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Relevant bibliographies by topics / Calcium/calmodulin-dependent protein kinase II

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Academic literature on the topic 'Calcium/calmodulin-dependent protein kinase II'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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

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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Calcium/calmodulin-dependent protein kinase II"

1

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

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

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3

He, Beixin Julie. "Calcium and calmodulin dependent protein kinase II hyperactivity in cardiac remodeling." Diss., University of Iowa, 2012. https://ir.uiowa.edu/etd/2516.

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

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

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

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BEAUMAN, SHIRELYN RAE. "THE FUNCTION OF CALCIUM/CALMODULIN DEPENDENT PROTEIN KINASE II IN CELL CYCLE REGULATION." University of Cincinnati / OhioLINK, 2003. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1054300335.

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Novak, Gabriela. "Schizophrenia, elevated mRNA for calcium/calmodulin-dependent protein kinase II ß in frontal cortex." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2001. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp05/MQ63175.pdf.

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Haus, Jacob M. "AMP-activated protein kinase (AMPK) and calcium/calmodulin-dependent protein kinase II (CAMKII) activation in exercising human skeletal muscle." Virtual Press, 2004. http://liblink.bsu.edu/uhtbin/catkey/1294245.

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8

Wenham, Robert M. (Robert Michael). "Evidence for a role of the multifunctional calcium/calmodulin-dependent protein kinase II in insulin secretion." Thesis, North Texas State University, 1993. https://digital.library.unt.edu/ark:/67531/metadc798159/.

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Calcium/calmodulin-dependent protein kinase II (CaM kinase II) is demonstrated to exist in the ß-cell and immunopecipitation. Glucose and potassium significantly stimulate the rapid autophosphorylation of CaM kinase II and proportionally induce autonomous activity of the kinase in a dose-dependent manner that parallels insulin secretion. The activation of CaM kinase II, alloxan, KN-62 and KN-93, suggest that the enzyme is an integral component of insulin secretion and/or related processes in the β-cell.

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9

Breen, Maria Adrienne. "Molecular characterisation of the calcium/calmodulin-dependent protein kinase II of human islets of Langerhans." Thesis, University of Oxford, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.337543.

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Mooney, Laura. "Development of a small animal of cardiac contractility and calcium/calmodulin-dependent protein kinase II." Thesis, University of Strathclyde, 2012. http://oleg.lib.strath.ac.uk:80/R/?func=dbin-jump-full&object_id=18577.

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Several drugs in development or on the market have adverse effects on cardiac contractility. Calcium/calmodulin-dependent protein kinase IIδ (CaMKIIδ) is an important regulator of cardiac contractility with a particularly prominent role in pathophysiological conditions where contractile dysfunction occurs. Therefore, CaMKIIδ may be an intracellular target for drugs that alter cardiac performance. The aim of the work presented in this thesis was to develop a small animal model for the integrated assessment of cardiac contractility and CaMKII. An anaesthetised guinea pig model was developed to assess haemodynamics and cardiac contractility via two indices - left ventricular (LV) dP/dtmax and the QA interval. Acute administration of isoprenaline and ouabain increased contractility whilst verapamil, imatinib and sunitinib decreased contractility. There was a strong inverse correlation between LVdP/dtmax and the QA interval. CaMKIIδ expression and CaMKII activity were not significantly altered by any acute drug treatment. Both LVdP/dtmax and the QA interval were influenced by changes in blood pressure. Additionally, LVdP/dtmax was influenced by changes in heart rate. Measurement of contractility via LV pressure-volume loops was also assessed. Surgical approaches and recordings were optimised and isoprenaline and verapamil had positive and negative inotropic actions, respectively. Several issues were identified which require further attention. Chronic administration of isoprenaline and verapamil decreased cardiac contractility and increased CaMKIIδ expression and CaMKII activity. Chronic imatinib and sunitinib treatments did not alter cardiac contractility significantly. However, both CaMKIIδ expression and CaMKII activity were increased. The work presented in this thesis indicates that the guinea pig is suitable for the integrated assessment of cardiac contractility and CaMKII. Alterations in CaMKIIδ expression and CaMKII activity following chronic drug treatments could be an indication of cellular cardiotoxicity associated with contractile dysfunction at the whole animal level. The circumstances under which increased CaMKII expression and activity translate to compromised contractile performance require more detailed investigation.

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Books on the topic "Calcium/calmodulin-dependent protein kinase II"

1

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

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2

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

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

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4

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

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Book chapters on the topic "Calcium/calmodulin-dependent protein kinase II"

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

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2

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

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

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

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Hetherington, A. M., D. Blowers, and A. Trewavas. "Calcium/Calmodulin Dependent Membrane Bound Protein Kinase." In Molecular and Cellular Aspects of Calcium in Plant Development, 123–30. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2177-4_16.

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Vallano, Mary Lou, James R. Goldenring, and Robert J. Delorenzo. "Calcium- and Calmodulin- Dependent Protein Kinase: Role in Memory." In Neural Mechanisms of Conditioning, 383–96. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2115-6_27.

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

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

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

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

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Conference papers on the topic "Calcium/calmodulin-dependent protein kinase II"

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

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

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Ming Wu and Douglas A. Lawrence. "Monotonicity and bistability of calcium/calmodulin-dependent protein kinase-phosphatase activation." In 2010 American Control Conference (ACC 2010). IEEE, 2010. http://dx.doi.org/10.1109/acc.2010.5531229.

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

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

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

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

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