نتایج جستجو برای: heat shock protein 27 hsp27 inhibitors

تعداد نتایج: 1741445  

Journal: :Folia biologica 2011
R Chen R Y Dai C Y Duan Y P Liu S K Chen D M Yan C N Chen M Wei H Li

It has been shown that drug resistance is extremely common in hepatocellular carcinoma (HCC) and is one of the major problems in HCC chemotherapy. However, the detailed mechanisms remain largely unknown. We have previously shown that endoplasmic reticulum (ER) stress is involved in the tumorigenesis of HCC. Here, we demonstrated that the unfolded protein response (UPR) inhibits cisplatin-induce...

Journal: :International journal of oncology 2006
Ken Ohnishi Jun-Ichi Yasumoto Akihisa Takahashi Takeo Ohnishi

The aim of this study was to ascertain whether LY294002, an inhibitor of PI-3K, enhances heat sensitivity in human cancer cells regardless of their p53 status. Colony formation assays showed that LY294002 enhanced heat sensitivity in two human lung cancer cell lines; H1299/wild-type p53 (wtp53) and H1299/mutated p53 (mp53) cells. These cell lines have identical genetic backgrounds except for th...

Journal: :Journal of leukocyte biology 2001
L A Cubano M L Lewis

Heat shock protein levels are increased in cells as a result of exposure to stress. To determine whether heat shock protein regulation could be used to evaluate stress in cells during spaceflight, the response of Jurkat cells to spaceflight and simulated space shuttle launch vibration was investigated by evaluating hsp70 and hsp27 gene expression. Gene expression was assessed by reverse transcr...

Journal: :Journal of immunology 2007
Neelakshi R Jog Venkatakrishna R Jala Richard A Ward Madhavi J Rane Bodduluri Haribabu Kenneth R McLeish

The targets of the p38 MAPK pathway responsible for regulation of neutrophil chemotaxis and exocytosis are unknown. One target of this pathway is the actin-binding protein, heat shock protein 27 (Hsp27). Therefore, we tested the hypothesis that Hsp27 mediates p38 MAPK-dependent chemotaxis and exocytosis in human neutrophils through regulation of actin reorganization. Sequestration of Hsp27 by i...

Journal: :Clinical cancer research : an official journal of the American Association for Cancer Research 1996
S Oesterreich S G Hilsenbeck D R Ciocca D C Allred G M Clark G C Chamness C K Osborne S A Fuqua

Heat shock protein 27 (hsp27) belongs to the family of heat shock proteins and is thought to be involved in thermotolerance, cell proliferation, drug resistance, and chaperone processes. The aim of this study was to investigate whether hsp27 levels are correlated with clinical outcome in axillary lymph node-negative breast cancer patients. We describe a Western blot study measuring hsp27 levels...

Journal: :Anticancer Research 2021

Background/Aim: We have previously reported the identification of cytotoxic chemotype compound-I (CC-I) from a chemical library screening against glioblastoma. Materials and Methods: The biological activity CC-I on drug-resistant neuroblastomas [e.g., HFE gene variant C282Y stably transfected human neuroblastoma SH-SY5Y cells (C282Y HFE/SH-SY5Y), SK-N-AS] was characterized using cell culture mo...

Journal: :The Tohoku journal of experimental medicine 2008
Yuko Takahashi-Horiuchi Kanji Sugiyama Hideaki Sakashita Osamu Amano

Heat shock protein 27 (Hsp27) has been suggested to participate in the cell proliferation and differentiation during tissue development. In fact, we have demonstrated the transient occurrence of Hsp27 during the differentiation of salivary gland acinar cells in postnatal rats. The purpose of the present study is to explore the potential role of Hsp27 in the proliferation and differentiation of ...

Journal: :American journal of physiology. Endocrinology and metabolism 2001
D Hatakeyama O Kozawa M Niwa H Matsuno K Kato N Tatematsu T Shibata T Uematsu

We have previously reported that endothelin-1 (ET-1) stimulates heat shock protein (HSP) 27 induction in osteoblast-like MC3T3-E1 cells and that p38 mitogen-activated protein (MAP) kinase acts at a point downstream from protein kinase C (PKC) in HSP27 induction. In the present study, we investigated the effect of the adenylyl cyclase-cAMP system on ET-1-stimulated induction of HSP27 in MC3T3-E1...

2017
Chin-Sheng Hung Chien-Yu Huang Chia-Hwa Lee Wei-Yu Chen Ming-Te Huang Po-Li Wei Yu-Jia Chang

Heat shock protein 27 (Hsp27) is a key chaperone that interacts with over 200 client proteins. The expression of Hsp27 might be correlated with poor outcome in many types of cancer. Previous study indicated that Hsp27 might be an important biomarker in hepatocellular carcinoma (HCC). However, the detailed mechanism is less well understood. The shRNA-mediated silencing of Hsp27 decreased the pro...

Journal: :Cancer research 2004
Palma Rocchi Alan So Satoko Kojima Maxim Signaevsky Eliana Beraldi Ladan Fazli Antonio Hurtado-Coll Kazuki Yamanaka Martin Gleave

Heat shock protein 27 (Hsp27) is a chaperone implicated as an independent predictor of clinical outcome in prostate cancer. Our aim was to characterize changes in Hsp27 after androgen withdrawal and during androgen-independent progression in prostate xenografts and human prostate cancer to assess the functional significance of these changes using antisense inhibition of Hsp27. A tissue microarr...

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