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Zhao Huang,1,* Nan Ma,2,* Yan-Lu Xiong,1,* Lei Wang,1 Wei-Miao Li,1 Yuan-Yang Lai,1 Chen-Xi Zhang,1 Zhi-Pei Zhang,1 Xiao-Fei Li,1 Jin-Bo Zhao1 1Department of Thoracic Surgery, Tangdu Hospital, Fourth Military Medical University, Xi’an, Shaanxi 710038, People’s Republic of China; 2Department of Ophthalmology, Tangdu Hospital, Fourth Military Medical University, Xi’an, Shaanxi 710038, People’s Republic of China*These authors contributed equally to this workCorrespondence: Jin-Bo Zhao; Xiao-Fei LiDepartment of Thoracic Surgery, Tangdu Hospital, Fourth Military Medical University, 1 Xinsi Road, Baqiao, Xi’an, Shaanxi 710038, People’s Republic of ChinaTel +86 29 8471 7367Fax +86 29 8471 7367Email zhaojinbo@aliyun.com; lxfchest@fmmu.edu.cnPurpose: High metastasis is a leading risk factor for the survival of non-small cell lung cancer (NSCLC) and epithelial-mesenchymal transition (EMT) is a vital step of metastasis. The expression of novel oncogene with kinase domain (NOK) has been observed in some human malignancies, including non-small cell lung cancer (NSCLC); however, the biological function of NOK in NSCLC remains unclear. In the study, we explored the function of NOK in NSCLC, with an aim to elucidate the relevant underlying mechanisms.Patients and methods: We investigate the expression of NOK, p-Akt, p-GSK-3β, E-cadherin and N-cadherin expression by immunohistochemical analysis using tissue microarrays of 72 paired NSCLC samples of cancerous and adjacent normal tissues. The associations between NOK expression and clinicopathological factors, overall survival, other proteins were assessed. Immunofluorescence analysis of NSCLC tissues was performed to study the location of NOK, Akt and GSK-3β. Up or down-regulated of NOK were conducted in two NSCLC cell lines to analyze its impact on AKT/GSK3β pathway.Results: Statistical analysis revealed NOK expression increased in NSCLC tissues compared with normal tissues (P

24 model rabbits with femoral arterial thrombosis were divided into two groups: the treatment group consisting of 12 rabbits which received API0134, and the control group composed of another 12 rabbits. 2 hours after recanalization by urokinase thrombolysis, reocclusion occurred only in 1/12 vessel (8%) with incomplete occlusion in the treated group, but in 8/12 (67%) with complete occlusion in the control group as assessed by angiograsphy. Pathological examination of specimen taken 24 hours after thrombolysis showed that 6/12 (50%) of the treated group gave the evidence of thrombus occlusion, and milder intimal injury and less adhered blood cells than in the control group, 83% of which had thrombus occlusion. In comparision with the control group, the function of platelet in the treated group demonstrated lower platelet aggregation rate (PAgR) and plasma thromboxane A2 (TXA2) level, higher prostacyclin (PGI2) and plasminogen activator (PA) activity as well as lower plasminogen activator inhibitor (PAI) activity. From the above it may be concluded that the preventive effect of API0134 on reocclusion might be due to inhibition of platelets aggregation and promotion of fibrinolysis.

The experimental models of cultured porcine aortic endothelial cells (EC) in vitro were established. 6-keto-prostaglandin F1 alpha (6-keto-PGF1 alpha), thromboxane B2(TXB2)content, plasminogen activator (PA), plasminogen activator inhibitor (PAI) activity in cultured medium and cyclic adenosine monophosphate (cAMP) level in EC were measured with radioimmunoassay (RIA), chromogenic substrates methods, in order to assess the effect and mechanism of captopril (CP) on antithrombus function of EC. The results showed that after administration of CP, the contents of 6-keto-PGF1 alpha and cAMP and PA activity were significantly higher, PAI activity were remarkably lower than those of control group. These effects were dose-dependent. Our finding indicated that CP might act as a prospective drug for antithrombosis through promoting anticoagulation and fibrinolysis function and increasing antithrombus action of EC.