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Hiroshi Enomoto Ayako Sawa Hiroshi Suhara Noriyoshi Yamamoto Hiroyuki Inoue Chikako Setoguchi Fumio Tsuji Masahiro Okamoto Yoshimasa Sasabuchi Masato Horiuchi Masakazu Ban 《Bioorganic & medicinal chemistry letters》2010,20(15):4479-4482
A three substituted urea derivative, SA13353 (compound 1a), exhibited potent inhibitory activity against lipopolysaccharide (LPS)-induced TNF-α production. We focused on the 1,1-substituted moiety (R1 and R2) of SA13353 and investigated substituent effects of this moiety on LPS-induced TNF-α production by oral administration in rats. The synthesis of the urea derivatives was performed rapidly in a one-pot manner using a manual synthesizer. Several compounds containing hydrophobic substituents at this moiety showed more potent inhibitory activities than SA13353. 相似文献
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Francesca Rapino Eloy F. Robles Jose A. Richter-Larrea Eric M. Kallin Jose A. Martinez-Climent Thomas Graf 《Cell reports》2013,3(4):1153-1163
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Niacin is converted to NAD and NADP in tissues, whose products are involved in a number of cellular processes; and it is associated with the regulation of adipogenesis. In this study, we identified the molecular mechanism by which niacin promotes the adipogenesis in mouse 3T3-L1 cells. When the cells were cultured with niacin, the expression of adipogenic peroxisome proliferator-activated receptor γ, CCAAT enhancer binding protein (C/EBP)α, and their target genes was enhanced concomitant with an increase in triglyceride storage. Moreover, niacin suppressed the expression of cyclooxygenase-2 and decreased the production of prostaglandin (PG) F(2α) in the early phase of adipogenesis, which PG suppresses the progression of adipogenesis via the PGF(2α) receptor. Furthermore, niacin decreased the C/EBPβ level in the early phase of adipogenesis. These results indicate that niacin promoted adipogenesis by suppressing the production of the anti-adipogenic PGF(2α) through down-regulation of C/EBPβ-activated cyclooxygenase-2 expression in adipocytes. 相似文献
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The gene coding for β-galactosidase fromEscherichia coli was cloned into plasmid pACT71 containing the replicon from plasmid pAC1 fromAcetobacter pasteurianus. E. coli MC4100,E. coli JM105,E. coli LE392.23 andA. pasteurianus 3614 were transformed with the recombinant plasmid pACB815. Cells were cultivated in LB, YPG and M media supplemented with
glucose, glycerol, lactose or ethanol and β-galactosidase activity was detected in the cells and in the cultivation medium.
The best substrate for production of β-galactosidase was lactose. To release β-galactosidase fromA. pasteurianus cells amino acids were added to the cultivation medium. The highest secretory activity was achieved using 1.5% glycine after
36 h of cultivation in the M medium. 相似文献