Comparative proteomic analysis between benign and malignant-transformed hydatidiform mole.

OBJECTIVE

To explore the differential protein expression between benign/remitting and malignant-transformed hydatidiform mole.

STUDY

DESIGN

Proteomic analysis was carried out on 7 remitting (including 3 partial moles and 4 complete moles) and 11 malignant-transformed (including 4 partial moles and 7 complete moles) hydatidiform moles. The extracted protein was separated with 2-dimensional electrophoresis, and differentially expressed proteins were analyzed and identified by matrix-assisted desorption/ionization time-of-flight spectrometry (MALDI-TOF-MS).

RESULTS

A total of 32 differentially expressed spots were selected. Of these, 17 spots were identified through database searching, mainly involving cytoskeletal protein, stress-associated proteins, apoptosis-associated protein, proteins involved in signal transduction, cell proliferation and differentiation, etc. Of these, 11 might be related to the malignant transformation of hydatidiform mole.

CONCLUSION

Seventeen differentially expressed proteins were identified, of which 11 might be associated with malignant transformation of hydatidiform mole. This has laid a foundation for further screening of biomarkers that predict prognosis of hydatidiform mole.