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Stimulus-Secretion Coupling: Intracellular Proteins and Nucleotides
Published in Stephen W. Carmichael, Susan L. Stoddard, The Adrenal Medulla 1986 - 1988, 2017
Stephen W. Carmichael, Susan L. Stoddard
Okumura-Noji, Kato and Tanaka (1986) examined the calcium-dependent phosphorylation of proteins in PC12 cells. They found that a group of proteins ranging from 50 kDa to 55 kDa and a 95 kDa protein were phosphorylated. Calcium/calmodulin-dependent protein kinase appeared to be responsible for the phosphorylation of the 50 kDa to 55 kDa proteins and, partly, of the 95 kDa protein. Depolarization of intact PC12 cells by potassium induced phosphorylation of the 95 kDa protein.
Mechanisms of inflammatory hyperalgesia
Published in Pamela E Macintyre, Suellen M Walker, David J Rowbotham, Clinical Pain Management, 2008
Calcium/calmodulin-dependent protein kinase (CaMKII) is involved in activity-induced synaptic changes throughout the CNS.41 CaMKII is expressed in small diameter DRG neurons, and in lamina I and II neurons in the dorsal horn.67 Activation of CaMKII enhances AMPA and NMDA inward currents,43 but the role of CaMKII in pain processing and central sensitization may vary depending on the intensity of the stimulus and the type of injury. Capsaicin injection has been shown to increase expression and phosphorylation of CaMKII in DH neurons, and enhance phosphorylation of AMPA GluR1 subunits.68 Experiments in mice with a mutation that prevents autophosphorylation of the enzyme suggest that activated CaMKII is not required for stimulus-evoked threshold changes after injury (i.e. no difference is seen between mutant and wildtype mice in mechanical and thermal thresholds after CFA), but it is necessary for the persistence of spontaneous pain behavior in the setting of tissue injury (e.g. reduction in second-phase formalin injection).67
Pathophysiology of Complex Regional Pain Syndrome
Published in Gary W. Jay, Practical Guide to Chronic Pain Syndromes, 2016
Glutamatergic AMPA receptors (GluR2/3 subunits) mediate fast pain (A-delta fiber) that is experienced after acute injury (63). A major component of synaptic plasticity of PTNs is due to the number and conductance of AMPA receptors in the postsynaptic membrane, which is dependent on synaptic NMDA modulation (64). A critical process in the induction and maintenance of LTP and LTD of PTNs is dependent upon the concentration and spatial and temporal influx of calcium through the NMDA receptor. These factors determine either the aggregation (LTP) or dispersal (LTD) of AMPA receptors at the postsynaptic membrane (65). Intracellular calcium-calmodulin—dependent protein kinase II is critical for LTP by providing anchoring sites for AMPA receptors and increasing their conductance (66). Regulatory and enhancing proteins located in the postsynaptic density control other important signaling cascades such as Rasmitogen-activated protein kinase and inositide 3-kinase during calcium influx (59,67,68)). Ras-mitogen-activated protein kinase expression regulates transcription factors such as cyclic adenosine 5’ monophosphate response element binding protein, which is one pathway for gene expression initiated by Ca2+ influx through NMPA receptors (50,69). Central (DH) and peripheral (C and A-delta fiber) sensitization is enhanced by the products of novel gene expression which lower the firing threshold of damaged C and A-delta fiber terminals at the site of injury and increase the sensitivity of PTNs in the DRG and DH. Failure of inhibitory circuitry in the DH may also contribute to central sensitization (62).
Molecular Mechanisms Associated with the Benefits of Variable Practice in Motor Learning
Published in Journal of Motor Behavior, 2020
Tércio Apolinário-Souza, Ana Flávia Santos Almeida, Natália Lelis-Torres, Juliana Otoni Parma, Grace Schenatto Pereira, Guilherme Menezes Lage
The synchronous activity of the pre- and post-synaptic neurons is associated with the activity of the n-methyl-d-aspartate (NMDA) receptor, an ionotropic glutamate receptor (Tabone & Ramaswami, 2012), since the opening of its ionic channels is dependent on the coincident activity of the pre- and post-synaptic neurons (Harms, Rioult-Pedotti, Carter, & Dunaevsky, 2008; Riedel, Platt, & Micheau, 2003; Rioult-Pedotti, Friedman, & Donoghue, 2000). This occurs when the post-synaptic membrane is in its resting potential and the NMDA channels are closed and blocked by a magnesium ion (Mg2+), preventing the influx of calcium ions (Ca2+) to the post-synaptic terminal (Mayer, Westbrook, & Guthrie, 1984). The bonding of glutamate in the NMDA receptor is insufficient to activate the Ca2+ channels. Two coincident actions are necessary to the opening of the channels: (1) increased release of the pre-synaptic glutamate and (2) post-synaptic depolarization (Nowak, Bregestovski, Ascher, Herbet, & Prochiantz, 1984; Tabone & Ramaswami, 2012). The influx of Ca2+ through the NMDA receptor acts as an important postsynaptic second messenger, activating many intracellular signaling (Cooke & Bliss, 2006). For instance, Ca2+ binds with calmodulin, activating kinase proteins such as the calcium/calmodulin-dependent protein kinase II (CaMKII) (Nicoll, 2017). One of the roles of the CAMKII is to promote the insertion of alfa-amino-3-hydroxy-5-methyl-4-isoxazolepropionic (AMPA) receptors in the post-synaptic membrane, another ionotropic glutamate receptor (Rumpel, Ledoux, Zador, & Malinow, 2007). The strengthening of the synaptic connections is a result of the insertion of novel AMPA receptors (Lu et al., 2001).
Role of the endogenous cannabinoid receptor 1 in brain injury induced by chronic intermittent hypoxia in rats
Published in International Journal of Neuroscience, 2018
Xiaoling Gao, Shujie Wu, Yanting Dong, Yaqiong Huang, Yan Chen, Yan Qiao, Zhanjun Dou, Bei Wang
Calcium/calmodulin-dependent protein kinase II (CaMKII), an enzyme found in high quantities in the brain, including presyanptic membranes in the hippocampus [15], has an important role in learning and memory function [16]. Thus, CaMKII may represent an important cause of CIH-induced hippocampal damage. However, it is unknown whether CB1 and CaMKII play a role on brain structure abnormalities and cognitive dysfunction induced by CIH. Thus, the present study will establish a CIH model and determine if the ECS protects against brain tissue damage and study its mechanisms.
CaMKII may regulate renal tubular epithelial cell apoptosis through YAP/NFAT2 in acute kidney injury mice
Published in Renal Failure, 2023
Zongshun Huang, Yonghua Peng, Guibao Ke, Yun Xiao, Yaqi Chen
Calcium/calmodulin-dependent protein kinase II (CaMKII) is a ubiquitously expressed multifunctional serine/threonine kinase that plays a critical role in cell apoptosis [4–6]. CaMKII pharmacological inhibition and genetic deletion protect against endoplasmic reticulum stress-induced cardiomyocyte apoptosis [7]. Furthermore, CaMKII overexpression enhances iohexol-induced mitochondrial damage and RTEC apoptosis [4]. However, it remains unclear whether CaMKII participates in the pathogenesis of RTEC apoptosis in AKI.