Abstract
Heat shock protein 10 (Hsp10), located in mitochondria, is a co-chaperone involved in the protein folding and aggregation with Hsp60. Besides, a wide range of other extramitochondrial and extracellular activities, such a mammalian mitochondrial chaperonin including modulation of apoptosis, inflammation, and carcinogenesis, have been reported. Expression of Hsp10 protein in oral squamous cell carcinomas (OSCC) and the non-cancerous squamous epithelium was detected using immunohistochemistry we retrospectively evaluated the correlations between Hsp10 expression and the clinicopathological characteristics of OSCC. Our results showed that percentage of high expression of Hsp10 in the OSCC was statistically higher than that in the non-cancerous squamous epithelium (P = 0.006). What is more, high Hsp10 expression was significantly associated with shorter overall survival in patients with OSCC (P<0.001). In addition, our results identified that the high expression of Hsp10 was significantly correlated with OSCC patients age, the history of chewing betel nut, pathological grade, lymph node metastasis and radiotherapy after operation (P = 0.008, P = 0.021, P = 0.026, P = 0.008, P = 0.049 respectively). Multivariate Cox regression analysis further identified that high expression of Hsp10 protein was an independent poor prognostic factor for OSCC (P<0.001). High Hsp10 expression might play important roles in the progression of OSCC, and it might act as a novel valuable independent biomarker to predict poor prognosis in patients with OSCC.