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Ting Xiao, Xiuci Liang, Hailan Liu, Feng Zhang, Wen Meng, and Fang Hu

( Haynes et al . 2007 , Broadley & Hartl 2008 , Haynes & Ron 2010 , Hu & Liu 2011 ). HSP60, an important mitochondrial stress protein, has been shown to play key roles in the protein synthesis, folding, and delivery of misfolded proteins to proteolytic

Open access

Farhana Naznin, Koji Toshinai, T M Zaved Waise, Tadashi Okada, Hideyuki Sakoda, and Masamitsu Nakazato

( Kohno et al . 2003 , Hardie 2004 ). Previous studies showed that neither central nor peripheral ghrelin administration induced feeding in diet-induced obese (DIO) mice fed a high-fat diet (HFD, 60% of energy from fat) for 12 or 16 weeks ( Perreault et

Free access

K Miura, J Zhu, NT Dittmer, L Chen, and AS Raikhel

In the mosquito Aedes aegypti, vitellogenesis is activated via an ecdysteroid hormonal cascade initiated by a blood meal. The functional ecdysone receptor is a heterodimer composed of the ecdysone receptor (EcR) and ultraspiracle, the homolog of the retinoid X receptor. The precise tuning of this hormonal response requires participation of both positive and negative transcriptional regulators. In Drosophila, Svp, a homolog of chicken ovalbumin upstream promoter transcription factor (COUP-TF), inhibits ecdysone receptor complex-mediated transactivation in vitro and in vivo. Here we report the cloning and characterization of the Svp homolog in mosquito Aedes aegypti, AaSvp. It possesses a high degree of amino acid sequence similarity to the members of the COUP-TF/Svp subfamily. AaSvp transcripts and protein are present in the fat body at high levels from the state of arrest to about 60 h post blood meal. AaSvp binds strongly to a variety of direct repeats of the sequence AGGTCA, but weakly to inverted repeats such as hsp27 EcRE. Transient transfection assays in Drosophila S2 cells showed that AaSvp was able to repress 20-hydroxyecdysone (20E)-dependent transactivation mediated by the mosquito ecdysteroid receptor complex. These data suggest that AaSvp negatively regulates the 20E signaling in the fat body during mosquito vitellogenesis.

Free access

I Paron, C D’Ambrosio, A Scaloni, M T Berlingieri, P L Pallante, A Fusco, N Bivi, G Tell, and G Damante

chaperone or chaperone-like activities were found to be significantly altered. Particularly, two members of the heat-shock protein family, Hsp90-beta and Hsp60, were found to be significantly increased. Hsp90-beta upregulation is very important for p53

Open access

Hyon-Seung Yi, Joon Young Chang, and Minho Shong

( Aldridge et al . 2007 ). In this context, the mitochondrial chaperone systems are required for facilitating protein-folding within the mitochondria ( Fig. 3 ). While HSP60 plays a prominent role in the UPR mt response, other mitochondrial chaperones are

Free access

Kjersti M Aagaard-Tillery, Kevin Grove, Jacalyn Bishop, Xingrao Ke, Qi Fu, Robert McKnight, and Robert H Lane

–Elmer Life Sciences), 500 nM primers, and 1.25 units Ampli Taq Gold (Applied Biosystems). Initial denaturation was performed at 95 °C for 10 min, followed by 40 cycles of 94 °C for 30 s, 44 °C for 60 s, and 72 °C for 90 s for primers 315–317; and annealing

Free access

Andrew P Trotta, Eleanor F Need, Lisa M Butler, Luke A Selth, Melissa A O'Loughlin, Gerhard A Coetzee, Wayne D Tilley, and Grant Buchanan

Introduction The unliganded androgen receptor (apo-AR) in normal cells is located predominately in the cytoplasm in association with heat-shock protein 70 (HSP70) and/or HSP90 chaperone complexes ( Marcelli et al . 2006 ). Although the interaction

Free access

Wen-Li Zhao, Chun-Yan Liu, Wen Liu, Di Wang, Jin-Xing Wang, and Xiao-Fan Zhao

this work. Materials and methods Experimental animal H. armigera larvae were raised on the artificial diet, which was made from powder of wheat germs and soybeans at 27 °C with 60–70% relative humidity. The illumination condition consisted of 14 h

Free access

Denis Nonclercq, Fabrice Journé, Ioanna Laïos, Carole Chaboteaux, Robert-Alain Toillon, Guy Leclercq, and Guy Laurent

determined by the ligand-binding status and/or interactions with partner proteins ( Nonclercq et al. 2004 , Tateishi et al. 2004 ). ER stability depends on many factors, such as post-translational modifications, interactions with other proteins (i.e. Hsp90

Open access

Yanjun Cui and Xianhong Gu

level, including changes in gene and protein expression, and biochemical adaptations. For example, the investigation reported by Yu et al . (2010) demonstrated that acute HS could increase HSP27, HSP70 and HSP90 expression and trigger MAPK signaling