Abstract
Purpose: :
Uveal melanoma is the most common primary intraocular tumor in adults. Metastasis is the single leading cause of death. Patient survival in uveal melanoma may benefit from earlier recognition of potential metastases. It would be of great value for screening biomarker candidates. Proteome analysis leads to the identification and characterization of tumor-associated protein variants by two-dimensional electrophoresis and mass spectrometry.
Methods: :
Proteins from uveal melanoma ,normal uvea,melanocytoma and benign schwannoma of the uvea were separated by two-dimensional electrophoresis (2-DE), respectively, and analysed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS).
Results: :
237 proteins from uveal melanoma were identified,which mainly involved in metabolism, gene expression regulation, signal transduction,cell proliferation, differentiation, tumor suppression and apoptosis. The profile of differentially expressed protein spots between uveal melanoma and normal uvea group revealed 36 proteins as up-regulated and 1 protein as down-regulated. There are 9 differentially expressed proteins between uveal melanoma and melanocytoma group,7 of which are down-regulated. Compared to benign schwannoma,22 proteins are up-regulated in uveal melanoma. These proteins were subdivided into groups according to cellular function, with important roles in tumor development.
Conclusions: :
This study established a protein database of uveal melanoma as a valuable resource. Our data show that proteomics technologies could be used in the study of uveal melanoma investing biomarker candidates.
Keywords: proteomics • melanoma • tumors