in the partitioning of the enzyme between the cytosol and particulate fractions. CaM kinase II is a multifunctional protein kinase, and the loss of activity may play a critical role in initiating the changes leading to ischemia-induced cell death. To identify a structural basis for the decrease in enzyme activity, tryptic peptide maps of CaM kinase II phosphorylated in vitro were compared. Phosphopeptide maps of CaM kinase α from particulate fractions of control and ischemic samples revealed not only reduced incorporation of phosphate into the protein but also the absence of a limited number of peptides in the ischemic samples. This suggested that certain sites are inaccessible, possibly due to a conformational change, a covalent modification of CaM kinase II, or steric hindrance by an associated molecule. Verifying one of these possibilities should help to elucidate the mechanism of ischemia-induced modulation of CaM kinase II.

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Walsh, Michael P. "Calcium-dependent mechanisms of regulation of smooth muscle contraction." Biochemistry and Cell Biology 69, no. 12 (December 1, 1991): 771–800. http://dx.doi.org/10.1139/o91-119.

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The contractile state of smooth muscle is regulated primarily by the sarcoplasmic (cytosolic) free Ca2+ concentration. A variety of stimuli that induce smooth muscle contraction (e.g., membrane depolarization, α-adrenergic and muscarinic agonists) trigger an increase in sarcoplasmic free [Ca2+] from resting levels of 120–270 to 500–700 nM. At the elevated [Ca2+], Ca2+ binds to calmodulin, the ubiquitous and multifunctional Ca2+-binding protein. The interaction of Ca2+ with CaM induces a conformational change in the Ca2+-binding protein with exposure of a site(s) of interaction with target proteins, the most important of which in the context of smooth muscle contraction is the enzyme myosin light chain kinase. The interaction of calmodulin with myosin light chain kinase results in activation of the kinase that catalyzes phosphorylation of myosin at serine-19 of each of the two 20-kDa light chains (native myosin is a hexamer composed of two heavy chains (230 kDa each) and two pairs of light chains (one pair of 20 kDa each and the other pair of 17 kDa each)). This simple phosphorylation reaction triggers cycling of myosin cross-bridges along actin filaments and the development of force. Relaxation of the muscle follows removal of Ca2+ from the sarcoplasm, whereupon calmodulin dissociates from myosin light chain kinase regenerating the inactive kinase; myosin is dephosphorylated by myosin light chain phosphatase(s), whereupon it dissociates and remains detached from the actin filament and the muscle relaxes. A substantial body of evidence has been accumulated in support of this central role of myosin phosphorylation–dephosphorylation in the regulation of smooth muscle contraction. However, a wide range of physiological and biochemical studies supports the existence of additional, secondary Ca2+-dependent mechanisms that can modulate or fine-tune the contractile state of the smooth muscle cell. Three such mechanisms have emerged: (i) the actin-, tropomyosin-, and calmodulin-binding protein, calponin; (ii) the actin-, myosin-, tropomyosin-, and calmodulin-binding protein, caldesmon; and (iii) the Ca2+- and phospholipid-dependent protein kinase (protein kinase C).Key words: smooth muscle, Ca2+, myosin phosphorylation, regulation of contraction.

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Schlender, K. K., and L. J. Bean. "Phosphorylation of chicken cardiac C-protein by calcium/calmodulin-dependent protein kinase II." Journal of Biological Chemistry 266, no. 5 (February 1991): 2811–17. http://dx.doi.org/10.1016/s0021-9258(18)49919-x.

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Churn, Severn B., Amy Yaghmai, John Povlishock, Azhar Rafiq, and Robert J. DeLorenzo. "Global Forebrain Ischemia Results in Decreased Immunoreactivity of Calcium/Calmodulin-Dependent Protein Kinase II." Journal of Cerebral Blood Flow & Metabolism 12, no. 5 (September 1992): 784–93. http://dx.doi.org/10.1038/jcbfm.1992.109.

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Previous studies utilizing crude brain homogenates have shown that forebrain ischemia results in inhibition of calcium/calmodulin-dependent protein kinase II (CaM kinase II) activity without large-scale proteolysis of the enzyme. In this report, a monoclonal antibody (1C3-3D6) directed against the β- (60-kDa) subunit of CaM kinase II that does not recognize ischemically altered enzyme was utilized to further investigate the ischemia-induced inhibition of CaM kinase II. Immunohistochemical investigations showed that the ischemia-induced decreased immunoreactivity of CaM kinase II occurred immediately following ischemic insult in ischemia-sensitive cells such as pyramidal cells of the hippocampus. No decrease in CaM kinase II immunoreactivity was observed in ischemia-resistant cells such as granule cells of the dentate gyrus. The decreased immunoreactivity was observed for CaM kinase II balanced for protein staining and calmodulin binding in vitro. In addition, autophosphorylation of CaM kinase II in the presence of low (7 μ M) or high (500 μ M) ATP did not alter immunoreactivity of the enzyme with 1C3-3D6. The data demonstrate the production of a monoclonal antibody that recognizes the β-subunit of CaM kinase II in a highly specific manner, but does not recognize ischemic enzyme. Together with previous studies, the data support the hypothesis that rapid, ischemia-induced inhibition of CaM kinase II activity may be involved in the cascade of events that lead to selective neuronal cell loss in stroke.

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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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Johnson, D. E., and A. Hudmon. "Activation State-Dependent Substrate Gating in Ca2+/Calmodulin-Dependent Protein Kinase II." Neural Plasticity 2017 (2017): 1–13. http://dx.doi.org/10.1155/2017/9601046.

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Calcium/calmodulin-dependent protein kinase II (CaMKII) is highly concentrated in the brain where its activation by the Ca2+sensor CaM, multivalent structure, and complex autoregulatory features make it an ideal translator of Ca2+signals created by different patterns of neuronal activity. We provide direct evidence that graded levels of kinase activity and extent of T287(T286αisoform) autophosphorylation drive changes in catalytic output and substrate selectivity. The catalytic domains of CaMKII phosphorylate purified PSDs much more effectively when tethered together in the holoenzyme versus individual subunits. Using multisubstrate SPOT arrays, high-affinity substrates are preferentially phosphorylated with limited subunit activity per holoenzyme, whereas multiple subunits or maximal subunit activation is required for intermediate- and low-affinity, weak substrates, respectively. Using a monomeric form of CaMKII to control T287autophosphorylation, we demonstrate that increased Ca2+/CaM-dependent activity for all substrates tested, with the extent of weak, low-affinity substrate phosphorylation governed by the extent of T287autophosphorylation. Our data suggest T287autophosphorylation regulates substrate gating, an intrinsic property of the catalytic domain, which is amplified within the multivalent architecture of the CaMKII holoenzyme.

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Tao-Cheng, J. H., L. Vinade, L. D. Pozzo-Miller, T. S. Reese, and A. Dosemeci. "Calcium/calmodulin-dependent protein kinase II clusters in adult rat hippocampal slices." Neuroscience 115, no. 2 (December 2002): 435–40. http://dx.doi.org/10.1016/s0306-4522(02)00451-7.

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Yang, Eungyeong, and Howard Schulman. "Structural Examination of Autoregulation of Multifunctional Calcium/Calmodulin-dependent Protein Kinase II." Journal of Biological Chemistry 274, no. 37 (September 10, 1999): 26199–208. http://dx.doi.org/10.1074/jbc.274.37.26199.

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Sun, Xiu Xia, James J. L. Hodge, Yi Zhou, Maidung Nguyen, and Leslie C. Griffith. "TheeagPotassium Channel Binds and Locally Activates Calcium/Calmodulin-dependent Protein Kinase II." Journal of Biological Chemistry 279, no. 11 (December 29, 2003): 10206–14. http://dx.doi.org/10.1074/jbc.m310728200.

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Moriguchi, Shigeki. "Pharmacological Study on Alzheimer’s Drugs Targeting Calcium/Calmodulin-Dependent Protein Kinase II." Journal of Pharmacological Sciences 117, no. 1 (2011): 6–11. http://dx.doi.org/10.1254/jphs.11r06cp.

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Wang, Zheng, Gisela F. Wilson, and Leslie C. Griffith. "Calcium/Calmodulin-dependent Protein Kinase II Phosphorylates and Regulates theDrosophilaEag Potassium Channel." Journal of Biological Chemistry 277, no. 27 (April 29, 2002): 24022–29. http://dx.doi.org/10.1074/jbc.m201949200.

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Shen, K., M. N. Teruel, J. H. Connor, S. Shenolikar, and T. Meyer. "Molecular memory by reversible translocation of calcium/calmodulin-dependent protein kinase II." Nature Neuroscience 3, no. 9 (September 2000): 881–86. http://dx.doi.org/10.1038/78783.

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Fang, Li, Jing Wu, Qing Lin, and William D. Willis. "Calcium–Calmodulin-Dependent Protein Kinase II Contributes to Spinal Cord Central Sensitization." Journal of Neuroscience 22, no. 10 (May 15, 2002): 4196–204. http://dx.doi.org/10.1523/jneurosci.22-10-04196.2002.

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Calman, B. G., A. W. Andrews, H. M. Rissler, S. C. Edwards, and B. A. Battelle. "Calcium/calmodulin-dependent protein kinase II and arrestin phosphorylation in Limulus eyes." Journal of Photochemistry and Photobiology B: Biology 35, no. 1-2 (August 1996): 33–44. http://dx.doi.org/10.1016/1011-1344(96)07312-5.

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Aronowski, Jaroslaw, M. Neal Waxham, and James C. Grotta. "Neuronal Protection and Preservation of Calcium/Calmodulin-Dependent Protein Kinase II and Protein Kinase C Activity by Dextrorphan Treatment in Global Ischemia." Journal of Cerebral Blood Flow & Metabolism 13, no. 4 (July 1993): 550–57. http://dx.doi.org/10.1038/jcbfm.1993.72.

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This study analyzed the ability of the N-methyl-d-aspartate receptor antagonist dextrorphan (DX) to prevent neuronal degeneration (analyzed by light microscopy), calmodulin (CaM) redistribution (analyzed by immunocytochemistry) and changes in activity of two major Ca2+-dependent protein kinases—calcium/calmodulin-dependent protein kinase II (CaM-KII) and protein kinase C (PKC) (analyzed by specific substrate phosphorylation) after 20 min of global ischemia (four-vessel occlusion model) in rats. DX treatment before and after ischemia significantly protected hippocampal and cortical neurons from neurodegeneration whereas DX posttreatment alone did not have any effect on preservation of neuronal morphology as compared with placebo treatment analyzed 72 h after 20 min of ischemia. Similarly to histological changes, DX exhibited protection against redistribution of CaM observed after ischemia. These changes were detected both in hippocampus as well as in cerebral cortex. Finally, DX administered before ligation of the carotid arteries reduced loss in both CaM-KII and PKC activity evoked by ischemia.

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