@article {10542,
	title = {Identification of proteins with different abundance associated with cell migration and proliferation in leiomyoma interstitial fluid by proteomics.},
	journal = {Oncol Lett},
	volume = {13},
	year = {2017},
	month = {2017 May},
	pages = {3912-3920},
	abstract = {<p>Uterine leiomyoma is the most common female reproductive tract benign tumor. Little is known about protein composition and changes in the leiomyoma interstitial fluid (IF). The present study focused on changes in protein abundance in the IF of leiomyoma. Leiomyoma IFs and adjacent myometrial IFs were obtained and analyzed by two-dimensional electrophoresis (2-DE) coupled with mass spectrometry and western blotting for 2-DE data validation. A total of 25 unique proteins were observed to change significantly (P<0.05). Of these proteins with different abundance, 22 had not been previously identified in leiomyoma IF.  analysis predicted that three of these proteins were secreted via classical mechanisms, while 22 were secreted via non-classical mechanisms. Ingenuity Pathway Analysis identified 17 proteins associated with cellular migration and proliferation. Among these, phosphoglycerate mutase 1 had not been previously associated with leiomyoma. The abundance of seven proteins was further validated by western blotting. A comparative proteomic approach identified a number of proteins associated with cellular migration and proliferation, with changes in abundance in IF likely to be involved in tumor development. Further studies will be required to investigate the role of these proteins in leiomyoma IF and their possible association with tumor development and growth.</p>},
	issn = {1792-1074},
	doi = {10.3892/ol.2017.5943},
	author = {Ura, Blendi and Scrimin, Federica and Franchin, Cinzia and Arrigoni, Giorgio and Licastro, Danilo and Monasta, Lorenzo and Ricci, Giuseppe}
}
@article {8341,
	title = {A Proteomic Approach for the Identification of Up-Regulated Proteins Involved in the Metabolic Process of the Leiomyoma.},
	journal = {Int J Mol Sci},
	volume = {17},
	year = {2016},
	month = {2016},
	pages = {540},
	abstract = {<p>Uterine leiomyoma is the most common benign smooth muscle cell tumor of the uterus. Proteomics is a powerful tool for the analysis of complex mixtures of proteins. In our study, we focused on proteins that were upregulated in the leiomyoma compared to the myometrium. Paired samples of eight leiomyomas and adjacent myometrium were obtained and submitted to two-dimensional gel electrophoresis (2-DE) and mass spectrometry for protein identification and to Western blotting for 2-DE data validation. The comparison between the patterns revealed 24 significantly upregulated (p < 0.05) protein spots, 12 of which were found to be associated with the metabolic processes of the leiomyoma and not with the normal myometrium. The overexpression of seven proteins involved in the metabolic processes of the leiomyoma was further validated by Western blotting and 2D Western blotting. Four of these proteins have never been associated with the leiomyoma before. The 2-DE approach coupled with mass spectrometry, which is among the methods of choice for comparative proteomic studies, identified a number of proteins overexpressed in the leiomyoma and involved in several biological processes, including metabolic processes. A better understanding of the mechanism underlying the overexpression of these proteins may be important for therapeutic purposes.</p>},
	issn = {1422-0067},
	doi = {10.3390/ijms17040540},
	author = {Ura, Blendi and Scrimin, Federica and Arrigoni, Giorgio and Franchin, Cinzia and Monasta, Lorenzo and Ricci, Giuseppe}
}
