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Insulin Signaling Modulates Neuronal Metabolism
Published in André Kleinridders, Physiological Consequences of Brain Insulin Action, 2023
Qian Huang, Jialin Fu, Kelly Anne Borges, Weikang Cai
Insulin is known to regulate glycogen metabolism via phosphorylation events on GSK3- glycogen synthase (GS) signaling cascade (97). However, whether insulin may directly affect glycogen metabolism in neurons through the same signaling pathways is not clear, due to the technical difficulties to assess neuronal glycogen storage in vivo. Nevertheless, insulin can regulate neuronal metabolism indirectly by regulating astrocytic glycogen breakdown. Thus, in response to the increase in energy demand by neurons, insulin inhibits norepinephrine uptake by neurons, resulting in the activation of the β-adrenoreceptors on astrocytes and stimulation of glucose extrusion from glycogen in astrocytes (98, 99).
Antioxidant Phytochemicals and Alzheimer’s Disease
Published in Atanu Bhattacharjee, Akula Ramakrishna, Magisetty Obulesu, Phytomedicine and Alzheimer’s Disease, 2020
Saikat Sen, Raja Chakraborty, Atanu Bhattacharjee
Luteolin is a well-known flavonoid which has been investigated widely for its beneficial effects on the CNS. Luteolin was found to enhance brain-derived neurotrophic factor (BDNF), synapsin I, and postsynaptic density protein 95 in the brains of obese mice, and to avert neuronal apoptosis. Luteolin also inhibits neuroinflammation by inhibiting the production of inflammatory markers. Luteolin reduces the activation of GSK-3, that also causes reduced levels of Aβ in the cerebral cortex of experimental animals. Luteolin also downregulates expression of BACE1 and NF-κB, the latter being key to a proinflammatory signaling pathway, followed by removal of Aβ peptides from the cerebral cortex and hippocampus. Luteolin reduces TNFα-induced inflammation through decreasing NF-κB and activator protein 1. Luteolin was found to inhibit activities of IL-6, IL-1β, COX-2, TNFα, and interferon gamma and to decrease activity of cholinesterase in the cortex and the hippocampus area of obese mice. Luteolin exerted strong antioxidant activity that may also contribute to its neuroprotective effect in AD (Kwon, 2017).
Antimanic Drugs
Published in Sahab Uddin, Rashid Mamunur, Advances in Neuropharmacology, 2020
Aman Upaganlawar, Abdulla Sherikar, Chandrashekhar Upasani
It is a serine/threonine kinase residue which is constitutively active in cells and is disabled by signals originating from numerous signaling pathways such as protein kinase C. GSK-3 signaling plays a significant role in bipolar disorder and the chemicals such as expression serotonin, dopamine, antidepressants, and psychostimulants act as GSK-3 signaling regulators. An augmented expression of GSK-3 acts as a pro-apoptotic, on the other hand, GSK-3 inhibitors prevents apoptosis. GSK-3 signaling cascade produces both antimanic and antidepressant effects in models of depression or mania. In patients with bipolar disorder, the genetic variations in GSK-3 signaling causes sleep deprivation which varies in age related response (Carlos et al., 2006).
The Occurrence of Valvular Atrial Fibrillation: Involvement of NGF/TrKA Signaling Pathway
Published in Journal of Investigative Surgery, 2021
Qianli Wang, Yong Zhao, Xin Dong, Cong Li, Lin Zhou, Chengwei Zou, Xiaodong Li, Nannan Zhou, Junni Liu, Yuanyuan Sun, Jianchun Wang
GSK3β expression in patients with valvular AF was significantly reduced. Combined with the changes of phosphorylation level, we supposed that GSK3β was involved in the occurrence of valvular AF. Meanwhile, the inactivation of GSK3β in patients with valvular AF may not be through phosphorylation. GSK-3 is a serine/threonine kinase, regulates multiple cellular functions, consists of two similar isoforms (α, β). Previous study revealed that GSK-3β is an endogenous negative regulator of cardiac hypertrophy [32]. GSK-3β activity is regulated by both phosphorylation-dependent and -independent mechanisms. Phosphorylation of GSK-3β occurs at two sites: serine 9 (Ser 9) and serine 389 (Ser 389). Akt, an upstream kinase, can induce the phosphorylation of the Ser 9 residue of GSK-3β, which blocks the entry of substrates to the GSK-3β catalytic domain. GSK-3β could be suppressed through Ser 389 phosphorylation by p38-MAPK [33]. It has also been proved that p-Ser 21/Ser 9 in GSK-3β may not be necessary for cardiac hypertrophy [34]. Therefore, the reduction of phosphorylated AKT and GSK3β does not negate the role of GSK3β in patients with valvular AF.
GAS5, a FoxO1-actived long noncoding RNA, promotes propofol-induced oral squamous cell carcinoma apoptosis by regulating the miR-1297-GSK3β axis
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2019
Chengshun Gao, Chunmei Ren, Zhongxi Liu, Li Zhang, Ranran Tang, Xiaojie Li
Accumulating studies have revealed that miR-1297 plays an important role in cancer. MiR-1297 was reported to suppress tumourigenesis in most cancers, including lung cancer, colorectal cancer, and prostate cancer [31–33]. However, we found that GSK3β is a novel target gene of miR-1297. GSK3β and GSK3α are two isoforms of GSK3, which are encoded by separate genes. GSK3 is a serine/threonine kinase, and thus transfers a phosphate group to either the serine or threonine residues of its substrates [34]. Phosphorylation of GSK3β at ser9 and GSK3α at ser 21 render their inactive [35,36]. Interestingly, we found that phosphorylation of GSK3β at ser9 and GSK3α ser 21 were not altered in response to propofol treatment. Only GSK3β was increased under propofol treatment in OSCC cells, which may own to the miR-1297 decrease by propofol. Thus, our data indicated that downregulation of miR-1297 by propofol enhances GSK3β expression and decreases Mcl1 protein levels.
Glucocorticoid exposure causes disrupted glucoregulation, cardiac inflammation and elevated dipeptidyl peptidase-4 activity independent of glycogen synthase kinase-3 in female rats
Published in Archives of Physiology and Biochemistry, 2019
Olufunto O. Badmus, Lawrence A. Olatunji
Glycogen synthase kinase-3 (GSK-3) is a multi-tasking and housekeeping serine/threonine kinase that has widespread influences on many cellular functions. It plays an important role in energy metabolism. GSK-3 constitutes part of the insulin signalling pathway, and it has been implicated in the pathogenesis of IR and diabetes mellitus (Nikoulina et al. 2000, Guo et al. 2016). It has also been discovered that GSK-3 promotes inflammation which supports its well-documented actions in several critical diseases which involve inflammation such as diabetes mellitus, mood disorders, Alzheimer’s disease and cancer (Jope et al. 2007). Nevertheless, there have been conflicting documents on the role of GSK-3 in GC-induced IR. Since earlier studies have revealed that GC treatment is relatively linked to IR and increased risk of cardiac inflammation, we therefore sought to determine whether DPP-4 activity and GSK-3 would be involved in glucose homeostasis disruption and cardiac inflammation following GC exposure in female rats.