Reduced expression of 14-3-3 gamma in uterine leiomyoma as identified by proteomics

Lv, Jieqiang; Zhu, Xueqiong; Dong, Ke; Lin, Yi Hui; Y, Hu; Zhu, Chundan

doi:10.1016/j.fertnstert.2007.08.039

Cited by 19 publications

(19 citation statements)

References 29 publications

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“…Using this approach we identified seven proteins with a significantly different expression between the leiomyoma and myometrium: α1-antitrypsin, desmin, peroxiredoxin-2 (upregulated in leiomyomas), and prelamin-A/C, transgelin, α-actinin-1, and heat shock 70 kDa protein 1A/1B (downregulated in leiomyomas). Two of the upregulated proteins, desmin and α1-antitrypsin (A1AT), found in the leiomyoma IF and further validated by immunohistochemistry, had been previously described at the tissue level of leiomyomas and leiomyosarcomas (17)(18)24). Thus, we were able to confirm and expand previous immunohistochemical data, indicating that these proteins were also secreted.…”

Section: Discussionsupporting

confidence: 84%

“…In addition to the group of blood soluble proteins, it contains a large subset of abnormal proteins released by tumor cells through classical secretion, non-classical secretion, membrane protein shedding and secretion via exosomes (16). The proteomic approach has been described for leiomyoma tissue (17) and plasma (18). However, to the best of our knowledge, no study has been conducted on the leiomyoma interstitial fluid (IF).…”

Section: Introductionmentioning

confidence: 99%

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Two-dimensional gel electrophoresis analysis of the leiomyoma interstitial fluid reveals altered protein expression with a possible involvement in pathogenesis

et al. 2015

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Abstract. Uterine leiomyoma is the most common smooth benign neoplasm. In the present study, we analyzed the global interstitial fluid (IF) profile of leiomyoma vs. normal myometrium to identify protein dysregulation involved in leiomyoma pathogenesis. Two-dimensional gel electrophoresis and mass spectrometry were used to generate and compare the global interstitial fluid profiles of the leiomyoma and of the normal tissue. Two proteins were validated by immunohistochemistry. By comparing the interstitial fluid profile of the leiomyoma with that of the normal myometrium, the levels of seven proteins were found to be significantly different: four structural organization proteins (desmin, prelamin-A/C, transgelin and α-actinin-1), an inflammatory response (α1-antitrypsin), a response to oxidative stress (peroxiredoxin-2), and a folding protein (heat shock 70 kDa protein 1A/1B). Desmin, α1-antitrypsin and peroxiredoxin-2 were upregulated in the leiomyoma, whereas heat shock 70 kDa protein 1A/1B, α-actinin-1, prelamin-A/C and transgelin were downregulated. Desmin and α1-antitrypsin were further validated by immunohistochemistry. By identifying proteins with altered expression levels compared to the myometrium from several pathways of the leiomyoma pathogenesis, we found the leiomyoma interstitial fluid to have a characteristic proteomic profile. A better appreciation of the pathophysiology of the disease can be useful in the development of conservative treatments that serve as viable alternatives to hysterectomy.

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Section: Discussionsupporting

confidence: 84%

Section: Introductionmentioning

confidence: 99%

Two-dimensional gel electrophoresis analysis of the leiomyoma interstitial fluid reveals altered protein expression with a possible involvement in pathogenesis

et al. 2015

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“…proteins, have been conducted in two-dimensional electrophoresis (2-DE) coupled with mass spectrometry (MS) (10) and gel electrophoresis liquid chromatography-MS (11). Our previous proteomic studies on leiomyoma tissue identified several dysregulated proteins involved in metabolic processes, oxidative stress and cell migration (12,13).…”

Section: Identification Of Proteins With Different Abundance Associatmentioning

confidence: 99%

Identification of proteins with different abundance associated with cell migration and proliferation in leiomyoma interstitial fluid by proteomics

et al. 2017

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Abstract. 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. In silico 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.

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“…Recently, Lv et al (13) reported reduced expression of 14-3-3 g in leiomyoma, and Bifulco et al (14) found a strong decrease in 14-3-3 level in GnRH agonist treated leiomyoma. The physiologic significance of nuclear accumulation of pSer 256 -FOXO1 is not known.…”

mentioning

confidence: 98%

Involvement of FKHR (FOXO1) transcription factor in human uterus leiomyoma growth

Kovács

Lengyel

Wilhelm

et al. 2010

Fertility and Sterility

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Reduced expression of 14-3-3 gamma in uterine leiomyoma as identified by proteomics

Cited by 19 publications

References 29 publications

Two-dimensional gel electrophoresis analysis of the leiomyoma interstitial fluid reveals altered protein expression with a possible involvement in pathogenesis

Two-dimensional gel electrophoresis analysis of the leiomyoma interstitial fluid reveals altered protein expression with a possible involvement in pathogenesis

Identification of proteins with different abundance associated with cell migration and proliferation in leiomyoma interstitial fluid by proteomics

Involvement of FKHR (FOXO1) transcription factor in human uterus leiomyoma growth

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