https://www.selleckchem.com/products/bt-11.html The expression levels of AFAP1-AS1 and HDGF were increased, while miR-545-3p was decreased in lung cancer tissues and cells. AFAP1-AS1 knockdown suppressed lung cancer cell proliferation, migration, and invasion and induced apoptosis. Furthermore, AFAP1-AS1 mediated cell progression through regulating miR-545-3p expression. In addition, miR-545-3p negatively regulated the expression level of HDGF via binding 3'-untranslated region of HDGF. As expected, AFAP1-AS1 knockdown inhibited lung cancer progression via affecting miR-545-3p/HDGF axis. Besides, AFAP1-AS1 knockdown suppressed lung cancer tumor growth in vivo. Collectively, our results suggested that AFAP1-AS1 promoted the development of lung cancer via regulating miR-545-3p/HDGF axis, providing a potential target for the treatment of lung cancer.Tyrosinase is a key enzyme for the biosynthesis of melanin pigments in peripheral tissues such as skin and retina. Although tyrosinase activity is specifically detected in melanocytes, several studies have shown the expression and enzymatic activity of tyrosinase in the central nervous system, especially in the midbrain substantia nigra. In the present study, we investigated the antioxidative effects of tyrosinase on protein damage in the substantia nigra of mice. C57BL/10JMsHir (B10) and tyrosinase-deficient albino B10.C-Tyrc/Hir (B10-c) mice were intraperitoneally administered retinol palmitate to induce oxidative stress, and the protein carbonyl content, a hallmark of protein oxidative damage, was examined in the substantia nigra. Retinol palmitate administration was found to decrease catalase activity in the substantia nigra of both B10 and B10-c mice, suggesting the induction of oxidative stress due to imbalanced antioxidant systems. In this model, we found that tyrosinase deficiency markedly increases the protein carbonyl content in the substantia nigra. Thus, we concluded that tyrosinase activity prevents protein dam