[Identification of tumor-associated proteins in laryngeal squamous cell carcinoma by proteomics]

To establish two-dimensional electrophoresis profiles from human laryngeal squamous cell carcinoma tissue and paired normal tumor-adjacent mucosa epithelia tissue, and to identify differential expression proteins.

The total proteins of human laryngeal squamous carcinoma tissue and paired normal tumor-adjacent mucosa epithelia tissue were separated by immobilized pH gradient-based two-dimensional gel electrophoresis (2-DE). The differential expression proteins were analyzed using image analysis software, then identified using mass spectrometry and database searching.

Well-resolved, reproducible 2-DE patterns of laryngeal squamous cell carcinoma and adjacent normal mucosa epithelial were obtained. Differential protein spots were defined as spots in 2-DE gels. Thirteen proteins were preliminarily identified, naming which 10 proteins were upregulated in laryngeal cancer tissue. Such as cofilin-1, nuclear body protein SP140, GRP94, HSP 90, GSTP1-1, superoxide dismutase [Mn], cyclophilin A, proteasome activator complex subunit 2, apolipoprotein A-I precursor, CaM-like protein and so on. There were 3 proteins downregulated in laryngeal cancer tissue, which were fatty acid-binding protein, calgranulin A and calgranulin B.

Thirteen proteins which are associated with the tumorigenesis of the laryngeal squamous cell carcinoma were characterized. These extensive protein variations indicate that multiple protein molecules should be simultaneously targeted as an effective strategy to counter the disease. It is better for understanding of the oncogenesis and pathogenesis in a global way, which in turn is a basis-for the rational designs of diagnostic and therapeutic methods.