Title:A Proteomic Analysis of Human Uterine Myoma
VOLUME: 18 ISSUE: 2
Author(s):Antonio Rizzello, Julien Franck, Marcello Pellegrino, Francesco De Nuccio, Pasquale Simeone, Giovanni Fiore, Silvia Di Tommaso, Antonio Malvasi, Andrea Tinelli, Isabelle Fournier, Michel Salzet, Michele Maffia and Daniele Vergara
Affiliation:Department of Biological and Environmental Sciences and Technologies, University of Salento, via Monteroni, Lecce, Italy.
Keywords:Uterine fibroids, mass spectrometry, system biology, pseudocapsule, estrogen receptor, progesterone receptor, extracellular
matrix.
Abstract:Uterine leiomyoma is a benign smooth muscle tumor characterized by a high incidence in
women of reproductive age. The aetiology of this tumor is still unknown but established risk factors include
high levels of female hormones, family history, African ancestry, early age of menarche and obesity. Here,
to identify proteomic features associated with this tumor type, we performed a liquid chromatography-mass
spectrometry (LC-MS/MS) analysis of uterine myomas. The identified proteins were subjected to a gene
ontology analysis to generate biological functions, molecular processes, and protein networks that were
relevant to the uploaded dataset. Pathway-based analysis was an effective approach to investigate the molecular
mechanisms underlying the disease and to create biological hypotheses about regulation of our proteins
including the identification of upstream regulators and main protein nodes. Moreover, proteomic and
in silico data were combined with immunohistochemistry and western blotting to identify a group of proteins
representative of some selected pathways, with a dysregulated expression in myoma, pseudocapsule,
and normal myometrium samples. Based on these results, we confirmed the over-expression of extracellular
matrix components, and estrogen and progesterone receptors in uterine myomas, and proposed biological
networks, canonical pathways and functions that may be relevant to the pathophysiology of this tumor.
