• Title/Summary/Keyword: c-jun

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Piezoelectric and Electrostriction Properties of Electrostriction Ceramic Prepared by Double Calcination (이단하소법에 의해 제조된 전왜세라믹의 압전 및 전왜특성)

  • Lee, S.H.;Yoo, K.M.;Cho, H.C.;Kim, H.G.;SaGong, G.
    • Proceedings of the KIEE Conference
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    • 1997.07d
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    • pp.1326-1329
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    • 1997

  • In this paper, PNN-PZN-PZT ceramics were fabricated with various mole ratio of the PZT[$Pb(Zr_{1/2}Tid_{1/2})O_3$]. PNN [$Pb(Ni_{1/3}Nb_{2/3})O_3$] and PZN[$Pb(Ni_{1/3}Nb_{2/3})O_3$ powders prepared by double calcination and PZT powders prepared by molten-salt synthesis method. The formation rate of perovskite phase in PNN-PZN-PZT ceramics could be obtained about 92% at PZT 0.3 mole ratio. The relative permittivity of specimen with PZT 0.3 mole ratio was shown 5,320 and appeared the relaxor ferroelectric feature. The maximum piezoelectric coefficient $d_{31}$ to be used for evaluation the displacement of piezoceramics in PNN-PZN-PZT ceramics was $324{\times}10^{-12}$(C/V) at the vicinity of morphotropic phase boundary and was larger than that of solid PZT ceramics($120{\times}10^{-12}C/V$).

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Inhibition of the Jun Aminoterminal Kinase by SP600125 Blocks PMA-Induced 92kDa Type IV Collagenase Secretion (PMA 유도 제4형 단백분해효소 분비를 차단하는 SP600125에 의한 Jun Aminoterminal Kinase의 억제)

  • Shin, Min
    • Journal of Oral Medicine and Pain
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    • v.26 no.2
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    • pp.95-105
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    • 2001

  • 제 4형 콜라젠을 분해하는 MMP-9은 조직 재생에 중요한 역할을 하기 때문에 주목받아 왔는데, 이전의 문헌들에서 PMA에 의해 이 유전자 발현이 강하게 상승발현된다고 알려져 있다. 비록 MMP-9 발현을 조절하는 PMA의 기전이 잘 밝혀지지는 않았지만, 다른 유전자발현에서의 이 phorbol ester의 효과는 c-raf-1-ERK 신호전달통로의 활성에 관해 연구되어 오고 있다. 하지만 이번 연구에서 저자는 MMP-9 발현에서 PMA의 상승효과에는 대개는 스트레스성 자극과 관련된 JNK1 의존성 신호전달과정이 또한 필요하다는 다른 가능성을 조사하였다. 그 결과 JNK 억제재중 하나인 SP 600125가 UM-SCC-1세포주에서 PMA에 의해 유도된 MMP-9 상승발현을 용량의존적으로 억제하는 것으로 나타났고 72시간동안 전처치를 한 경우에 그의 억제효과가 최대이었다. phorbol ester로 처리한 세포에 GAL4 luciferase reporter와 vector를 주입해서 조사한 결과 PMA가 c-Jun transacting 활성을 상승시켰다. 그뿐 아니라 PMA에 의한 MMP-9 촉진자 활성에는 AP-1 motif가 필요하며 이 motif에 c-Jun이 결합하는 것을 EMSA를 통해 확인하였다. 결론적으로 UM-SCC-1 세포주에서 PMA에 의한 MMP9의 증가된 발현은 이미 밝혀진 ERK 경로뿐 아니라 JNK 경로를 통한 결과임이 밝혀져 이 경로를 차단하는 방법이 또하나의 암치료 방향을 제시해주고 있다.

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Protein Kinase A Functions as a Negative Regulator of c-Jun N-terminal Kinase but not of p38 Mitogen-activated Protein Kinase in PC12 Cells

  • Hur, Kyu-Chung
    • Animal cells and systems
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    • v.9 no.3
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    • pp.173-179
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    • 2005

  • Cyclic-AMP-dependent protein kinase (PKA) seems to function as a negative regulator of the c-Jun $NH_2-terminal$ kinase (JNK) signaling pathway. We demonstrate here that the activity of the PKA catalytic subunit (PKAc) is reduced in apoptotic PC12 pheochromocytoma cells. Apoptotic progress was inhibited by dibutyryl cyclic AMP (dbcAMP), an analog of cAMP. The rescue by dbcAMP was attributable to inhibition of the JNK but not of the p38 signaling pathway, due to the induction of PKA activity. JNK was present in immunocomplexes of PKAc, and PKAc phosphorylated JNK in vitro. Presence of p38 kinase, however, was not prominent in immunocomplexes of PKAc. Our data suggest that JNK is a target point of negative regulation by PKAc in the JNK signaling pathway.

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Inhibition of C2-ceramide induced contraction in cat esophageal smooth muscle cell by newly synthesized Ceramide analogues

  • Lee, Doo-Won;Yang, Sung-Jun;Lee, Yul-Pyo;Lee, Tai-Sang;Park, Jun-Hong;Choi, Su-Hang;Yim, Chul-Bu;Sohn, Uy-Dong;Choi, Tae-Sik
    • Proceedings of the PSK Conference
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    • 2002.10a
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    • pp.248.1-248.1
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    • 2002

  • It has been shown that C2-ceramide (C2), short chain ceramide, plays a role in mediating contraction of cat esophageal smooth muscle cells. We examined the effect of newly synthesized ceramide analogues on the C2-ceramide induced contraction in esophageal smooth muscle cells isolated with collagenase. C2-ceramide produced contraction of smooth muscle cells in a dose dependent manner. (omitted)

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Phosphorylation of Transcriptional Factor by Mitogen-activated Protein (MAP) Kinase Purified from Nucleus (핵 내에서 분리한 Mitogen-Activated Protein (MAP) Kinase의 Transcription Factor에 대한 인산화)

  • 김윤석;김소영;김태우
    • Biomedical Science Letters
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    • v.2 no.2
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    • pp.175-185
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    • 1996

  • The mitogen-activated protein(MAP) kinase signal transduction pathway represents an important mechanism by which mitogen, such as serum and PMA, regulate cell proliferation and differentiation. Target substrates of the MAP kinase are located within several compartments containing plasma membranes and nucleus. We now report that serum addition induces proliferation of the P388 murine leukemia cell, but PMA does not, while both serum and PMA treatment cause translocation of the MAP kinase, mainly p42$^{mapk}$ isoform, from cytosol into the nucleus, which was monitored by immunoblot analysis using polyclonal anti-ERK1 antibodies. We investigated whether the MAP kinase was capable of phosphorylating c-Jun protein and GST-fusion proteins, the P562$^{kk}$N-terminal peptides (1-77 or 1-123 domain) of the T cell tyrosine kinase, using the partially purified MAP kinase by SP-sephadex C-50, phenyl superose and Mono Q column chromatography. We found that the partially purified MAP kinase was able to phosphorylate c-Jun protein and the GST-fusion protein expressed using E.coli DH5$\alpha$ which is transformed with pGEX-3Xb plasmid vector carrying of p562$^{kk}$N-terminal peptide-encoding DNA. These results imply that tyrosine kinase receptor/Ras/Raf/MAP kinase pathway is a major mechanism for mitogen-induced cell proliferation in P388 murine leukemia cell and that the various MAP kinase isoforms may have their own target substrates located in distinct subcellular compartments.

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