Abstract
Premature ovarian failure (POF) is defined as loss of ovarian function in women less than 40 years of age. The causes of POF are diverse and include environmental factors. Di-2-ethylhexyl phthalate (DEHP) is one factor that may cause POF. The ubiquitin-proteasome system maintains intracellular balance by promoting or inhibiting protein degradation. To investigate the differential expressions of deubiquitinating enzyme (DUB) genes in patients with POF, we developed two in vitro POF models by treating A2780 or OVCAR5 with DEHP. Using these models, a multiplex RT-PCR system for DUB genes was applied to identify biomarkers by comparing expression patterns and DUB mRNA levels; multiplex RT-PCR results were validated by qRT-PCR and Western blotting analyses. Observed differential expression levels of several DUB genes including USP12, COPS5, ATXN3L, USP49, and USP34 in A2780 and OVCAR5 cells at the mRNA and protein levels suggest that they should be investigated as potential biomarkers of POF.
Highlights
Ubiquitination is an essential process that results in the degradation of dispensable proteins via the ubiquitin-proteasomal pathway (UPP) [1]
Our results showed the differential expressions of mRNA and protein for several deubiquitinating enzyme (DUB) genes including Ataxin-3-like protein (ATXN3L), Ubiquitin specific peptidase 12 (USP12), Ubiquitin specific peptidase 49 (USP49), COP9 signalosome subunit 5 (COPS5), and Ubiquitin specific peptidase 34 (USP34) in A2780 and OVCAR5 cells
To investigate DUB genes associated with Di-2-ethylhexyl phthalate (DEHP), ovarian cell lines were treated with different concentrations of DEHP (Table 1) [16]
Summary
Ubiquitination is an essential process that results in the degradation of dispensable proteins via the ubiquitin-proteasomal pathway (UPP) [1]. Protein ubiquitination is mediated by a series of enzymatic actions by ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), and ubiquitin ligases (E3) [1,2]. Deubiquitination is the inverse of ubiquitination, and deubiquitinating enzymes (DUBs) play a crucial role in protein stabilization by removing ubiquitin (Ub) from conjugated target proteins by hydrolyzing the isopeptide bonds of Ub-substrates. These ubiquitin-associated systems maintain intracellular protein balance by promoting or inhibiting degradation. The biological functions of DUBs are not completely understood yet
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
