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- 저자 : Kenichiro Mori (검색결과 3 건)
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Kenichiro Mori,Youn Uck Kim 한국미생물학회 2008 The journal of microbiology Vol.46 No.5
Benzoylecgonine is a major metabolite of cocaine. We generated hybridoma cells (C1303) producing antibenzoylecgonine monoclonal antibody (mAb) with a single-chain variable fragment (scFv) and an antigenbinding domain from the C1303 cells. Genes encoding an scFv antibody and constant region (Fc) were amplified from a cDNA library of C1303 cells using PCR. The two frameworks built for scFv and scFv-Fc consisted of HL [(heavy chain variable region, VH) - linker - (light chain variable region, VL)] and HL-Fc, respectively. A 45 base-pair-long sequence encoding (Gly₄-Ser)₃ was used as the linker, and the mouse IgG1 constant region sequence (225 amino acids) was used as the Fc domain. These two types of recombinant Abs were determined to be 750 bp in length (which corresponds to a 30 kDa protein) in the HL and 1,432 bp in length (which corresponds to a 65 kDa protein) in the HL-Fc, respectively. The parental Ab and HL-Fc affinities against benzoylecgonine were measured by ELISA and found to be nearly equal to the Ab concentration. We were also able to measure HL affinity using an agarose diffusion assay (Ouchterlony test). The affinity of the recombinant single-chain antibody against benzoylecgonine was sufficiently comparable to that of the parent antibodies to be used for the immunodetection of specific drug compounds or the detoxification of drug abusers by immunotherapy.
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김연욱,Katsuki Ohtani,Kenichiro Mori,장성재,Yasuhiko Suzuki,Nobutaka Wakamiya 한국유전학회 2011 Genes & Genomics Vol.33 No.3
Scavenger receptors including collection-placenta 1 (CL-P1)are cell surface glycoproteins capable of binding to oxidized low density lipoprotein (oxLDL), which are expressed on endothelial cells, macrophages, and smooth muscle cells. We cloned and characterized a 750 base-pair fragment containing the 5′-flanking region of the human CL-P1 gene using a human genomic library. The fragment obtained from the translational start site, which contained three specificity protein-1 (Sp1)sites upstream of transcriptional start site and putative binding sites for granulocyte chemotactic factor and early growth response factor-1, was ligated to the pGL4.10-basic vector, and promoter activity was confirmed by transfection studies. Luciferase and electrophoretic gel motility shift assays revealed that three Sp1 binding sites showed specific DNA-protein binding. Deletion and mutation analyses showed that the region comprising the three Sp1 sites was required for CL-P1proximal promoter activity in human umbilical vein endothelial cells, Hs683 cells, and SK-LMS cells. Furthermore, the third Sp1 (-28/-20) binding site was regulated through some factor, not the Sp1 protein, by hydrogen peroxide stimulation.
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Functional Analysis of Novel Collectins
SeongJae Jang,Atsushi Fukuoh,Katsuki Ohtani,Kenichiro Mori,Itsuro Yoshida,Yasuhiko Suzuki,Nobutaka Wakamiya 한국당과학회 2010 한국당과학회 학술대회 Vol.2010 No.1
Collectins are a family of collagenous calcium-dependent defense lectins in animals. Their polypeptide chains consist of four regions: a cysteine-rich N-terminal domain, a collagen-like region, an alpha-helical coiled-coil neck domain and a C-terminal lectin or carbohydrate-recognition domain. These polypeptide chains form trimers that may assemble into larger oligomers. The best studied family members are the mannan-binding lectin, which is secreted into the blood by the liver, and the surfactant proteins A and D, which are secreted into the pulmonary alveolar and airway lining fluid. The collectins represent an important group of pattern recognition molecules, which bind to oligosaccharide structures and/or lipid moities on the surface of microorganisms. Collectin placenta 1 (CL-P1), a recently discovered scavenger receptor, mediates the uptake of oxidized low density lipoprotein and microbes. In this study, we investigated CL-P1-mediated binding and ingestion of yeast-derived zymosan bioparticles using Chinese hamster ovary (CHO) cells stably expressing human CL-P1 (CHO/CL-P1) and human vascular endothelial cells constitutively expressed CL-P1. The uptake of zymosan by CHO/CL-P1 was dependent upon the level of CL-P1 expressed on the membrane and was inhibited by cytochalasin D and wortmannin. The binding of zymosan was also inhibited by ligands of other scavenger receptors such as poly(I) and dextran sulfate. Real time reverse transcription-PCR analyses showed that other scavenger receptors, namely LOX-1, Stabilin-2, or macrophage receptor with collagenous structure (MARCO), were not expressed in human umbilical vein endothelial cells isolated from different individuals. Nonopsonic zymosan ingestion was inhibited in three primary cultured vascular endothelial cells, including different human umbilical vein endothelial cells from nine individuals treated with CL-P1 small interfering RNAs (siRNAs), although small interfering RNAs of other scavenger receptors had no effect on zymosan uptake in these cells. Furthermore, we confirmed that CL-P1 is expressed in human and murine vascular endothelial layers. Our results demonstrated that CL-P1 predominantly mediated phagocytosis for fungi in vascular endothelia.
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