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@# Objective: To investigate the expression of Tim-3 on the surface of T cells in patients with esophageal cancer, and to explore its clinical significance. Methods: Fresh tumor tissues, paracancerous tissues, and peripheral blood were collected from 25 patients with esophageal cancer at the first affiliated Hospital of Zhengzhou University from September 2016 to April 2018. Peripheral blood from 10 healthy subjects was also collected during the same time period. The expressions of Tim-3, early apoptotic molecules and intrinsic factors in tumor tissues and peripheral blood PBMCs of 25 esophageal cancer patients were determined by flow cytometry. Also, the correlation between Tim-3+ T cell proportion and pathological parameters was investigated. The expression of Tim-3 in tumor tissues and paracancerous tissues was detected by fluorescence quantitative real-time polymerase chain reaction (qPCR). TCGA database was used to further verify the expression of Tim-3 in tumor tissues and paracancerous tissues, as well as its relationship with prognosis. Results: Tim-3 expression on T cells was higher in tumor tissues from esophageal cancer patients (P<0.01). Tim-3+ T cell function was in an exhausted status(P<0.05 or P<0.01), and the expression of Tim-3 on the surface of T cells in esophageal cancer microenvironment was closely related to lymph node metastasis and clinical staging (all P<0.01). Conclusion: Taken together, Tim3 expression on the surface of T cells could induce T cell dysfunction in patients with esophageal cancer, suggesting that Tim-3 may serve as a potential therapeutic target for esophageal cancer.
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Alzheimer’s disease (AD) is a common and devastating disease and there is no readily available biomarker to aid diagnosis or monitor progression of it. To further understand the pathogenic mechanism of AD, proteomic approach was used to study the cerebral synaptosomes proteins of rats injected with A1-40. Compared with the untreated samples, 14 proteins were found apparently altered through 2-dimensional gel electrophoresis. 12 of them were down-regulated and 2 were up-regulated. Three proteins including alpha-2-globin chain, peptidyl-prolycis-trans isomerase A (PPIaseA) and cofilin-1 protein were identified by matrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF-MS) and SWISS-PROT database query. Alpha-2-globin chain has not been shown to be associated with AD. PPIaseA and cofilin-1 protein are correlated with cell apoptosis and signaling. The altered proteins identified may help to understand the pathogenesis of AD.