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Mechanism for the Differentiation of EoL-1 Cells into Eosinophils by Histone Deacetylase Inhibitors
Kaneko, Motoko,Ishihara, Kenji,Takahashi, Aki,Hong, JangJa,Hirasawa, Noriyasu,Zee, OkPyo,Ohuchi, Kazuo S.Karger 2007 International archives of allergy and immunology Vol.143//SUP1 No.-
<P><I>Background:</I> EoL-1 cells have a <I>FIP1L1-PDGFRA</I> fusion gene which causes the transformation of eosinophilic precursor cells into leukemia cells. Recently, we suggested that the induction of differentiation of EoL-1 cells into eosinophils by the HDAC inhibitors apicidin and n-butyrate is due to the continuous inhibition of HDACs. However, neither apicidin nor n-butyrate inhibited the expression of FIP1L1-PDGFRA mRNA, although both these inhibitors suppressed cell proliferation. Therefore, in this study, we analyzed whether the levels of FIP1L1-PDGFRα protein and phosphorylated-Stat5 involved in the signaling for the proliferation of EoL-1 cells are attenuated by HDAC inhibitors. <I>Methods:</I> EoL-1 cells were incubated in the presence of apicidin, TSA or n-butyrate. FIP1L1-PDGFRα and phosphorylated-Stat5 were detected by Western blotting. <I>Results:</I> Treatment of EoL-1 cells with apicidin at 100 n<I>M</I> or n-butyrate at 500 μ<I>M</I> decreased the levels of FIP1L1-PDGFRα protein and phosphorylated-Stat5, while that with trichostatin A at 30 n<I>M</I> did not. <I>Conclusions:</I> The decrease in the level of FIP1L1-PDGFRα protein caused by apicidin and n-butyrate might be one of the mechanisms by which EoL-1 cells are induced to differentiate into eosinophils by these HDAC inhibitors.</P><P>Copyright © 2007 S. Karger AG, Basel</P>
Unscheduled Hospitalization in Adults with Congenital Heart Disease
Jun Negishi,Hideo Ohuchi,Kenji Yasuda,Aya Miyazaki,Nakanishi Norifumi,Osamu Yamada 대한심장학회 2015 Korean Circulation Journal Vol.45 No.1
Background and Objectives: Little information is available regarding adult patients with congenital heart disease (CHD) who needed unscheduledhospitalization (USH). This paper aims to elucidate the clinical features of adult patients with CHD requiring USH. Subjects and Methods: Study subjects included patients with CHD aged 18 years or older who were hospitalized at our facility during a5-year study period. Medical records were retrospectively reviewed and data regarding USH were collected. Patient’s background, underlyingheart disease, cause of hospitalization, and prognosis (second USH regardless of cause or death) were examined. Results: Overall, 959 CHD patients underwent a total of 1761 hospitalizations, including 145 patients who were unexpectedly hospitalized239 times. The median age at USH was 27 years old. Of the 959 patients, 54% were male. Underlying heart diseases included repaired tetralogyof Fallot (21%), single ventricular physiology after Fontan operation (17%), and Eisenmenger syndrome (12%). The causes of USH includedarrhythmia (40%), heart failure (20%), infectious disease (13%), and hemorrhage or thrombus (13%). A total of 48 patients requiredreadmission. In total, 13 patients died, including four hospital deaths. The USH-free survival rate was 77% for 1 year and 58% for 3 years. Conclusion: The rate of USH was high for adults with complicated CHD. Common causes of USH included arrhythmia, heart failure, hemorrhage-related or thrombus-related conditions and infection. These data provide the current status of medical care for adult CHD patientsin Japan and their therapeutic needs.
Hong, JangJa,Yokomakura, Aya,Nakano, Yasuhiro,Ban, Hyun Seung,Ishihara, Kenji,Ahn, Jong-Woong,Zee, OkPyo,Ohuchi, Kazuo Williams Wilkins 2005 The Journal of Pharmacology and Experimental Thera Vol.312 No.3
<P>We previously reported that apicularen A [2,4-heptadienamide, N-[(1E)-3-[(3S,5R,7R,9S)-3,4,5,6,7,8,9,10-octahydro-7,14 dihydroxy-1-oxo-5,9-epoxy-1H-2-benzoxacyclododecin-3-yl]-1 propenyl]-, (2Z,4Z)-(9CI)], a highly cytostatic macrolide isolated from the myxobacterial genus Chondromyces, induces apoptosis in the mouse leukemic monocyte cell line RAW 264.7. To analyze the action mechanism of apicularen A for the induction of apoptosis, effects of apicularen A on nitric oxide (NO) production in RAW 264.7 cells were examined. It was demonstrated that apicularen A at 10 and 100 nM induced nitrite production, whereas apicularen B [2,4-heptadienamide, N-[(1E)-3-[(3S,5R,7R,9S)-7-[[2-(acetylamino)-2-deoxy-beta-d-glucopyranosyl]oxy]-3,4,5,6,7,8,9,10-octahydro-14-hydroxy-1-oxo-5,9-epoxy-1H-2-benzoxacyclododecin-3-yl]-1 propenyl]-, (2Z,4Z)-(9CI)], an N-acetyl-glucosamine glycoside of apicularen A, had no effect at 100 nM. The apicularen A-induced nitrite production was accompanied by an increase in the level of inducible nitric-oxide synthase (iNOS) and its mRNA and was suppressed by the NOS inhibitor N(G)-monomethyl-l-arginine acetate (l-NMMA). In addition, apicularen A activated nuclear factor-kappaB (NF-kappaB) and activator protein-1 (AP-1) and decreased the level of IkappaB-alpha and increased that of phosphorylated c-Jun N-terminal kinase (JNK). Furthermore, the apicularen A-induced nitrite production was suppressed by the NF-kappaB inhibitor Bay 11-7082 [(E)-3-(4-methylphenylsulfonyl)-2-propenenitrile] and the JNK inhibitor SP600125 [anthra[1,9-cd]pyrazol-6(2H)-one]. These findings suggested that apicularen A activates NF-kappaB and AP-1, thus triggering the expression of iNOS mRNA and iNOS protein and induces NO production. Finally, apicularen A decreased cell growth and survival and cell viability and disrupted the mitochondrial membrane potential. The addition of l-NMMA partially recovered the apicularen A-induced decrease in cell growth and survival and cell viability and the disruption of mitochondrial membrane potential. These findings suggested that NO produced by apicularen A treatment participate partially in the apicularen A-induced apoptosis in RAW 264.7 cells.</P>
Purification, characterization and gene cloning of metalloprotease from Nomuraea atypicola
Naomi Yamamoto,Mitsuhiro Ueda,Mizuho Kusuda,Masami Nakazwa,Kenji Ohuchi,Minoru Sakaguchi,Kuniyo Inouye,Kazutaka Miyatake 한국버섯학회 2010 한국버섯학회지 Vol.8 No.4
We have purified and characterized of metalloprotease metalloprotease from Nomuraea atypicola. N. atypicola was cultured in Sabouraud medium supplemented with powdered pupae. The metalloprotease from culture supernatant was purified to electrophoretically homogeneous state. The molecular mass of metalloprotease from N. atypicola was 50 kDa. The enzyme was most active at pH 8.5 and 40oC and stable at pH 5.0-7.0 and up to 40oC. The activity was inhibited by o-phenanthroline and EDTA. The N-terminal amino acid sequence of the enzyme showed a similarity to those of proteases (Metallo peptidase M36 family (Fungalysin)) from Coccidioides posadasii and Aspergillus fumigatus. The enzyme was found to be Fungalysin-like metalloprotease. cDNA encoding metalloprotease from N. atypicola was amplified by PCR using oligonucleotides deduced from the N-terminal endo peptide sequence, 5’- and 3’-RACE. Predicted enzyme structure consists of 637 amino acids with pro- and signal sequences. The mature enzyme had 391 amino acids and its deduced amino acid sequence coincided completely with the N- terminal amino end (20 amino acids) of metalloprotease purified from N. atypicola. We are studying on expression of the metalloprotease gene in Escherichia coli.