Efficient gene activation in mammalian cells by using recombinant adenovirus expressing site-specific Cre recombinase

Kanegae, Yumi; Lee, G; Sato, Yuichi; Tanaka, Masayuki; Nakai, Michiko; Sakaki, Toshiyuki; Sugano, Sumio; Saito, Izumu

doi:10.1093/nar/23.19.3816

Cited by 590 publications

(438 citation statements)

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“…Adenoviral expression of JDP2 and adipocyte induction. The Adeno-JDP2 vector was constructed by inserting JDP2 cDNA into pAxCAwt 33 and infectious viral particles were produced and purified as described elsewhere. 34 3T3-L1 cells or Jdp2 À/À MEFs were distributed in 24 wells at 1 Â 10 5 cells/well to generate nearly confluent culture.…”

Section: Methodsmentioning

confidence: 99%

JDP2 suppresses adipocyte differentiation by regulating histone acetylation

Nakade¹,

Pan²,

Yoshiki

et al. 2007

Cell Death Differ

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Among the events that control cellular differentiation, the acetylation of histones plays a critical role in the regulation of transcription and the modification of chromatin. Jun dimerization protein 2 (JDP2), a member of the AP-1 family, is an inhibitor of such acetylation and contributes to the maintenance of chromatin structure. In an examination of Jdp2 'knock-out' (KO) mice, we observed elevated numbers of white adipocytes and significant accumulation of lipid in the adipose tissue in sections of scapulae. In addition, mouse embryo fibroblasts (MEFs) from Jdp2 KO mice were more susceptible to adipocyte differentiation in response to hormonal induction and members of the CCAAT/enhancer-binding proteins (C/EBP) gene family were expressed at levels higher than MEFs from wild-type mice. Furthermore, JDP2 inhibited both the acetylation of histone H3 in the promoter of the gene for C/EBPd and transcription from this promoter. Our data indicate that JDP2 plays a key role as a repressor of adipocyte differentiation by regulating the expression of the gene for C/EBPd via inhibition of histone acetylation.

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Section: Methodsmentioning

confidence: 99%

JDP2 suppresses adipocyte differentiation by regulating histone acetylation

Nakade¹,

Pan²,

Yoshiki

et al. 2007

Cell Death Differ

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show abstract

“…21,22 The recombinant adenovirus vector was generated from adenovirus type 5, and the E1 and E3 regions were deleted to prevent virus replication. Thegal gene was driven by the cytomegalovirus-enhancer chicken -actin hybrid promoter (CAG promoter ) 23 and a rabbit -globin poly (A ) signal located downstream from the gene.…”

Section: Recombinant Adenovirus Vectormentioning

confidence: 99%

Efficient and cancer-selective gene transfer to hepatocellular carcinoma in a rat using adenovirus vector with iodized oil esters

et al. 2001

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Gene therapy for cancer requires efficient, selective gene transfer to cancer cells. In gene therapy for hepatocellular carcinoma ( HCC ) , gene transfer is efficient for small tumors, but not for large tumors. The delivery of anticancer agents and of iodized oil esters as embolic agents through tumor -feeding arteries is known as transarterial embolization. We speculate that genes may be efficiently and selectively transferred for HCC using iodized oil esters because these esters may remain together with a genetic vector within HCC selectively. Hence, we have studied the effect of iodized oil esters on adenovirus vector -mediated gene transfer for HCC in vivo. A rat model of HCC induced with diethylnitrosamine and phenobarbital was injected with either AxCALacZ, which expresses the -galactosidase of Escherichia coli, or AxCALacZ and iodized oil esters into the hepatic artery. Histological comparisons revealed that the -galactosidase expression in the rats with HCC injected with AxCALacZ and iodized oil esters was greater ( P < .0001 ) in small tumors ( P = .0046 ) and large tumors ( P = .0023 ) , and more selective ( P = .0229 ) than in only AxCALacZinjected rats. These results suggest that iodized oil esters are injected into hepatic artery together with adenovirus vector, and that genes may be efficiently and cancer -selectively transferred to HCC. Cancer Gene Therapy ( 2001 ) 8, 713 -718

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“…These ®ndings prompted us to examine the involvement of h-l(3)mbt in cell cycle regulation. To investigate the role of h-l(3)mbt in proliferating cells, we employed the inducible overexpression of h-l(3)mbt gene in U251MG cells by using the Cre-mediated gene activation system (Kanegae et al, 1995(Kanegae et al, , 1996. The U251MG cells, in which endogenous h-l(3)mbt proteins has not been detected, were transfected with pCALNL5, pCALNL5/h-l(3)mbt-I, or pCALNL5/ h-l(3)mbt-II, and clones were selected with G418.…”

Section: Overexpression Of H-l(3)mbt Induces Multinucleated Cellsmentioning

confidence: 99%

“…The constructs corresponding to Cre-mediated h-l(3)mbt-I and h-l(3)mbt-II expression plasmids were generated by ligating the EcoRI/BamHI fragments containing the fulllength ORF of the h-l(3)mbt-I and h-l(3)mbt-II cDNA into the pCALNL5 plasmid which has a Cre-mediated activation unit (Kanegae et al, 1995(Kanegae et al, , 1996. These constructs were named pCALNL5/h-l(3)mbt-I and pCALNL5/h-l(3)mbt-II.…”

Section: Inducible Expression Of the H-l(3)mbt In Mammalian Cellsmentioning

confidence: 99%

“…These ®ndings suggest that the h-l(3)mbt is structurally similar to a member of PcG chromatin-binding complex but is not involved in the previously identi®ed PcG complex. Furthermore, we expressed the h-l(3)mbt gene in the human glioma cell line U251MG with the use of an adenovirus-mediated gene activation system (Kanegae et al, 1995(Kanegae et al, , 1996, and we found that overexpression of h-l(3)mbt a ects nuclear segregation and cytokinesis, resulting in the formation of multinucleated cells. The h-l(3)mbt is potentially involved in regulation of cell cycle progression by participating in the formation of a DNA-binding protein complex.…”

Section: Introductionmentioning

confidence: 99%

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