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Expression of Human $\beta$-defensin 2 mRNA by Lipopolysaccharide in Human Corneal Epithelial Cells
Bae, Eon-Hee,Park, Keon-Wuk,Kim, Jong-Wook,Jang, Byeong-Churl,Lim, Ki-Jo,Jung, Tae-Young,Kwon, Young-Kyu,Shin, Sang-Woo,Kim, Sang-Pyo,Park, Jong-Hyun,Kwon, Taeg-Kyu,Baek, Won-Ki,Suh, Min-Ho The Korean Society for Microbiology 2004 Journal of Bacteriology and Virology Vol.34 No.1
Recently the transcriptional up-regulation of human $\beta$-defensin 2 (HBD-2) by lipopolysaccharide (LPS) was found to be associated with NF-${\kappa}B$ binding site. Although the general mechanisms of NF-${\kappa}B$ activation by LPS stimulation are well understood, less is known about the signal transduction pathway leading to LPS-induced NF-${\kappa}B$ activation in human corneal epithelial (HCE) cells. The aim of this study was to investigate the intracellular signals involved in LPS-induced HBD-2 mRNA expression in HCE cells. Pretreatments of inhibitors for NF-${\kappa}B$, protein tyrosine kinase, p38 mitogen activated protein kinase (MAPK), and c-Jun N-terminal kinase (JNK) attenuated the LPS-induced NF-${\kappa}B$ DNA binding activity and HBD-2 mRNA expression. Furthermore, pretreatments with inhibitors for protein kinase C (PKC), phosphatidylcholine-phospholipase C, phosphatidylinositol-phospholipase C, or phosphatidate phosphohydrolase prevented LPS-induced HBD-2 mRNA expression and HBD-2 promoter-driven luciferase activity. However, the increased expression of HBD-2 mRNA and the increased DNA binding activity of NF-${\kappa}B$ induced by LPS were not changed by the blockage of extracellular signal-regulated kinase (ERK) and of addition of antioxidants. Forskolin, a protein kinase A (PKA) agonist did not induce HBD-2 mRNA expression. These data demonstrate that LPS-induced HBD-2 mRNA expression via NF-${\kappa}B$ is, at least in part, dependent on PKC, p38 MAPK, JNK, and protein tyrosine kinase status, but appears to be independent on PKA, ERK and ROS in HCE cells. Taken together, there may be more than one signaling pathways that lead to LPS-induced up-regulation of HBD-2 mRNA expression in HCE cells.
Expression of Human β-defensin 2 mRNA by Lipopolysaccharide in Human Corneal Epithelial Cells
Eon-Hee Bae,Keon-Wuk Park,Jong-Wook Kim,Byeong-Churl Jang,Ki-Jo Lim,Tae-Young Jung,Young-Kyu Kwon,Sang-Woo Shin,Sang-Pyo Kim,Jong-Hyun Park,Taeg Kyu Kwon,Won-Ki Baek,Min-Ho Suh,Seong-Il Suh 대한미생물학회 2004 Journal of Bacteriology and Virology Vol.34 No.1
Nam, Soo Wan,Choi, Dae Keon,Ryu, Wuk Sang,Jang, Hyung Wook,Chung, Bong Hyun,Park, Young Hoon 한국미생물 · 생명공학회 1994 Journal of microbiology and biotechnology Vol.4 No.2
The β-1,4-endoglucanase gene from Actinomyces sp. 40 was cloned into Escherichia coli DH5α with pUC19. Chromosomal DNA from Actinomyces sp. 40 was cleaved with the restriction enzyme Sau3Al and ligated into pUC19 for the transformation of Escherichia coli DH5α. Positive clones of β-1,4-endoglucanase gene were detected as the clear zones on a medium supplemented with carboxymethylcellulose (CMC). This transformant possessed a single plasmid, designated pDS1, which contained the vector DNA and a 3.5 kilobase (kb) Sau3Al insertion fragment encoding endoglucanase. The size of the cloned fragment was reduced to 2.0 kb. The endoglucanase activity produced by the E. coli DH5a (pDS6) was higher than that of Actinomyces sp. 40 strain. The optimum pH and temperature of the cloned enzyme were pH 4.0∼5.0 and 55℃, respectively. The cloned enzyme was stable at 55℃ or below and in buffer ranging from pH 4.0 to 7.0. The enzyme degraded CMC but did not degrade xylan, cellobiose, and methyl-umbelliferylcellobiopyranoside (MUC).