Changes in the activity of the GPx-1 anti-oxidant selenoenzyme in mononuclear cells following imatinib treatment

Terry, Emily N.; Gann, Peter H.; Molokie, Robert E.; Deininger, Michael W.; Diamond, Alan M.

doi:10.1016/j.leukres.2011.01.007

Cited by 4 publications

(4 citation statements)

References 7 publications

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“…This study was initiated because our previous results indicated a higher level of GPx activity in mononuclear cells obtained from patients post-imatinib treatment [11]. Using two different CML-derived cell lines, we established that exposure of these cells to imatinib increased GPx activity and GPx-1 levels, this being consistent with what was observed by examining the patient samples.…”

Section: Discussionsupporting

confidence: 80%

“…Based on the observation that GPx-1 activity could be enhanced by tyrosine phosphorylation and inhibited using the Bcr-Abl small molecule inhibitor imatinib [10] , we explored the possibility that patients being treated for chronic myelogenous leukemia (CML), a form of leukemia characterized by the Bcr-Abl translocation and treated with imatinib, would possess mononuclear blood cells with decreased GPx activity. Contrary to expectation, most of the samples examined from CML patients expressed increased GPx enzyme activity following imatinib therapy [11] . To examine this phenomenon in greater detail, studies were initiated in which established CML cell lines were exposed to imatinib in culture and consequential effects on GPx-1 examined.…”

Section: Introductioncontrasting

confidence: 71%

“…Contrary to expectation, most of the samples examined from CML patients expressed increased GPx enzyme activity following imatinib therapy [11]. To examine this phenomenon in greater detail, studies were initiated in which established CML cell lines were exposed to imatinib in culture and consequential effects on GPx-1 examined.…”

Section: Introductionmentioning

confidence: 93%

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Translational Regulation of GPx-1 and GPx-4 by the mTOR Pathway

et al. 2014

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Glutathione peroxidase activity was previously determined to be elevated in lymphocytes obtained from patients treated with the Bcr-Abl kinase inhibitor imatinib mesylate. In order to expand upon this observation, the established chronic myelogenous leukemia cell lines KU812 and MEG-01 were treated with imatinib and the effect on several anti-oxidant proteins was determined. The levels of GPx-1 were significantly increased following treatment with imatinib. This increase was not due to altered steady-state mRNA levels, and appeared to be dependent on the expression of Bcr-Abl, as no increases were observed following imatinib treatment of cells that did not express the fusion protein. The nutrient-sensing signaling protein, mammalian target of rapamycin (mTOR), can be activated by Bcr-Abl and its activity regulates the translation of many different proteins. Treatment of those same cells used in the imatinib studies with rapamycin, an inhibitor of mTOR, resulted in elevated GPx-1 and GPx-4 protein levels independent of Bcr-Abl expression. These proteins all belong to the selenoprotein family of peptides that contain the UGA-encoded amino acid selenocysteine. Collectively, these data provide evidence of a novel means of regulating anti-oxidants of the selenoprotein family via the mTOR pathway.

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Section: Discussionsupporting

confidence: 80%

Section: Introductioncontrasting

confidence: 71%

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Translational Regulation of GPx-1 and GPx-4 by the mTOR Pathway

et al. 2014

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“…36 We previously confirmed the positive regulatory role of oligonol in glucose metabolism in AD mice. We have also detected increased mRNA levels of antioxidant-related genes, such as Gclc , 37 Gpx1 , 38 Sod2 , 39 and G6pdh , 40 and nuclear factor erythroid-2-related factor 2 ( Nrf2 ) 41 in the livers of 5 × FAD mice (Fig. 1).…”

Section: Discussionmentioning

confidence: 76%

Oligonol ameliorates liver function and brain function in the 5 × FAD mouse model: transcriptional and cellular analysis

Jo,

Arjunan,

Choi

et al. 2023

Food Funct.

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Se Enhances MLCK Activation by Regulating Selenoprotein T (SelT) in the Gastric Smooth Muscle of Rats

Zhou

Wang

et al. 2016

Biol Trace Elem Res

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Selenium (Se), a nutritionally essential trace element, is associated with health and disease. Selenoprotein T (SelT) was identified as a redoxin protein with a selenocystein, localizing in the endoplasmic reticulum. The myosin light chain kinase (MLCK) and myosin light chain (MLC) play key roles in the contraction process of smooth muscle. The present study was to detect the effect and mechanism of SelT on the contraction process of gastric smooth muscle. The WT rats were fed with different Se concentration diets, and Se and Ca(2+) concentrations were detected in the gastric smooth muscle. Western blot and qPCR were performed to determine SelT, CaM, MLCK, and MLC expressions. MLCK activity was measured by identifying the rates of [γ-32P]ATP incorporated into the MLC. The results showed Se and Ca(2+) concentrations were enhanced with Se intake in gastric smooth muscle tissues. With increasing Se, SelT, CaM, MLCK and MLC expressions increased, and MLCK and MLC activation improved in gastric smooth muscle tissue. The SelT RNA interference experiments showed that Ca(2+) release, MLCK activation, and MLC phosphorylation were regulated by SelT. Se affected the gastric smooth muscle constriction by regulating Ca(2+) release, MLCK activation, and MLC phosphorylation through SelT. Se plays a major role in regulating the contraction processes of gastric smooth muscle with the SelT.

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Changes in the activity of the GPx-1 anti-oxidant selenoenzyme in mononuclear cells following imatinib treatment

Cited by 4 publications

References 7 publications

Translational Regulation of GPx-1 and GPx-4 by the mTOR Pathway

Translational Regulation of GPx-1 and GPx-4 by the mTOR Pathway

Oligonol ameliorates liver function and brain function in the 5 × FAD mouse model: transcriptional and cellular analysis

Se Enhances MLCK Activation by Regulating Selenoprotein T (SelT) in the Gastric Smooth Muscle of Rats

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