scholarly journals Decreased Activity in Neuropathic Pain Form and Gene Expression of Cyclin-Dependent Kinase5 and Glycogen Synthase Kinase-3 Beta in Soleus Muscle of Wistar Male Rats

2015 ◽  
Vol 17 (6) ◽  
Author(s):  
Masoud Rahmati ◽  
Seyed Jalal Taherabadi ◽  
Mahmoud Mehrabi
Keyword(s):  
Gene Expression ◽  
Neuropathic Pain ◽  
Soleus Muscle ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Male Rats ◽  
Glycogen Synthase Kinase 3 ◽  
Wistar Male Rats

scholarly journals MafA Stability in Pancreatic β Cells Is Regulated by Glucose and Is Dependent on Its Constitutive Phosphorylation at Multiple Sites by Glycogen Synthase Kinase 3

2007 ◽  
Vol 27 (19) ◽  
pp. 6593-6605 ◽  
Author(s):  
Song-iee Han ◽  
Shinsaku Aramata ◽  
Kunio Yasuda ◽  
Kohsuke Kataoka
Keyword(s):  
Gene Expression ◽  
Glycogen Synthase ◽  
Glucose Sensing ◽  
Insulin Gene ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Β Cells ◽  
Pancreatic Β Cells ◽  
Amino Terminal ◽  
Insulin Gene Expression

ABSTRACT Regulation of insulin gene expression by glucose in pancreatic β cells is largely dependent on a cis-regulatory element, termed RIPE3b/C1, in the insulin gene promoter. MafA, a member of the Maf family of basic leucine zipper (bZip) proteins, is a β-cell-specific transcriptional activator that binds to the C1 element. Based on increased C1-binding activity, MafA protein levels appear to be up-regulated in response to glucose, but the underlying molecular mechanism for this is not well understood. In this study, we show evidence supporting that the amino-terminal region of MafA is phosphorylated at multiple sites by glycogen synthase kinase 3 (GSK3) in β cells. Mutational analysis of MafA and pharmacological inhibition of GSK3 in MIN6 β cells strongly suggest that the rate of MafA protein degradation is regulated by glucose, that MafA is constitutively phosphorylated by GSK3, and that phosphorylation is a prerequisite for rapid degradation of MafA under low-glucose conditions. Our data suggest a new glucose-sensing signaling pathway in islet β cells that regulates insulin gene expression through the regulation of MafA protein stability.

Effects of a fructose-rich diet and chronic stress on insulin signaling and regulation of glycogen synthase kinase-3 beta and the sodium–potassium pump in the hearts of male rats

2020 ◽  
Vol 11 (2) ◽  
pp. 1455-1466 ◽  
Author(s):  
Snjezana Romic ◽  
Ana Djordjevic ◽  
Snezana Tepavcevic ◽  
Tijana Culafic ◽  
Mojca Stojiljkovic ◽  
...  
Keyword(s):  
Chronic Stress ◽  
Insulin Signaling ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Male Rats ◽  
Glycogen Synthase Kinase 3 ◽  
Sodium Potassium ◽  
Sodium Potassium Pump

This study provides new insights into the effects of chronic stress and a combination of a fructose diet and chronic stress on the studied molecules in the heart.

scholarly journals Differential expression of glycogen synthase kinase 3α and 3β isomers in brain cortex of mice following high doses of glucose

2020 ◽  
Vol 11 (1) ◽  
pp. 993-999
Author(s):  
Mohd Alaraj ◽  
Irena Kosinska ◽  
Bahaa Deen Al-Trad ◽  
Ammar Almaaytah ◽  
Tarek D. Hussein ◽  
...  
Keyword(s):  
Gene Expression ◽  
Cerebral Cortex ◽  
Mitochondrial Dysfunction ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Ultrastructural Changes ◽  
Histopathological Analysis ◽  
Modulation Of Gene Expression ◽  
High Doses

Glycogen synthase kinase 3 (GSK3) encodes a serine/threonine protein kinase. We investigated the effects of Subcutaneous (SC) glucose administration on the expression of glycogen synthase kinase 3 (GKS-3) isomers (α and β) genes in the cerebral cortex of mice with the aim of determining the possible mechanism(s) involved in mitochondrial dysfunction induced by hyperglycemia. Adult male BALB/c mice were treated with 12 gm/kg glucose solution SC once daily for 3 days. Ultrastructure study, histopathological analysis, and Real-time PCR investigations were carried out on the cerebral cortex from glucose treated mice and from vehicle-treated control animals. We observed significant ultrastructural damage of mitochondria in the cerebral cortex of mice received high doses of glucose. Histopathological alterations in the cortex of these animals were also detected. A significant increased of GSK-3α gene expression and decreased expressions of GKS-3β gene in high glucose treated animals were noticed. The hyperglycemia-induced ultrastructural changes may occur via modulation of gene expression of GSK-3 isomers, and we hypothesize this as an early etiopathological factor in hyperglycemia-related neurodegenerative diseases (NDD). It considered the first study describing "modulation of expression of GSK-3 isomer genes" as a possible mechanism of hyperglycemia-induced mitochondrial dysfunction.

scholarly journals Shared Roles of Yeast Glycogen Synthase Kinase 3 Family Members in Nitrogen-Responsive Phosphorylation of Meiotic Regulator Ume6p

2000 ◽  
Vol 20 (15) ◽  
pp. 5447-5453 ◽  
Author(s):  
Yang Xiao ◽  
Aaron P. Mitchell
Keyword(s):  
Gene Expression ◽  
Nitrogen Limitation ◽  
Glycogen Synthase ◽  
Gene Activation ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Meiotic Gene ◽  
Transduction Mechanisms

ABSTRACT Nitrogen limitation activates meiosis and meiotic gene expression in yeast, but nitrogen-responsive signal transduction mechanisms that govern meiotic gene expression are poorly understood. We show here that Ume6p, a subunit of the Ume6p-Ime1p meiotic transcriptional activator, undergoes increased phosphorylation in vivo in response to nitrogen limitation. Phosphorylation depends on an N-terminal glycogen synthase kinase 3 (GSK3) target site in which substitutions cause reduced Ume6p-Ime1p interaction and meiotic gene expression, thus arguing that phosphorylation promotes functional Ume6p-Ime1p interaction. Phosphorylation of this site depends on two GSK3 homologs, Rim11p and Mck1p. Prior studies indicate that Rim11p phosphorylates both Ume6p and Ime1p in vitro and is required for Ume6p-Ime1p interaction, but no evidence has linked Mck1p function to Ume6p activity. Here we find that Mck1p-Ume6p interaction is detectable by two-hybrid assays and that meiosis in a partially defective rim11-K68R mutant is completely dependent on Mck1p. These findings argue that nitrogen limitation governs Rim11p/Mck1p-dependent phosphorylation of Ume6p, which in turn is required for Ume6p-Ime1p interaction and meiotic gene activation.

scholarly journals Interaction of yeast repressor-activator protein Ume6p with glycogen synthase kinase 3 homolog Rim11p.

1997 ◽  
Vol 17 (12) ◽  
pp. 7230-7236 ◽  
Author(s):  
K Malathi ◽  
Y Xiao ◽  
A P Mitchell
Keyword(s):  
Gene Expression ◽  
Saccharomyces Cerevisiae ◽  
Transcriptional Activation ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Amino Acid Substitutions ◽  
Activation Domain ◽  
Yeast Saccharomyces Cerevisiae ◽  
Transcriptional Activation Domain

Meiosis and expression of early meiotic genes in the budding yeast Saccharomyces cerevisiae depend upon Rim11p, Ume6p, and Ime1p. Rim11p (also called Mds1p and ScGSK3) is a protein kinase related to glycogen synthase kinase 3 (GSK3); Ume6p is an architectural transcription factor; and Imelp is a Ume6p-binding protein that provides a transcriptional activation domain. Rim11p is required for Ime1p-Ume6p interaction, and prior studies have shown that Rim11p binds to and phosphorylates Ime1p. We show here that Rim11p binds to and phosphorylates Ume6p, as well. Amino acid substitutions in Ume6p that alter a consensus GSK3 site reduce or abolish Rim11p-Ume6p interaction and Rim11p-dependent phosphorylation, and they cause defects in interaction between Ume6p and Ime1p and in meiotic gene expression. Therefore, interaction between Rim11p and Ume6p, resulting in phosphorylation of Ume6p, is required for Ime1p-Ume6p complex formation. Rim11p, like metazoan GSK3beta, phosphorylates both interacting subunits of a target protein complex.

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