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Isolation of Ich-1S (caspase-2S)-binding protein that partially inhibits caspase activity 査読

A Ito, T Uehara, Y Nomura

FEBS LETTERS 470 ( 3 ) 360 - 364 2000年3月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：ELSEVIER SCIENCE BV

Members of the caspase family are essential executors of apoptosis, Caspase-2 has two messenger RNAs generated by alternative splicing, which encode caspase-2L and caspase-2S, Although caspase-2L induces apoptosis, caspase-2S also has the ability to antagonize cell death. Experiments in caspase-2-deficient mice showed that caspase-2 functions to delay cell death in some neuronal populations, suggesting that caspase-2S dominantly acts for cell survival in the brain, However, the mechanism of caspase-2S-mediated anti-apoptotic effect is still unclear. Here. we isolated a protein that interacts with caspase-2S, designated as Ich-1S (caspase-2S)-binding protein (ISBP), by yeast two-hybrid screening using full-length caspase-2S cDNA as a bait. ISBP is identical to the recently isolated calcium and integrin-binding protein, and a small molecule calcium-binding protein with two EF-hand motifs of its C-terminus. In vitro transcribed and translated ISBP interacts specifically with glutathione-S-transferase-fused caspase-2S, Moreover, the interaction between ISBP and caspase-2S was observed in cultured cells, Northern blot analysis indicated that ISBP may be a ubiquitous protein. Interestingly, ISBP can partially inhibit the processing of pro-caspase-2L induced by anti-Fas antibody-treated Jurkat cytosolic lysates, These results suggested that ISBP mag be the mediator for the survival function of caspase-2S. (C) 2000 Federation of European Biochemical Societies.

DOI： 10.1016/S0014-5793(00)01351-X

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Possible involvement of cytochrome c release and sequential activation of caspases in ceramide-induced apoptosis in SK-N-MC cells. 査読

Ito A, Uehara T, Tokumitsu A, Okuma Y, Nomura Y

Biochimica et biophysica acta 1452 ( 3 ) 263 - 274 1999年12月

Transient nuclear factor kappaB (NF-kappaB) activation stimulated by interleukin-1beta may be partly dependent on proteasome activity, but not phosphorylation and ubiquitination of the IkappaBalpha molecule, in C6 glioma cells. Regulation of NF-kappaB ・・・

Uehara T, Matsuno J, Kaneko M, Nishiya T, Fujimuro M, Yokosawa H, Nomura Y

J. Biol. Chem. 274 ( 22 ) 15875 - 15882 1999年5月

記述言語：英語掲載種別：研究論文（学術雑誌）

DOI： 10.1074/jbc.274.22.15875

Possible involvement of p38 MAP kinase in HSP70 expression induced by hypoxia in rat primary astrocytes 査読

T Uehara, M Kaneko, S Tanaka, Y Okuma, Y Nomura

BRAIN RESEARCH 823 ( 1-2 ) 226 - 230 1999年3月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：ELSEVIER SCIENCE BV

The aim of this study was to elucidate the possible mechanism of HSP induction in response to hypoxia in rat primary astrocytes. Treatment with SB203580, a selective p38 MAP kinase (p38 MAPK) inhibitor, attenuated the increase in HSP70 in a concentration-dependent manner. p38 MAPK was activated in response to hypoxic treatment. These results suggest that p38 MAPK positively regulates hypoxia-induced HSP70 expression in astrocytes. (C) 1999 Elsevier Science B.V. All rights reserved.

DOI： 10.1016/S0006-8993(99)01178-6

グリア細胞のiNos，ケモカイン発現に関わるNF-κB系活性制御と薬物作用

野村靖幸, 上原孝, 西屋禎

日本薬理学雑誌 114 92 - 95 1999年

記述言語：日本語出版者・発行元：公益社団法人日本薬理学会

転写因子NF-κBの活性制御機構を明らかにするために，ラットC6グリオーマ細胞を使用し，細菌内毒素(LPS)/IFNγ刺激に伴う誘導型NO合成酵素(iNOS)発現，およびIL-1β刺激に伴うケモカイン(CINC)発現へのNF-κB活性化(p50·p65·IκBαの複合体よりIκBαを脱離し，活性2量体p50·p65を形成する反応)の関与とその機構を検討した．その結果，優性抑制変異型IκBαを強制発現したC6細胞では，LPS/IFNγによるiNOS発現が抑制されることからNF-κB/IκBαがiNOS発現に重要な役割を果たすこと，またIL-1βによるCINC発現にはNF-κBが深く関わること，さらに一過性のNF-κB活性化にはIκBαのリン酸化，ユビキチン化よりもプロテアソーム活性が関わることが示された．この結果は，脳虚血などのストレスに伴う脳ニューロン死や浮腫の発症に関わるNF-κB活性化系を標的とする新規抗脳梗塞薬の開発に有用な示唆を与えると考えられる．

DOI： 10.1254/fpj.114.supplement_92

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その他リンク： https://jlc.jst.go.jp/DN/JALC/00304061547?from=CiNii

Regulation of Bcl-2 protein expression in human neuroblastoma SH-SY5Y cells: Positive and negative effects of protein kinases C and A, respectively 査読

Y Itano, A Ito, T Uehara, Y Nomura

JOURNAL OF NEUROCHEMISTRY 67 ( 1 ) 131 - 137 1996年7月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：LIPPINCOTT-RAVEN PUBL

The regulatory mechanism of Bcl-2 protein expression was investigated in SH-SY5Y cells, the human neuroblastoma cell line that expresses natively Bcl-2 proteins. When the cells were treated with 12-O-tetradecanoylphorbol 13-acetate (TPA) or retinoic acid, the level of Bcl-2 protein was increased compared with the control. These effects were inhibited by pretreatment with a protein kinase C (PKC) inhibitor, staurosporine or calphostin C. The level of Bcl-2 protein was also increased by treatment with carbachol, a muscarinic acetylcholine receptor (mAChR) agonist, and the effects were also inhibited by pretreatment with staurosporine or calphostin C. In addition, a carbachol-induced increase in Bcl-2 protein levels and a transient elevation of [Ca2+](i) were inhibited by pretreatment with 4-DAMP (4-diphenylacetoxy-N-methylpiperidine), an m(3) mAChR antagonist. In contrast, the level of Bcl-2 protein was decreased by treatment with dibutyryl cAMP (diBu-cAMP), forskolin, or cholera toxin, and the effects of diBu-cAMP were inhibited by pretreatment with a protein kinase A (PKA) inhibitor, H-89. From these results, we suggest that the expression of Bcl-2 proteins is regulated by PKC and PKA in positive and negative manners, respectively, in SH-SY5Y cells. Furthermore, the nucleosomal DNA fragmentation induced by serum depletion for 4 h was observed in SH-SY5Y cells when the level of Bcl-2 protein was down-regulated by treatment with 1 mM diBu-cAMP for 3 days, although the DNA fragmentation by serum depletion for 4 h was not observed in nontreatment cells, indicating that Bcl-2 proteins whose expression is regulated by PKC and PKA play important roles in serum depletion-induced apoptosis.

DOI： 10.1046/j.1471-4159.1996.67010131.x

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Possible involvement of phosphatidylinositol-specific phospholipase C related to pertussis toxin-sensitive GTP-binding proteins during adipocyte differentiation of 3T3-L1 fibroblasts: Negative regulation of protein kinase C 査読

Takashi Uehara, Shin-ichi Hoshino, Michio Ui, Yukiko Tokumitsu, Yasuyuki Nomura

BBA - Molecular Cell Research 1224 ( 2 ) 302 - 310 1994年11月

記述言語：英語掲載種別：研究論文（学術雑誌）

Insulin/dexamethasone/methylisobutylxanthine (hormones/IBMX) induce 3T3-L1 fibroblasts to differentiate into adipocytes. Our previous study suggested that pertussis toxin (IAP)-sensitive GTP-binding protein(s) (G-protein) is involved in the process of differentiation by hormones/IBMX, accompanied by c-fos induction. Northern blotting indicated that among the IAP-sensitive G-proteins, the levels of Gi2α, Goα, and Gi3α mRNA were decreased, increased and unchanged, respectively. Gi1α was undetectable and IAP attenuated the decrease in Gi2α mRNA level but did not affect the change in Goα mRNA level during the adipocyte differentiation. These results indicate that IAP-sensitive Gi2α mRNA level is decreased during adipocyte differentiation. A combination of phosphatidylinositol-specific phospholipase C (PI-PLC) and IBMX induced c-fos expression in 3T3-L1 fibroblasts similar to that induced with hormones/IBMX. c-fos induced by both stimulators was also diminished by anti-inositolglycan antibody or anti-PI-PLC antiserum. Insulin stimulated the release of inositolproteoglycan and diacylglycerol from 3T3-L1 fibroblasts, which was suppressed by IAP treatment. These findings suggested that one of the pathways of adipocyte differentiation induced by hormones/IBMX occurs via the inositolglycan-specific PI-PLC cascade coupled to IAP-sensitive G-protein(s). Both activation of glycerophosphate dehydrogenase and stimulation of insulin-dependent 2-deoxyglucose uptake induced by hormones/IBMX were enhanced in protein kinase C-depleted cells exposed to phorbol 12-myristate 13-acetate (PMA), and attenuated in IAP-treated cells. The level of a 32P-labeled 52 kDa protein in plasma membrane fractions immunoprecipitated by anti-PI-PLC antiserum was increased by PMA stimulation, abolished in PMA-treated cells, and increased in IAP-treated cells. These findings suggest that protein kinase C phosphorylates PI-PLC, resulting in a decrease in PI-PLC activity related to the signal transduction pathway of adipocyte differentiation of 3T3-L1 fibroblasts. © 1994.

DOI： 10.1016/0167-4889(94)90204-6

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