Log in

Relevant bibliographies by topics / GSK-3beta / Journal articles

To see the other types of publications on this topic, follow the link: GSK-3beta.

Journal articles on the topic 'GSK-3beta'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'GSK-3beta.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Sun, Yi, Lu Yang, and Qiang Wei. "Protection of prostate cancer cells from GSK-3β-induced oxidative stress by Il-8 through activating the mTOR signaling pathway." Journal of Clinical Oncology 37, no. 7_suppl (March 1, 2019): 311. http://dx.doi.org/10.1200/jco.2019.37.7_suppl.311.

Full text

Abstract:

311 Background: Both oxidative stress and inflammation play important roles in prostate cancer cell apoptosis or proliferation. However, the mechanisms underlying these processes remain unclear. Thus, we chose IL-8 as the bridge between inflammation and cancer cell oxidative stress-induced death and confirmed its connection with mTOR and GSK-3beta. Methods: We overexpressed GSK-3beta and observed the effect of GSK-3beta on reactive oxygen species (ROS) and cell death induced by oxidative stress. Then, IL-8 was upregulated or downregulated to determine its impact on preventing cells from damage by GSK-3beta-induced oxidative stress. In addition, we confirmed the role of mTOR in this process through its overexpression or knockdown. Real-time PCR, Western blotting, transcription, Cell Counting Kit 8, flow cytometry and other techniques were used. Results: IL-8 promotes prostate cancer cell proliferation and decreases apoptosis, while GSK-3beta induces cell death by oxidative stress through the activation of the caspase-3 signaling pathway by increasing ROS. In addition, mTOR can also decrease the activation of the caspase-3 signaling pathway by inhibiting GSK--3beta and thus decreasing ROS production. Moreover, the inhibitory effect of IL-8 on GSK-3beta occurs through the regulation of mTOR. Conclusions: The results of this study highlight the importance of GSK-3beta, which increases the production of ROS and then induces oxidative stress in tumor cells, while IL-8 and mTOR attenuate the oxidative stress to protect prostate cancer cells through the inhibitor GSK-3beta.

APA, Harvard, Vancouver, ISO, and other styles

2

Lucas, F. R., R. G. Goold, P. R. Gordon-Weeks, and P. C. Salinas. "Inhibition of GSK-3beta leading to the loss of phosphorylated MAP-1B is an early event in axonal remodelling induced by WNT-7a or lithium." Journal of Cell Science 111, no. 10 (May 15, 1998): 1351–61. http://dx.doi.org/10.1242/jcs.111.10.1351.

Full text

Abstract:

WNT-7a induces axonal spreading and branching in developing cerebellar granule neurons. This effect is mediated through the inhibition of GSK-3beta, a serine/threonine kinase and a component of the WNT pathway. Lithium, an inhibitor of GSK-3beta, mimics WNT-7a in granule cells. Here we examined further the effect of GSK-3beta inhibition on cytoskeletal re-organisation. Lithium induces axonal spreading and increases growth cone area and perimeter. This effect is associated with the absence or reduction of stable microtubules in spread areas. Lithium induces the loss of a phosphorylated form of MAP-1B, a microtubule associated protein involved in axonal outgrowth. Down-regulation of the phosphorylated MAP-1B, MAP-1B-P, from axonal processes occurs before axonal remodelling is evident. In vitro phosphorylation assays show that MAP-1B-P is generated by direct phosphorylation of MAP-1B by GSK-3beta. WNT-7a, like lithium, also leads to loss of MAP-1B-P from spread axons and growth cones. Our data suggest that WNT-7a and lithium induce changes in microtubule dynamics by inhibiting GSK-3beta which in turn lead to changes in the phosphorylation of MAP-1B. These findings suggest a novel role for GSK-3beta and WNTs in axonal remodelling and identify MAP-1B as a new target for GSK-3beta and WNT.

APA, Harvard, Vancouver, ISO, and other styles

3

Fisher, D. L., N. Morin, and M. Doree. "A novel role for glycogen synthase kinase-3 in Xenopus development: maintenance of oocyte cell cycle arrest by a beta-catenin-independent mechanism." Development 126, no. 3 (February 1, 1999): 567–76. http://dx.doi.org/10.1242/dev.126.3.567.

Full text

Abstract:

We have examined the expression of glycogen synthase kinase-3beta in oocytes and early embryos of Xenopus and found that the protein is developmentally regulated. In resting oocytes, GSK-3beta is active and it is inactivated on maturation in response to progesterone. GSK-3beta inactivation is necessary and rate limiting for the cell cycle response to this hormone and the subsequent accumulation of beta-catenin. Overexpression of a dominant negative form of the kinase accelerates maturation, as does inactivation by expression of Xenopus Dishevelled or microinjection of an inactivating antibody. Cell cycle inhibition by GSK-3beta is not mediated by the level of beta-catenin or by a direct effect on either the MAP kinase pathway or translation of mos and cyclin B1. These data indicate a novel role for GSK-3beta in Xenopus development: in addition to controlling specification of the dorsoventral axis in embryos, it mediates cell cycle arrest in oocytes.

APA, Harvard, Vancouver, ISO, and other styles

4

Strekalova, Tatyana, Nataliia Markova, Elena Shevtsova, Olga Zubareva, Anastassia Bakhmet, Harry M. Steinbusch, Sergey Bachurin, and Klaus-Peter Lesch. "Individual Differences in Behavioural Despair Predict Brain GSK-3beta Expression in Mice: The Power of a Modified Swim Test." Neural Plasticity 2016 (2016): 1–17. http://dx.doi.org/10.1155/2016/5098591.

Full text

Abstract:

While deficient brain plasticity is a well-established pathophysiologic feature of depression, little is known about disorder-associated enhanced cognitive processing. Here, we studied a novel mouse paradigm that potentially models augmented learning of adverse memories during development of a depressive-like state. We used a modification of the classic two-day protocol of a mouse Porsolt test with an additional session occurring on Day 5 following the initial exposure. Unexpectedly, floating behaviour and brain glycogen synthase kinase-3 beta (GSK-3beta) mRNA levels, a factor of synaptic plasticity as well as a marker of distress and depression, were increased during the additional swimming session that was prevented by imipramine. Observed increases of GSK-3beta mRNA in prefrontal cortex during delayed testing session correlated with individual parameters of behavioural despair that was not found in the classic Porsolt test. Repeated swim exposure was accompanied by a lower pGSK-3beta/GSK-3beta ratio. A replacement of the second or the final swim sessions with exposure to the context of testing resulted in increased GSK-3beta mRNA level similar to the effects of swimming, while exclusion of the second testing prevented these changes. Together, our findings implicate the activation of brain GSK-3beta expression in enhanced contextual conditioning of adverse memories, which is associated with an individual susceptibility to a depressive syndrome.

APA, Harvard, Vancouver, ISO, and other styles

5

Dao, Kim-Hien T., Michael D. Rotelli, Jane E. Yates, Brieanna Brown, Juha Rantala, Keaney Rathbun, Jeffrey W. Tyner, Brian J. Druker, and Grover C. Bagby. "Regulation of FANCL by Glycogen Synthase Kinase-3beta Links the Fanconi anemia pathway to Self Renewal and Survival Signals." Blood 120, no. 21 (November 16, 2012): 1263. http://dx.doi.org/10.1182/blood.v120.21.1263.1263.

Full text

Abstract:

Abstract Abstract 1263 The molecular basis for how a Fanconi anemia (FA) genetic background contributes to hematopoietic stem cell defects and hypoplastic organ development remains poorly understood. Protein modification by ubiquitination is a mechanism that diversifies the function and regulation of proteins. In light of this, we focus on the dysfunction of FANCL, the E3 ubiquitin ligase of the FA pathway, as a key molecular defect in Fanconi anemia. Here we report our studies investigating mechanisms of post-translational regulation of FANCL. We view these mechanisms as potential targets to augment the function of the FA core complex and correct hematopoietic stem cell defects. We provide evidence that FANCL is exquisitely regulated by ubiquitin-proteosome degradation. Ligase-inactive mutants (FANCL-C307A and -W341G) are less sensitive to this regulation, suggesting a role for auto-ubiquitination in directing lysine-48 polyubiquitination. This constitutive negative regulation of FANCL is partially reversed with an ATP-competitive glycogen synthase kinase-3beta (GSK-3beta) inhibitor. GSK-3beta is a serine/threonine kinase that phosphorylates proteins and marks them for ubiquitin-mediated proteolysis. Mitogenic and survival pathways, including Ras/MAPK and PI3K/Akt, negatively regulate GSK-3beta by serine-9 phosphorylation. We show that the regulation of FANCL by GSK-3beta is likely direct because FANCL and GSK-3beta co-immunoprecipitate in cell lysates and as GST-fusion proteins. To define the biochemical mechanisms of FANCL regulation, we generated N-terminal deletion mutants of FANCL and we show that the regulation of FANCL is dictated by a region at the N-terminus (aa1-78). Mutational analysis of FANCL (lysine to arginine) in this N-terminus region does not affect the overall protein level or ubiquitination of FANCL, suggesting that FANCL may be targeted for degradation by phosphorylation and/or in a complex with other proteins. The potential biological relevance of our findings, that FANCL is regulated by GSK-3beta is revealed in studies overexpressing constitutively active, myristoylated-Akt. This experimental condition increases FANCL protein levels and suggests a role for FANCL as a downstream effector of PI3K/Akt signaling. In turn, FANCL likely regulates non-canonical targets that alter the transcriptome profile favoring self-renewal and survival of hematopoietic stem cells. We recently published our studies identifying beta-catenin as one such downstream target (Blood 2012 Jul 12;120:323). Suppression of FANCL expression severely disrupts Wnt/beta-catenin signaling and expression of downstream Wnt-responsive targets MYC and CCND1. We also identified that GSK3B gene expression is approximately 5-fold higher in Fancc-deficient hematopoietic stem cells exposed to TNF-alpha compared to untreated cells or to wildtype cells with or without TNF-alpha. Our current studies show that inhibition of GSK-3beta preserves the number of murine Fancc-deficient hematopoietic stem cells exposed to TNF-alpha compared with no GSK-3beta inhibition. Taken together, we have accumulated evidence suggesting that GSK-3beta is a promising molecular target to improve the self-renewal and survival of FA hematopoietic stem cells. Disclosures: No relevant conflicts of interest to declare.

APA, Harvard, Vancouver, ISO, and other styles

6

Lemoine, Sandrine, Lan Zhu, Gallic Beauchef, Olivier Lepage, Gérard Babatasi, Caline Ivascau, Massimo Massetti, Philippe Galera, Jean-Louis Gérard, and Jean-Luc Hanouz. "Role of 70-kDa Ribosomal Protein S6 Kinase, Nitric Oxide Synthase, Glycogen Synthase Kinase-3β, and Mitochondrial Permeability Transition Pore in Desflurane-induced Postconditioning in Isolated Human Right Atria." Anesthesiology 112, no. 6 (June 1, 2010): 1355–63. http://dx.doi.org/10.1097/aln.0b013e3181d74f39.

Full text

Abstract:

Background Desflurane during early reperfusion has been shown to postcondition human myocardium. Whether it involves "reperfusion injury salvage kinase" pathway remains incompletely studied. The authors tested the involvement of 70-kDa ribosomal protein S6 kinase, nitric oxide synthase, glycogen synthase kinase (GSK)-3beta, and mitochondrial permeability transition pore in desflurane-induced postconditioning. Methods The authors recorded isometric contraction of human right atrial trabeculae suspended in an oxygenated Tyrode's solution (34 degrees C, stimulation frequency 1 Hz). After a 30-min hypoxic period, desflurane 6% was administered during the first 5 min of reoxygenation. Desflurane was administered alone or with pretreatment of rapamycin, a 70-kDa ribosomal protein S6 kinase inhibitor, NG-nitro-L-arginine methyl ester, a nitric oxide synthase inhibitor, and atractyloside, the mitochondrial permeability transition pore opener. GSK-3beta inhibitor VII was administered during the first few minutes of reoxygenation alone or in the presence of desflurane 6%, rapamycin, NG-nitro-L-arginine methyl ester, and atractyloside. Developed force at the end of a 60-min reoxygenation period was compared (mean +/- SD). Phosphorylation of GSK-3beta was measured using blotting. Results Desflurane 6% (84 +/- 4% of baseline) enhanced the recovery of force after 60 min of reoxygenation when compared with the control group (54 +/- 4%, P < 0.0001). Rapamycin (68 +/- 8% of baseline), NG-nitro-L-arginine methyl ester (57 +/- 8%), atractyloside (52 +/- 7%) abolished desflurane-induced postconditioning (P < 0.001). GSK-3beta inhibitor-induced postconditioning (84 +/- 5%, P < 0.0001 vs. control) was not modified by desflurane (78 +/- 6%), rapamycin (81 +/- 6%), and NG-nitro-L-arginine methyl ester (82 +/- 10%), but it was abolished by atractyloside (49 +/- 6%). Desflurane increased the phosphorylation of GSK-3beta (3.30 +/- 0.57-fold increase in desflurane vs. control; P < 0.0001). Conclusions In vitro, desflurane-induced postconditioning protects human myocardium through the activation of 70-kDa ribosomal protein S6 kinase, nitric oxide synthase, inhibition, and phosphorylation of GSK-3beta, and preventing mitochondrial permeability transition pore opening.

APA, Harvard, Vancouver, ISO, and other styles

7

Lin, Xiao, and Yu Li. "Mechanisms of Plant Polyphenol Genistein on Regulation of EMT in Ovarian Carcinoma." Advanced Materials Research 1120-1121 (July 2015): 803–6. http://dx.doi.org/10.4028/www.scientific.net/amr.1120-1121.803.

Full text

Abstract:

More and more studies have reported that epithelial-mesenchymal translation (EMT) plays key roles not only on genesis, development and metastasis, but also on drug-resistance of chemotherapy of tumor. Meanwhile, the fact that beta-catenin transfer from membrance and cytoplasm to nucleus is major steps in process of EMT [1]. Research found that Genistein would suppress Wnt/beta-catenin signal pathway though inhibiting beta-catenin translation [2]. Furthermore, our research showed that Genistein could decrease the expression of GSK-3beta in ovarian carcinoma cell SKOV3. Beta-catenin and GSK-3beta are important factors of EMT, which indicated that Genistein would regulate EMT signal pathway through beta-catenin and GSK-3beta, but the mechanism is not clear. So, there has been great interest in understanding the molecular mechanisms on the effect of Genistein.

APA, Harvard, Vancouver, ISO, and other styles

8

Ray, L. B. "Hsp90 Controls GSK-3beta Kinase Specificity." Science's STKE 2006, no. 362 (November 14, 2006): tw395. http://dx.doi.org/10.1126/stke.3622006tw395.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Lin, Fei-xiang, Gui-zhou Zheng, Bo Chang, Rong-chun Chen, Qi-hao Zhang, Peng Xie, Da Xie, et al. "Connexin 43 Modulates Osteogenic Differentiation of Bone Marrow Stromal Cells Through GSK-3beta/Beta-Catenin Signaling Pathways." Cellular Physiology and Biochemistry 47, no. 1 (2018): 161–75. http://dx.doi.org/10.1159/000489763.

Full text

Abstract:

Background/Aims: Bone marrow stromal cells (BMSCs) are multipotent precursors that give rise to osteoblasts, and contribute directly to bone formation. Connexin 43 (Cx43) is the most ubiquitous gap junction protein expressed in bone cell types, and plays crucial roles in regulating intercellular signal transmission for bone development, differentiation and pathology. However, the precise role and mechanism of Cx43 in BMSCs are less known. Here, we investigate the function of Cx43 in osteogenic differentiation of BMSCs in vitro. Methods: BMSCs were isolated by whole bone marrow adherent culture. Knock down of Cx43 was performed by using lentiviral transduction of Cx43 shRNA. BMSCs were induced to differentiate by culturing in a-MEM, 10% FBS, 50 µM ascorbic acid, 10 mM beta-glycerophosphate, and 100 nM dexamethasone. Alkaline phosphatase (ALP) activity and alizarin red S staining were used to evaluate osteogenic differentiation in calcium nodules. Target mRNAs and proteins were analyzed by using real-time quantitative PCR (qPCR) and western blotting. Results: Cx43 expression markedly increased during osteogenic differentiation. Osteogenic differentiation was suppressed following lentiviral-mediated knockdown of Cx43 expression, as judged by decreased levels of Runt-related transcription factor 2 (Runx2), bone sialoprotein (BSP), osteocalcin (Bglap), Osterix (Osx), alkaline phosphatase (ALP) activity and the number of calcium nodules in response to osteogenic differentiation stimuli. Knock down of Cx43 reduced the level of phosphorylation of GSK-3beta at Ser9 (p-GSK-3beta), resulting in decreased beta-catenin expression and activation. Furthermore, treatment of Cx43-knockdown cells with lithium chloride (LiCl), a GSK-3beta inhibitor, reduced osteogenic differentiation and decreased GSK-3beta levels, as well as partially rescued levels of both total and activated beta-catenin. Conclusion: These findings indicate that Cx43 positively modulates osteogenic differentiation of BMSCs by up-regulating GSK-3beta/beta-catenin signaling pathways, suggesting a potential role for Cx43 in determining bone mass and bone mineral density by modulating osteogenesis.

APA, Harvard, Vancouver, ISO, and other styles

10

Cui, Dehua, Y. Yoshiike, J. M. Park, Y. L. Jin, M. Murayama, E. Planel, Y. Tatebayashi, and A. Takashima. "P3-245 Participation of GSK-3beta in neurodegeneration." Neurobiology of Aging 25 (July 2004): S424. http://dx.doi.org/10.1016/s0197-4580(04)81395-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

11

Ermak, Gennady, Cathryn D. Harris, Denis Battocchio, and Kelvin J. A. Davies. "RCAN1 (DSCR1 or Adapt78)* stimulates expression of GSK-3beta." FEBS Journal 273, no. 10 (May 2006): 2100–2109. http://dx.doi.org/10.1111/j.1742-4658.2006.05217.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

12

Wang, X. "3.339 OVEREXPRESSION OF HDAC2 ACTIVATED GSK-3BETA WITHOUT DIRECT INTERACTION." Parkinsonism & Related Disorders 18 (January 2012): S228. http://dx.doi.org/10.1016/s1353-8020(11)70972-5.

Full text

APA, Harvard, Vancouver, ISO, and other styles

13

Jaworski, Tomasz. "Control of neuronal excitability by GSK-3beta: Epilepsy and beyond." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1867, no. 9 (September 2020): 118745. http://dx.doi.org/10.1016/j.bbamcr.2020.118745.

Full text

APA, Harvard, Vancouver, ISO, and other styles

14

Twomey, Ciara M., and Justin V. McCarthy. "P3-400: Presenilin-1 is an unprimed GSK-3beta substrate." Alzheimer's & Dementia 2 (July 2006): S493. http://dx.doi.org/10.1016/j.jalz.2006.05.1670.

Full text

APA, Harvard, Vancouver, ISO, and other styles

15

Armagan, Güliz. "REGULATION OF NRF2/ARE PATHWAY THROUGH GSK-3BETA INHIBITION IN NEURODEGENERATION." Pathophysiology 25, no. 3 (September 2018): 186–87. http://dx.doi.org/10.1016/j.pathophys.2018.07.062.

Full text

APA, Harvard, Vancouver, ISO, and other styles

16

Kozlovsky, N. "Low GSK-3beta Immunoreactivity in Postmortem Frontal Cortex of Schizophrenic Patients." American Journal of Psychiatry 157, no. 5 (May 1, 2000): 831–33. http://dx.doi.org/10.1176/appi.ajp.157.5.831.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Zhang, Xiong, Lu Si, Yu Li, and Can Mi. "Expressions of GSK-3beta, Beta-catenin and PPAR-gamma in medulloblastoma." Chinese Journal of Cancer Research 21, no. 3 (August 11, 2009): 235–39. http://dx.doi.org/10.1007/s11670-009-0235-0.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Ikeda, S. "Axin, a negative regulator of the Wnt signaling pathway, forms a complex with GSK-3beta and beta -catenin and promotes GSK-3beta -dependent phosphorylation of beta -catenin." EMBO Journal 17, no. 5 (March 2, 1998): 1371–84. http://dx.doi.org/10.1093/emboj/17.5.1371.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Itoh, S., T. Saito, M. Hirata, M. Ushita, T. Ikeda, K. Nakamura, U. i. Chung, and H. Kawaguchi. "52 GSK-3ALPHA AND GSK-3BETA MODULATE EARLY STAGES OF CHONDROCYTE DIFFERENTIATION THROUGH PHOSPHORYLATION OF RELA/NF-KAPPAB P65." Osteoarthritis and Cartilage 19 (September 2011): S29—S30. http://dx.doi.org/10.1016/s1063-4584(11)60079-4.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

Zakharova, Irina O., Tatiana V. Sokolova, Liubov V. Bayunova, Inna I. Zorina, Maria P. Rychkova, Alexander O. Shpakov, and Natalia F. Avrova. "The Protective Effect of Insulin on Rat Cortical Neurons in Oxidative Stress and Its Dependence on the Modulation of Akt, GSK-3beta, ERK1/2, and AMPK Activities." International Journal of Molecular Sciences 20, no. 15 (July 29, 2019): 3702. http://dx.doi.org/10.3390/ijms20153702.

Full text

Abstract:

Insulin is a promising drug for the treatment of diseases associated with brain damage. However, the mechanism of its neuroprotective action is far from being understood. Our aim was to study the insulin-induced protection of cortical neurons in oxidative stress and its mechanism. Immunoblotting, flow cytometry, colorimetric, and fluorometric techniques were used. The insulin neuroprotection was shown to depend on insulin concentration in the nanomolar range. Insulin decreased the reactive oxygen species formation in neurons. The insulin-induced modulation of various protein kinase activities was studied at eight time-points after neuronal exposure to prooxidant (hydrogen peroxide). In prooxidant-exposed neurons, insulin increased the phosphorylation of GSK-3beta at Ser9 (thus inactivating it), which resulted from Akt activation. Insulin activated ERK1/2 in neurons 5–30 min after cell exposure to prooxidant. Hydrogen peroxide markedly activated AMPK, while it was for the first time shown that insulin inhibited it in neurons at periods of the most pronounced activation by prooxidant. Insulin normalized Bax/Bcl-2 ratio and mitochondrial membrane potential in neurons in oxidative stress. The inhibitors of the PI3K/Akt and MEK1/2/ERK1/2 signaling pathways and the AMPK activator reduced the neuroprotective effect of insulin. Thus, the protective action of insulin on cortical neurons in oxidative stress appear to be realized to a large extent through activation of Akt and ERK1/2, GSK-3beta inactivation, and inhibition of AMPK activity increased by neuronal exposure to prooxidant.

APA, Harvard, Vancouver, ISO, and other styles

21

Lucas, J. J. "Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice." EMBO Journal 20, no. 1 (January 15, 2001): 27–39. http://dx.doi.org/10.1093/emboj/20.1.27.

Full text

APA, Harvard, Vancouver, ISO, and other styles

22

Bickler, Philip E., Xinhua Zhan, and Christian S. Fahlman. "Isoflurane Preconditions Hippocampal Neurons against Oxygen–Glucose Deprivation." Anesthesiology 103, no. 3 (September 1, 2005): 532–39. http://dx.doi.org/10.1097/00000542-200509000-00016.

Full text

Abstract:

Background Isoflurane preconditions neurons to improve tolerance of subsequent ischemia in both intact animal models and in in vitro preparations. The mechanisms for this protection remain largely undefined. Because isoflurane increases intracellular Ca2+ concentrations and Ca2+ is involved in many processes related to preconditioning, the authors hypothesized that isoflurane preconditions neurons via Ca2+-dependent processes involving the Ca2+- binding protein calmodulin and the mitogen-activated protein kinase-ERK pathway. Methods The authors used a preconditioning model in which organotypic cultures of rat hippocampus were exposed to 0.5-1.5% isoflurane for a 2-h period 24 h before an ischemia-like injury of oxygen-glucose deprivation. Survival of CA1, CA3, and dentate neurons was assessed 48 later, along with interval measurements of intracellular Ca2+ concentration (fura-2 fluorescence microscopy in CA1 neurons), mitogen-activated protein kinase p42/44, and the survival associated proteins Akt and GSK-3beta (in situ immunostaining and Western blots). Results Preconditioning with 0.5-1.5% isoflurane decreased neuron death in CA1 and CA3 regions of hippocampal slice cultures after oxygen-glucose deprivation. The preconditioning period was associated with an increase in basal intracellular Ca2+ concentration of 7-15%, which involved Ca2+ release from inositol triphosphate-sensitive stores in the endoplasmic reticulum, and transient phosphorylation of mitogen-activated protein kinase p42/44 and the survival-associated proteins Akt and GSK-3beta. Preconditioning protection was eliminated by the mitogen-activated extracellular kinase inhibitor U0126, which prevented phosphorylation of p44 during preconditioning, and by calmidazolium, which antagonizes the effects of Ca2+-bound calmodulin. Conclusions Isoflurane, at clinical concentrations, preconditions neurons in hippocampal slice cultures by mechanisms that apparently involve release of Ca2+ from the endoplasmic reticulum, transient increases in intracellular Ca2+ concentration, the Ca2+ binding protein calmodulin, and phosphorylation of the mitogen-activated protein kinase p42/44.

APA, Harvard, Vancouver, ISO, and other styles

23

Kim, M., A. Datta, P. Brakeman, W. Yu, and K. E. Mostov. "Polarity proteins PAR6 and aPKC regulate cell death through GSK-3beta in 3D epithelial morphogenesis." Journal of Cell Science 120, no. 14 (July 15, 2007): 2309–17. http://dx.doi.org/10.1242/jcs.007443.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Muller, Werner, Uri Frank, Regina Teo, Ofer Mokady, Christina Guette, and Gunter Plickert. "Wnt signaling in hydroid development: ectopic heads and giant buds induced by GSK-3beta inhibitors." International Journal of Developmental Biology 51, no. 3 (2007): 211–20. http://dx.doi.org/10.1387/ijdb.062247wm.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Wang, Jian-Zhi. "P2-316: I2PP2A regulates PP2A and GSK-3beta activity and its role in Alzheimer's disease." Alzheimer's & Dementia 7 (July 2011): S411. http://dx.doi.org/10.1016/j.jalz.2011.05.1194.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

Alessandrini, Alessandro, Stephanie de Haseth, Michael Fray, Winfred Williams, A. Benedict Cosimi, and Gilles Benichou. "F.100. GM-CSF Induced Maturation of Dendritic Cells is Associated with GSK-3beta Inhibition." Clinical Immunology 127 (January 2008): S76. http://dx.doi.org/10.1016/j.clim.2008.03.212.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

Yang, Cuicui, Li Zhang, Yali Li, Lan Zhang, and Lin Li. "Cornel iridoid glycoside inhibits tau pathology via regulating cross-talk between GSK-3beta and PP2A signaling." Proceedings for Annual Meeting of The Japanese Pharmacological Society WCP2018 (2018): PO2–12–13. http://dx.doi.org/10.1254/jpssuppl.wcp2018.0_po2-12-13.

Full text

APA, Harvard, Vancouver, ISO, and other styles

28

Naito, Sei, Vladimir Bilim, Kaori Yuuki, Andrei V. Ougolkov, Daniel D. Billadeau, Teiichi Motoyama, and Yoshihiko Tomita. "ROLE OF THE NUCLEAR ACCUMULATION OF GSK-3BETA IN BLADDER CANCER MALIGNANT PHENOTYPE - POTENTIAL THERAPEUTIC TARGET." Journal of Urology 181, no. 4S (April 2009): 411. http://dx.doi.org/10.1016/s0022-5347(09)61167-8.

Full text

APA, Harvard, Vancouver, ISO, and other styles

29

Zhang, Jingjing, Changlei Cui, Yanhui Li, and Haiyang Xu. "Inhibition of GSK-3beta Signaling Pathway Rescues Ketamine-Induced Neurotoxicity in Neural Stem Cell-Derived Neurons." NeuroMolecular Medicine 20, no. 1 (December 7, 2017): 54–62. http://dx.doi.org/10.1007/s12017-017-8472-8.

Full text

APA, Harvard, Vancouver, ISO, and other styles

30

Hoozemans, Jeroen J., Elise S. van Haastert, Sidhartha M. Chafekar, Robert Veerhuis, Piet Eikelenboom, Frank Baas, Annemieke J. Rozemuller, and Wiep Scheper. "P1-377: The unfolded protein response is associated with increased GSK-3beta activity in Alzheimer's disease." Alzheimer's & Dementia 2 (July 2006): S208. http://dx.doi.org/10.1016/j.jalz.2006.05.755.

Full text

APA, Harvard, Vancouver, ISO, and other styles

31

Alkhateeb, Hakam. "Thujone improves glucose homeostasis in streptozotocin-induced diabetic rats through activation of Akt/GSK-3beta signaling pathway." Journal of Experimental and Integrative Medicine 5, no. 1 (2015): 30. http://dx.doi.org/10.5455/jeim.260115.or.122.

Full text

APA, Harvard, Vancouver, ISO, and other styles

32

Peng, Fuwang, Honghong Yao, Halis Kaan Akturk, and Shilpa Buch. "Platelet-Derived Growth Factor CC-Mediated Neuroprotection against HIV Tat Involves TRPC-Mediated Inactivation of GSK 3beta." PLoS ONE 7, no. 10 (October 15, 2012): e47572. http://dx.doi.org/10.1371/journal.pone.0047572.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

Chao, Hung-Hsing, Li-Chin Sung, Cheng-Hsien Chen, Ju-Chi Liu, Jin-Jer Chen, and Tzu-Hurng Cheng. "Lycopene Inhibits Urotensin-II-Induced Cardiomyocyte Hypertrophy in Neonatal Rat Cardiomyocytes." Evidence-Based Complementary and Alternative Medicine 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/724670.

Full text

Abstract:

This study investigated how lycopene affected urotensin-II- (U-II-) induced cardiomyocyte hypertrophy and the possible implicated mechanisms. Neonatal rat cardiomyocytes were exposed to U-II (1 nM) either exclusively or following 6 h of lycopene pretreatment (1–10 μM). The lycopene (3–10 μM) pretreatment significantly inhibited the U-II-induced cardiomyocyte hypertrophy, decreased the production of U-II-induced reactive oxygen species (ROS), and reduced the level of NAD(P)H oxidase-4 expression. Lycopene further inhibited the U-II-induced phosphorylation of the redox-sensitive extracellular signal-regulated kinases. Moreover, lycopene treatment prevented the increase in the phosphorylation of serine-threonine kinase Akt and glycogen synthase kinase-3beta (GSK-3β) caused by U-II without affecting the protein levels of the phosphatase and tensin homolog deleted on chromosome 10 (PTEN). However, lycopene increased the PTEN activity level, suggesting that lycopene prevents ROS-induced PTEN inactivation. These findings imply that lycopene yields antihypertrophic effects that can prevent the activation of the Akt/GSK-3βhypertrophic pathway by modulating PTEN inactivation through U-II treatment. Thus, the data indicate that lycopene prevented U-II-induced cardiomyocyte hypertrophy through a mechanism involving the inhibition of redox signaling. These findings provide novel data regarding the molecular mechanisms by which lycopene regulates cardiomyocyte hypertrophy.

APA, Harvard, Vancouver, ISO, and other styles

34

Vallée, Alexandre, Jean-Noël Vallée, and Yves Lecarpentier. "Parkinson’s Disease: Potential Actions of Lithium by Targeting the WNT/β-Catenin Pathway, Oxidative Stress, Inflammation and Glutamatergic Pathway." Cells 10, no. 2 (January 25, 2021): 230. http://dx.doi.org/10.3390/cells10020230.

Full text

Abstract:

Parkinson’s disease (PD) is one of the major neurodegenerative diseases (ND) which presents a progressive neurodegeneration characterized by loss of dopamine in the substantia nigra pars compacta. It is well known that oxidative stress, inflammation and glutamatergic pathway play key roles in the development of PD. However, therapies remain uncertain and research for new treatment is mandatory. This review focuses on the potential effects of lithium, as a potential therapeutic strategy, on PD and some of the presumed mechanisms by which lithium provides its benefit properties. Lithium medication downregulates GSK-3beta, the main inhibitor of the WNT/β-catenin pathway. The stimulation of the WNT/β-catenin could be associated with the control of oxidative stress, inflammation, and glutamatergic pathway. Future prospective clinical trials could focus on lithium and its different and multiple interactions in PD.

APA, Harvard, Vancouver, ISO, and other styles

35

Rouhani, Maryam, Samira Ramshini, and Maryam Omidi. "The Psychiatric Drug Lithium Increases DNA Damage and Decreases Cell Survival in MCF-7 and MDA-MB-231 Breast Cancer Cell Lines Expos ed to Ionizing Radiation." Current Molecular Pharmacology 12, no. 4 (October 15, 2019): 301–10. http://dx.doi.org/10.2174/1874467212666190503151753.

Full text

Abstract:

Background: Breast cancer is the most common cancer among women. Radiation therapy is used for treating almost every stage of breast cancer. A strategy to reduce irradiation side effects and to decrease the recurrence of cancer is concurrent use of radiation and radiosensitizers. We studied the effect of the antimanic drug lithium on radiosensitivity of estrogen-receptor (ER)-positive MCF-7 and ER-negative, invasive, and radioresistant MDA-MB-231 breast cancer cell lines. Methods: MCF-7 and MDA-MB-231 breast cancer cell lines were treated with 30 mM and 20 mM concentrations of lithium chloride (LiCl), respectively. These concentrations were determined by MTT viability assay. Growth curves were depicted and comet assay was performed for control and LiCl-treated cells after exposure to X-ray. Total and phosphorylated inactive levels of glycogen synthase kinase-3beta (GSK-3β) protein were determined by ELISA assay for control and treated cells. Results: Treatment with LiCl decreased cell proliferation after exposure to X-ray as indicated by growth curves of MCF-7 and MDA-MB-231 cell lines within six days following radiation. Such treatment increased the amount of DNA damages represented by percent DNA in Tails of comets at 0, 1, 4, and even 24 hours after radiation in both studied cell lines. The amount of active GSK-3β was increased in LiCl-treated cells in ER-positive and ER-negative breast cancer cell lines. Conclusion: Treatment with LiCl that increased the active GSK-3β protein, increased DNA damages and decreased survival independent of estrogen receptor status in breast cancer cells exposed to ionizing radiation.

APA, Harvard, Vancouver, ISO, and other styles

36

Datusalia, A. K., and S. S. Sharma. "Inhibition of GSK-3beta signalling improves cognitive deficits and glutamate-excitotoxicity in diabetes through transcription regulation of CREB." European Neuropsychopharmacology 26 (October 2016): S237. http://dx.doi.org/10.1016/s0924-977x(16)31101-4.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

Bauer, K., A. Dowejko, A. K. Bosserhoff, T. E. Reichert, and R. Josef Bauer. "P-cadherin induces an epithelial-like phenotype in oral squamous cell carcinoma by GSK-3beta-mediated Snail phosphorylation." Carcinogenesis 30, no. 10 (July 14, 2009): 1781–88. http://dx.doi.org/10.1093/carcin/bgp175.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Frey, Benício Noronha, Manoela M. Rodrigues da Fonseca, Rodrigo Machado-Vieira, Jair C. Soares, and Flávio Kapczinski. "Anormalidades neuropatológicas e neuroquímicas no transtorno afetivo bipolar." Revista Brasileira de Psiquiatria 26, no. 3 (September 2004): 180–88. http://dx.doi.org/10.1590/s1516-44462004000300008.

Full text

Abstract:

OBJETIVOS: Estudos pós-mortem, farmacológicos, de neuroimagem e em modelos animais têm demonstrado uma possível associação de mecanismos de sinalização intracelular na fisiopatologia do transtorno afetivo bipolar (TAB). Esse trabalho tem como objetivo revisar os achados em neuropatologia e bioquímica celular. MÉTODOS: Foi realizada uma pesquisa ao MEDLINE, entre 1980 e 2003, tendo sido utilizados os unitermos: bipolar disorder, signaling, second messengers e postmortem, além de referências cruzadas dos artigos selecionados. RESULTADOS: uropatológicos demonstraram uma diminuição do número de células neuronais e gliais, principalmente no córtex pré-frontal de pacientes bipolares. Estudos neuroquímicos demonstraram alterações nas vias do AMPc, fosfatidilinositol, Wnt/GSK-3beta e Ca++ intracelular nesses pacientes. CONCLUSÃO: Os achados de alterações neuropatológicas e neuroquímicas no TAB podem estar relacionados com a fisiopatologia deste transtorno e com os efeitos dos estabilizadores de humor. No entanto, mais estudos são necessários para esclarecer o papel das cascatas de sinalização intracelular na patogênese deste transtorno.

APA, Harvard, Vancouver, ISO, and other styles

39

Salles, M. J., D. Hervé, M. J. Millan, J. A. Girault, and C. Mannoury la Cour. "P.1.006 Stimulation of D3 receptors activates Akt/GSK-3beta and mTOR signalling pathways in nucleus accumbens and striatum." European Neuropsychopharmacology 22 (March 2012): S8. http://dx.doi.org/10.1016/s0924-977x(12)70008-1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Zhou, Binhua P., and Mien-Chie Hung. "Wnt, Hedgehog, and Snail: Sister Pathways That Control by GSK-3beta and beta-Trcp in the Regulation of Metastasis." Cell Cycle 4, no. 6 (April 13, 2005): 772–76. http://dx.doi.org/10.4161/cc.4.6.1744.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Sun, Dongdong, Min Shen, Jiayi Li, Weijie Li, Yingmei Zhang, Zheng Zhang, Li Zhao, Yuan Yuan, Haichang Wang, and Feng Cao. "Cardioprotective effects of tanshinone IIA pretreatment via kinin B2 receptor-Akt-GSK-3beta dependent pathway in experimental diabetic cardiomyopathy." Cardiovascular Diabetology 10, no. 1 (2011): 4. http://dx.doi.org/10.1186/1475-2840-10-4.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Abrahamsson, Annelie, Ifat Geron, Jason Gotlib, Jeffrey Durocher, Remi Creusot, Edward Kavalerchik, Daniel Goff, et al. "Aberrant Regulation of Wnt/Beta-Catenin Pathway Mediators in Chronic Myelogenous Leukemia Stem Cells." Blood 108, no. 11 (November 1, 2006): 2135. http://dx.doi.org/10.1182/blood.v108.11.2135.2135.

Full text

Abstract:

Abstract Background Recent research suggests that self-renewing leukemia stem cells (LSC) with increased beta-catenin expression are involved in chronic myelogenous leukemia (CML) progression. We investigated whether aberrant regulation of beta-catenin destruction complex genes contributed to the enhanced self-renewal potential of CML LSC. Methods FACS Aria purified normal and CML hematopoietic stem cells (HSC), granulocyte-macrophage progenitors (GMP) and lineage positive cells were transduced for 48 hours with lentiviral luciferase GFP and transplanted intrahepatically into newborn RAG2−/−gama−/− mice. At 8 to 12 weeks human CD45+ cells were FACS-purified and transplanted into secondary recipients to establish a bioluminescent CML LSC model. RT-PCR for BCR-ABL was used to confirm CML engraftment. Wnt mediator mutation analysis was performed on cDNA via fluorescent denaturing high performance liquid chromatography (DHPLC) technology and SURVEYOR mismatch cleavage analysis both with the WAVE-HS System (Transgenomic, Gaithersberg, MD). Aliquots of PCR product (3-15 ul) from all samples were scanned for mutations by DHPLC and confirmed by Surveyor mismatch cleavage, and identified with bidirectional sequence analysis on an ABI 3100 sequencer using BigDye V3.1 terminator chemistry. Quantitative RT-PCR was also performed on CML progenitors using destruction complex gene specific primers. FACS analysis was performed with the aid of a FACS Aria to analyze changes in Wnt signaling pathway mediators. Results Advanced phase CML was typified by expansion of a GMP population with aberrantly activated beta-catenin expression, enhanced in vitro replating capacity as well as serial transplantation potential in a CML LSC bioluminescent imaging model suggesting that the GMP population was enriched for LSC (Figure 1). A targeted Wnt mutation analysis revealed a mutation in a key component of the beta-catenin destruction complex - glycogen synthase kinase 3beta (GSK) in progenitors from three of six blast crisis CML samples analyzed. Decreased GSK expression was confirmed via FACS analysis using a GSK specific antibody in three separate experiments with CML blast crisis progenitors (Figure 2). Some CML blast crisis progenitors also demonstrated a decrease in axin 2 by quantitative RT-PCR. Conclusions Altered expression of Wnt signaling pathway regulators, such as GSK3, may result in increased LSC self-renewal capacity and may represent novel therapeutic targets for advanced phase CML. Figure 1. Bioluminescent Chronic Myeloneous Leukemis stem cell Model Figure 1. Bioluminescent Chronic Myeloneous Leukemis stem cell Model Figure 2. GSK FACS Analysis. Figure 2. GSK FACS Analysis.

APA, Harvard, Vancouver, ISO, and other styles

43

Gao, Qing, Maojuan Guo, Xijuan Jiang, Xiantong Hu, Yijing Wang, and Yingchang Fan. "A Cocktail Method for Promoting Cardiomyocyte Differentiation from Bone Marrow-Derived Mesenchymal Stem Cells." Stem Cells International 2014 (2014): 1–11. http://dx.doi.org/10.1155/2014/162024.

Full text

Abstract:

A growing body of evidence supports the argument that bone marrow-derived mesenchymal stem cells (MSCs) can differentiate into cardiomyocyte-like cells in an appropriate cellular environment, but the differentiation rate is low. A cocktail method was designed: we investigated the role of 5-azacytidine (5-aza), salvianolic acid B (SalB), and cardiomyocyte lysis medium (CLM) in inducing MSCs to acquire the phenotypical characteristics of cardiomyocytes. The fourth-passage MSCs were treated with 5-aza, SalB, CLM, 5-aza+salB, 5-aza+CLM, SalB+CLM, and 5-aza+SalB+CLM for 2 weeks. Immunofluorescence results showed that cTnT expression in the 5-aza+salB+CLM group was stronger than other groups. Real-time qPCR and Western blotting analyses showed that cTnT, alpha-cardiac actin, mef-2c, Cx43, and GSK-3beta expression increased while beta-catenin expression decreased. The salB+5-aza+CLM group had the most evident effects. SalB combined with 5-aza and CLM improved cardiomyocyte differentiation from MSCs. In the MSCs differentiation process, the Wnt/beta-catenin signaling pathway had been inhibited.

APA, Harvard, Vancouver, ISO, and other styles

44

Mirzoev, Timur, Sergey Tyganov, Natalia Vilchinskaya, Yulia Lomonosova, and Boris Shenkman. "Key Markers of mTORC1-Dependent and mTORC1-Independent Signaling Pathways Regulating Protein Synthesis in Rat Soleus Muscle During Early Stages of Hindlimb Unloading." Cellular Physiology and Biochemistry 39, no. 3 (2016): 1011–20. http://dx.doi.org/10.1159/000447808.

Full text

Abstract:

Background/Aims: The purpose of the study was to assess the amount of rRNA and phosphorylation status of the key markers of mTORC1-dependent (70s6k, 4E-BP1) and mTORC1-independent (GSK-3β, AMPK) signaling pathways controlling protein synthesis in rat soleus during early stages of mechanical unloading (hindlimb suspension (HS) for 1-, 3- and 7 days). Methods: The content of the key signaling molecules of various anabolic signaling pathways was determined by Western-blotting. The amount of 28S rRNA was evaluated by RT-PCR. The rate of protein synthesis was assessed using in-vivo SUnSET technique. Results: HS for 3 and 7 days induced a significant (p<0.05) decrease in the rate of global protein synthesis in soleus muscle in comparison with control. HS within 24 hours resulted in a significant (p<0.05) decrease in p-4E-BP1 content, p-AMPK content and increase in p-p70s6k content in rat soleus muscle. Following three days of HS the content of p-AKT was decreased (p<0.05). After 7 days of HS the phosphorylation level of AKT and GSK-3beta was significantly reduced (p<0.05) compared to control. We also observed a significant decrease in the amount of 28S rRNA in rat soleus following 1, 3 and 7 days of HS. Conclusion: Taken together, the results of our study suggest that a decline in the global rate of protein synthesis in rat soleus during early stages of simulated microgravity is associated with impaired ribosome biogenesis as well as reduced activity of mTORC1-independent signaling pathways.

APA, Harvard, Vancouver, ISO, and other styles

45

Schulz, Daniela, Irene Stancev, Antonio Sorrentino, Ayse-Nur Menevse, Philipp Beckhove, Gero Brockhoff, Matthias Günther Hautmann, Torsten Erich Reichert, Richard Josef Bauer, and Tobias Ettl. "Increased PD-L1 expression in radioresistant HNSCC cell lines after irradiation affects cell proliferation due to inactivation of GSK-3beta." Oncotarget 10, no. 5 (January 15, 2019): 573–83. http://dx.doi.org/10.18632/oncotarget.26542.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

Ohta, Etsuro, Tomoko Nihira, Akiko Uchino, Yoichi Imaizumi, Yohei Okada, Wado Akamatsu, Kayoko Takahashi, et al. "I2020T LRRK2 iPSC-derived neurons in the Sagamihara family exhibit increased Tau phosphorylation through the AKT/GSK-3beta signaling pathway." Parkinsonism & Related Disorders 22 (January 2016): e167. http://dx.doi.org/10.1016/j.parkreldis.2015.10.405.

Full text

APA, Harvard, Vancouver, ISO, and other styles

47

Hu, Bo, Yuhong Wu, Jie Liu, Xiaohua Shen, Fei Tong, Guangtao Xu, and Ruilin Shen. "GSK-3beta Inhibitor Induces Expression of Nrf2/TrxR2 Signaling Pathway to Protect against Renal Ischemia/Reperfusion Injury in Diabetic Rats." Kidney and Blood Pressure Research 41, no. 6 (2016): 937–46. http://dx.doi.org/10.1159/000452598.

Full text

APA, Harvard, Vancouver, ISO, and other styles

48

Kelly, G. M., D. A. Buckley, P. A. Kiely, and R. O'Connor. "OR10,55 GSK-3beta regulates insulin-like growth factor receptor tyrosine kinase activity by phosphorylation of S1248 in the C-terminus." Growth Hormone & IGF Research 20 (January 2010): S25. http://dx.doi.org/10.1016/s1096-6374(10)70069-1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

49

Liu, Fei, Nana Jin, Jianhua Shi, Wei Qian, Xiaomin Yin, Inge Grundke-Iqbal, Khalid Iqbal, and Cheng-Xin Gong. "O1-07-06: Truncation of GSK-3beta by calpain I contributes to the hyperphosphorylation of tau in the Alzheimer's brain." Alzheimer's & Dementia 8, no. 4S_Part_3 (July 2012): P98. http://dx.doi.org/10.1016/j.jalz.2012.05.244.

Full text

APA, Harvard, Vancouver, ISO, and other styles

50

Wang, Chang-Dong, Cheng-Fu Yuan, You-Quan Bu, Xiang-Mei Wu, Jin-Yuan Wan, Li Zhang, Ning Hu, et al. "Fangchinoline Inhibits Cell Proliferation Via Akt/GSK-3beta/cyclin D1 Signaling and Induces Apoptosis in MDA-MB-231 Breast Cancer Cells." Asian Pacific Journal of Cancer Prevention 15, no. 2 (January 30, 2014): 769–73. http://dx.doi.org/10.7314/apjcp.2014.15.2.769.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!