Comparative proteomic analysis between benign and malignant-transformed hydatidiform mole

J Reprod Med. 2008 Aug;53(8):623-8.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Biomarkers, Tumor / metabolism*
  • Cell Transformation, Neoplastic*
  • Cohort Studies
  • Disease Progression
  • Female
  • Humans
  • Hydatidiform Mole / metabolism*
  • Hydatidiform Mole / pathology
  • Middle Aged
  • Neoplasm Proteins / metabolism*
  • Pregnancy
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Up-Regulation
  • Uterine Neoplasms / metabolism*
  • Uterine Neoplasms / pathology
  • Young Adult

Substances

  • Biomarkers, Tumor
  • Neoplasm Proteins