Leiomyoma phosphoproteins involved in inhibition of oxidative stress and synthesis of reactive oxygen species

Ura, Blendi; Monasta, Lorenzo; Arrigoni, Giorgio; Licastro, Danilo; Lorenzo, Giovanni Di; Romano, Federico; Gaita, Bartolomea; Scrimin, Federica; Ricci, Giuseppe

doi:10.3892/ijmm.2019.4377

Cited by 2 publications

(3 citation statements)

References 28 publications

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“…Uterine leiomyoma is a benign tumor that affects 70-80% of women, which is the highest incidence amongst the benign tumors of the female reproductive tract (1,2). This neoplasm is responsible for serious health problems (3) and is characterized by abnormal extracellular matrix (4), altered phosphoproteins (5), dysregulated chaperones (6), and alterations in the proteins involved in cell migration (7).…”

Section: Introductionmentioning

confidence: 99%

Proteins involved in oxidative stress in leiomyoma tissues treated with ulipristal acetate

et al. 2020

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Uterine leiomyoma presents the highest incidence among benign tumors of the female reproductive tract. The present study compared the proteome of leiomyoma treated with ulipristal acetate with that of untreated leiomyoma to investigate protein expression patterns in relation to oxidative stress. Paired tissue samples from seven treated and untreated leiomyomas were collected and the proteome was analyzed by two-dimensional gel electrophoresis (2-DE). Western blotting was used to validate the results of 2-DE, and mass spectrometry was used to identify proteins. The tissue expression of 30 proteins was markedly affected by treatment with ulipristal acetate. Bioinformatics analysis revealed that several of the differentially expressed proteins were involved in the degradation of hydrogen peroxide and the synthesis of reactive oxygen species. The present study suggested the involvement of oxidative stress as a novel mechanism of action of ulipristal acetate. These findings require further investigations to understand the role of ulipristal acetate in the treatment of the leiomyoma.

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Section: Introductionmentioning

confidence: 99%

Proteins involved in oxidative stress in leiomyoma tissues treated with ulipristal acetate

et al. 2020

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“…Phosphoprotein-enriched samples were generated from red cell membrane protein extracts using a TALON PMAC Phosphoprotein Enrichment Kit (ClonTech, CA, USA) according to the manufacturer's instructions [32,33].…”

Section: Phosphoprotein-enriched Samplesmentioning

confidence: 99%

“…This intrigued us, since previous studies on Tyr-phospho-maps of red cells from both healthy mice and human subjects did not find phospho-Tyr-Prx2 associated with the membrane [14,31]. We then carried out phospho-peptide enrichment using a phospho-specific metal ion affinity resin (TALON PMAC Phosphoprotein Enrichment Kit) of mouse red cells exposed to diamide [32,33]. Prx2 was identified by MALDI-TOF analysis and further confirmed by LC-MS/MS analysis (Figure 2b).…”

Section: Prx2 Is Tyrosine-phosphorylated In Response To Oxidation and Associates To The Membranementioning

confidence: 99%

Tyrosine Phosphorylation Modulates Peroxiredoxin-2 Activity in Normal and Diseased Red Cells

et al. 2021

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Peroxiredoxin-2 (Prx2) is the third most abundant cytoplasmic protein in red blood cells. Prx2 belongs to a well-known family of antioxidants, the peroxiredoxins (Prxs), that are widely expressed in mammalian cells. Prx2 is a typical, homodimeric, 2-Cys Prx that uses two cysteine residues to accomplish the task of detoxifying a vast range of organic peroxides, H2O2, and peroxynitrite. Although progress has been made on functional characterization of Prx2, much still remains to be investigated on Prx2 post-translational changes. Here, we first show that Prx2 is Tyrosine (Tyr) phosphorylated by Syk in red cells exposed to oxidation induced by diamide. We identified Tyr-193 in both recombinant Prx2 and native Prx2 from red cells as a specific target of Syk. Bioinformatic analysis suggests that phosphorylation of Tyr-193 allows Prx2 conformational change that is more favorable for its peroxidase activity. Indeed, Syk-induced Tyr phosphorylation of Prx2 enhances in vitro Prx2 activity, but also contributes to Prx2 translocation to the membrane of red cells exposed to diamide. The biologic importance of Tyr-193 phospho-Prx2 is further supported by data on red cells from a mouse model of humanized sickle cell disease (SCD). SCD is globally distributed, hereditary red cell disorder, characterized by severe red cell oxidation due to the pathologic sickle hemoglobin. SCD red cells show Tyr-phosphorylated Prx2 bound to the membrane and increased Prx2 activity when compared to healthy erythrocytes. Collectively, our data highlight the novel link between redox related signaling and Prx2 function in normal and diseased red cells.

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Leiomyoma phosphoproteins involved in inhibition of oxidative stress and synthesis of reactive oxygen species

Cited by 2 publications

References 28 publications

Proteins involved in oxidative stress in leiomyoma tissues treated with ulipristal acetate

Proteins involved in oxidative stress in leiomyoma tissues treated with ulipristal acetate

Tyrosine Phosphorylation Modulates Peroxiredoxin-2 Activity in Normal and Diseased Red Cells

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