Increase of cyclin B by overexpression of cystatin α

Hiwasa, Takaki; Ma, Jun; Ike, Yoshimasa; Katunuma, Nobuhiko; Sato, Shigeru

doi:10.1002/cbf.290130411

Cited by 15 publications

(10 citation statements)

References 16 publications

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“…After isolating G418-resistant clones, the expression of calpastatin in each clone was examined before and after treatment with a synthetic glucocorticoid, dexamethasone (Dex), as described. 39 Two of the transfected clones, TnMc-17 and -22, expressed high levels of calpastatin after treatment with Dex while the empty-vector-transfected control Tn-V cells showed barely detectable levels of calpastatin irrespective of Dex treatment ( Figure 5A). …”

Section: Sensitization To Pep By Calpain Inhibitor Allnmentioning

confidence: 93%

Enhancement of chemosensitivity toward peplomycin by calpastatin-stabilized NF-κB p65 in esophageal carcinoma cells: possible involvement of Fas/Fas-L synergism

et al. 2006

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Chemosensitivity to anticancer drugs was compared between two human esophageal carcinoma cell lines, T.Tn and YES-6 cells. T.Tn cells were more resistant than YES-6 cells to peplomycin (PEP) but not to the other anticancer drugs such as camptothecin, mitomycin C and cytosine arabinoside. Western blot analysis showed higher expression levels of m-calpain and activated mu-calpain in T.Tn cells than in YES-6 cells. On the other hand, YES-6 cells showed a high expression level of calpastatin, which is a calpain-specific endogenous inhibitor. To investigate whether calpain activity was involved in the chemosensitivity, T.Tn cells were transfected with calpastatin cDNA in an inducible expression vector. The induction of calpastatin was accompanied by increased chemosensitivity to PEP. The increases in calpastatin levels were followed by serial increases in the expression levels of NF-kappaB p65 and Fas. Since purified m- or mu-calpain degraded NF-kappaB p65 in vitro, it is possible that calpastatin suppressed calpain-mediated degradation of NF-kappaB p65. Fas ligand (Fas-L) protein levels increased after treatment of the parental T.Tn and calpastatin-transfected cells with PEP, suggesting the synergism between calpastatin-induced Fas and PEP-induced Fas-L. These results suggest that calpain/calpastatin expression levels are effective markers for predicting the sensitivity of human esophageal carcinoma cells to PEP.

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Section: Sensitization To Pep By Calpain Inhibitor Allnmentioning

confidence: 93%

Enhancement of chemosensitivity toward peplomycin by calpastatin-stabilized NF-κB p65 in esophageal carcinoma cells: possible involvement of Fas/Fas-L synergism

et al. 2006

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“…70 Immunoblot analysis was carried out using ECL system (Amersham) as described previously. 71 The antibodies used were anti-Src (Oncogene Science), anti-PKCa, PKCg, PKCz, PKCl, PKCm and PKCy, anti-p53 (Transduction Laboratories), anti-Bax (Santa Cruz Biotechnology), anti-m-calpain and anti-m-calpain (Chemicon International, Temecula, CA, USA), anti-calpastatin (Takara, Kyoto, Japan) and anti-activated m-calpain antibodies. 48 …”

Section: Preparation Of Cell Extract and Immunoblot Analysismentioning

confidence: 99%

Increase in ultraviolet sensitivity by overexpression of calpastatin in ultraviolet-resistant UVr-1 cells derived from ultraviolet-sensitive human RSa cells

et al. 2000

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Human RSa cells are highly sensitive to apoptotic-like cell death by ultraviolet irradiation (UV) while UV r -1 cells are their variant with an increased resistance to UV. Three days after UV at 10 J/m 2 , the viability of RSa cells was approximately 17% while that of UV r -1 cells was 65%. This different survival might reflect apoptotic cell death since apoptosis-specific DNA ladder was more clearly observed in RSa cells than in UV r -1 cells after UV. Addition of ALLN/calpain inhibitor I to the culture medium after UV resulted in similar survival (14 ± 18%) between RSa and UV r -1 cells. Immunoblot analysis showed down-regulation of protein kinase Cy, Src, Bax and m-calpain after UV was more prominent in UV r -1 than in RSa cells. Activated m-calpain appeared within 1 h post-UV only in UV r -1 cells. The expression of calpastatin, a specific endogenous inhibitor of calpain, was higher in RSa than in UV r -1 cells. To further examine the role of calpain in UV-induced cell death, cDNA of human calpastatin was transfected into UV r -1 cells. The results showed that overexpression of calpastatin suppressed down-regulation of Src, m-calpain and Bax. Concomitantly, colony survival after UV was reduced in calpastatin-transfected cells as compared to vector control cells. Our results suggest that activation of calpain might account for, at least in part, the lower susceptibility to UVinduced cell death in UV r -1 cells. Cell Death and Differentiation (2000) 7, 531 ± 537.

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“…If the decrease in PKC is caused by calpain, the level of PKC might increase by a calpain inhibitor. FMD6, another DAN ‐transfected ras‐NIH clone, was treated with a calpain inhibitor, ZLLH [12], for 24 h and PKC was examined by immunoblot. FMD6 showed a similar decrease in PKCα without Dex treatment compared with a vector control, FVE8, probably due to a leaked expression of DAN (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Cells were lysed in 0.5% Nonidet P‐40, 20 mM Tris‐HCl (pH 7.5), 1 mM EDTA, 1 mM EGTA, 1 mM phenylmethylsulfonyl fluoride and 50 μM N ‐acetyl‐leucyl‐leucyl‐norleucinal as described, incubated at 0°C for 10 min and centrifuged at 13 000× g for 10 min. The supernatant was then electrophoresed through an SDS‐polyacrylamide gel followed by immunoblot analysis using affinity‐purified anti‐rat DAN polyclonal antibody [3, 4], anti‐PKC antibody (Amersham), anti‐PKCα, ‐β, ‐γ, ‐δ, ‐ϵ, ‐ι, ‐μ, ‐θ, ‐λ and ‐ζ antibodies (Transduction Laboratories), and anti‐150‐kDa‐non‐erythroid α‐spectrin (fodrin) antibody [11], as described previously [12].…”

Section: Methodsmentioning

confidence: 99%

Down‐regulation of protein kinase Cα and γ and enhanced TPA‐induced neurite formation in DAN‐transfected neuroblastoma cells

et al. 1998

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DAN gene was first isolated by differential screening between rat 3Y1 and v-src-transformed 3Y1 cells and showed a tumor-suppressive activity toward v-src-transformed 3Y1 cells. When DAN-transfected neuroblastoma cells were treated with a tumor promoter phorbol ester, TPA, neurite-like processes appeared within 2 h whereas no apparent change was observed in the parent and vector-transfected cells up to 8 h. This suggests some difference in TPA-receptor, protein kinase C (PKC), between DAN-transfectants and the control cells. DAN-transfected SH-SY5Y cells showed complete loss in PKCK K and a large decrease in PKCQ Q. Similar down-regulation in PKCK K and PKCQ Q was also observed in DAN-transfected Ha-ras-transformed NIH 3T3 cells. The decreased level of PKCK K was partially recovered after treatment with a calpain inhibitor, ZLLH. A 150-kDa proteolytic product of a calpain-specific substrate, non-erythroid K K-spectrin, was detectable in DAN-transfected SH-SY5Y cells but not in the parent or vector-transfected control cells. This suggests that DAN-transfected cells contain activated calpain which may cause down-regulation of PKC and hence induce the altered TPA response.z 1998 Federation of European Biochemical Societies.

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Increase of cyclin B by overexpression of cystatin α

Cited by 15 publications

References 16 publications

Enhancement of chemosensitivity toward peplomycin by calpastatin-stabilized NF-κB p65 in esophageal carcinoma cells: possible involvement of Fas/Fas-L synergism

Enhancement of chemosensitivity toward peplomycin by calpastatin-stabilized NF-κB p65 in esophageal carcinoma cells: possible involvement of Fas/Fas-L synergism

Increase in ultraviolet sensitivity by overexpression of calpastatin in ultraviolet-resistant UVr-1 cells derived from ultraviolet-sensitive human RSa cells

Down‐regulation of protein kinase Cα and γ and enhanced TPA‐induced neurite formation in DAN‐transfected neuroblastoma cells

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