
Leiomyoma phosphoproteins involved in inhibition of oxidative stress and synthesis of reactive oxygen species
Author(s) -
Blendi Ura,
Lorenzo Monasta,
Giorgio Arrigoni,
Danilo Licastro,
Giovanni Di Lorenzo,
Federico Romano,
Bartolomea Gaita,
Federica Scrimin,
Giuseppe Ricci
Publication year - 2019
Publication title -
international journal of molecular medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.048
H-Index - 90
eISSN - 1791-244X
pISSN - 1107-3756
DOI - 10.3892/ijmm.2019.4377
Subject(s) - myometrium , oxidative stress , reactive oxygen species , blot , chemistry , uterine leiomyoma , biochemistry , leiomyoma , oxidative phosphorylation , microbiology and biotechnology , biology , endocrinology , pathology , medicine , uterus , gene
Uterine leiomyomas are benign smooth muscle cell tumors originating from the myometrium. The present study focused on leiomyoma and myometrium phosphoproteome enrichment by using immobilized metal affinity chromatography (IMAC). The phosphoproteome was analyzed by two‑dimensional gel electrophoresis coupled with mass spectrometry. Western blotting was used for data validation. The results from IMAC identified 26 proteins significantly differentially phosphorylated in leiomyomas compared with normal myometrium. Three upregulated proteins (peroxiredoxin 2, protein disulfide isomerase family A member 3 and peroxiredoxin 4) were further validated by western blotting. Ingenuity pathway analysis revealed that four phosphoproteins were involved in the inhibition of oxidative stress and synthesis of reactive oxygen species. The present results demonstated for the first time an association between oxidative stress and phosphorylation in leiomyoma development.