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Protein Kinase D1, a New Molecular Player in VEGF Signaling and Angiogenesis
하창훈,Zheng Gen Jin 한국분자세포생물학회 2009 Molecules and cells Vol.28 No.1
Vascular endothelial growth factor (VEGF) is essential for many angiogenic processes both in normal and pathologi-cal conditions. However, the signaling pathways involved in VEGF-induced angiogenesis are incompletely under-stood. The protein kinase D1 (PKD1), a newly described calcium/calmodulin-dependent serine/threonine kinase, has been implicated in cell migration, proliferation and mem-brane trafficking. Increasing evidence suggests critical roles for PKD1-mediated signaling pathways in endothelial cells, particularly in the regulation of VEGF-induced an-giogenesis. Recent studies show that class IIa histone deacetylases (HDACs) are PKD1 substrates and VEGF signal-responsive repressors of myocyte enhancer factor-2 (MEF2) transcriptional activation in endothelial cells. This review provides a guide to PKD1 signaling pathways and the direct downstream targets of PKD1 in VEGF signaling, and suggests important functions of PKD1 in angiogene-sis.
( Guo Hong Gong ),( Zhi Ming Zheng ),( Hui Liu,Li Wang ),( Jin Shan Diao ),( Peng Wang ),( Gen Hai Zhao ) 한국미생물 · 생명공학회 2014 Journal of microbiology and biotechnology Vol.24 No.6
An extracellular β-glucosidase from Aspergillus niger Au0847 was purified to homogeneity by precipitation with ammonium sulfate, anion exchange, and gel filtration. The purified protein was composed of two subunits with molecular masses of 110 and 120 kDa. Au0847 β-glucosidase exhibited relatively high thermostability and pH stability, and its highest activity was obtained at 65°C and pH 4.6, respectively. As a potential metalloprotein, its enzymatic activity was potently stimulated by manganese ion and DTT. The β-glucosidase displayed avid affinity and high catalytic efficiency for geniposide. Au0847 β-glucosidase has potential value as an industrial enzyme for the hydrolysis of geniposide to genipin.