نتایج جستجو برای: hsp70

تعداد نتایج: 7202  

Journal: :Molecular and cellular biology 2000
D D Mosser A W Caron L Bourget A B Meriin M Y Sherman R I Morimoto B Massie

Cellular stress can trigger a process of self-destruction known as apoptosis. Cells can also respond to stress by adaptive changes that increase their ability to tolerate normally lethal conditions. Expression of the major heat-inducible protein hsp70 protects cells from heat-induced apoptosis. hsp70 has been reported to act in some situations upstream or downstream of caspase activation, and i...

2013
Zhengke Peng Na Liu Damao Huang Chaojun Duan Yuejin Li Xiaowei Tang Wenhua Mei Feng Zhu Faqing Tang

N,N'-Dinitrosopiperazine (DNP) is invovled in nasopharyngeal carcinoma (NPC) development and metastasis, and it shows organ specificity to the nasopharyngeal epithelium. Herein, we demonstrate that DNP induces heat-shock protein (HSP) 70-2 expression in NPC cells (6-10B) at a non-cytotoxic concentration. DNP induced HSP70-2 expression in a dose- and time- dependent manner, but showed no effect ...

Journal: :Clinical cancer research : an official journal of the American Association for Cancer Research 1995
R Ralhan J Kaur

Transformed cells differ from normal cells in their pattern of heat shock protein expression. Here, we report differential expression of a Mr 70,000 heat shock protein (HSP70) in squamous cell carcinomas of the uterine cervix compared to normal or premalignant uterine cervix. Expression of HSP70 was measured using a mouse mAb against HSP70 by an ELISA. A significant increase in the level of exp...

2017
Christian Ostheimer Sophie Gunther Matthias Bache Dirk Vordermark Gabriele Multhoff

Hypoxia mediates resistance to radio(chemo)therapy (RT) by stimulating the synthesis of hypoxia-related genes, such as osteopontin (OPN) and stress proteins, including the major stress-inducible heat shock protein 70 (Hsp70). Apart from its intracellular localization, Hsp70 is also present on the plasma membrane of viable tumor cells that actively release it in lipid vesicles with biophysical c...

Journal: :Journal of immunology 2002
Caroline A Dobbin Nicholas C Smith Alan M Johnson

We propose that the 70-kDa heat shock protein (HSP70) protects virulent Toxoplasma gondii from the effects of the host by immunomodulation. This hypothesis was tested using quercetin and antisense oligonucleotides targeting the start codon of the virulent T. gondii HSP70 gene. Oligonucleotides were transiently transfected into two virulent (RH, ENT) and two avirulent (ME49, C) strains of T. gon...

Journal: :Physiological and biochemical zoology : PBZ 2002
Martin E Feder Trevor B C Bedford Daisy R Albright Pawel Michalak

To test whether expression of the inducible heat-shock protein Hsp70 increases under selection for inducible thermotolerance in Drosophila melanogaster, we performed artificial selection on replicate sets of Drosophila lines founded from two independent populations. Selection entailed pretreatment at 36 degrees C to induce thermotolerance and Hsp70 expression, followed by a more severe heat sho...

Journal: :Blood 2004
Sergey Iordanskiy Yuqi Zhao Paola DiMarzio Isabelle Agostini Larisa Dubrovsky Michael Bukrinsky

HIV-1 viral protein R (Vpr) shuttles between the nucleus and the cytoplasm and is believed to contribute to the process of nuclear translocation of the viral preintegration complex, thus facilitating HIV-1 replication in macrophages. In this report, we demonstrate that Hsp70, a heat-shock protein contributing to cellular stress responses, inhibits nuclear translocation of HIV-1 Vpr. In macropha...

2016
Ji Hae Seo Ji-Hyeon Park Eun Ji Lee Tam Thuy Lu Vo Hoon Choi Jun Yong Kim Jae Kyung Jang Hee-Jun Wee Hye Shin Lee Se Hwan Jang Zee Yong Park Jaeho Jeong Kong-Joo Lee Seung-Hyeon Seok Jin Young Park Bong Jin Lee Mi-Ni Lee Goo Taeg Oh Kyu-Won Kim

Heat shock protein (Hsp)70 is a molecular chaperone that maintains protein homoeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. However, the mechanisms by which Hsp70 balances these opposing functions under stress conditions remain unknown. Here, we demonstrate that Hsp70 preferentially facilitates protein refolding after stress, gradually swit...

Journal: :Development 1993
B Billoud M L Rodriguez-Martin L Berard N Moreau N Angelier

We isolated and characterized a sequence coding for heat-shock protein 70 (HSP70) of the amphibian Pleurodeles waltl. Results from S1 nuclease protection assays led us to conclude that an hsp70 gene, strictly inducible in somatic cells during heat shock, is constitutively active during oogenesis. By quantitative northern and western blot analysis, we showed that both hsp70 mRNA and HSP70-relate...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1984
J C Bardwell E A Craig

The Escherichia coli dnaK gene is homologous to the major heat shock-induced gene in Drosophila (Hsp70). The primary DNA sequence of the entire protein-coding region of the dnaK gene was determined and compared with that of the Hsp70 gene of Drosophila. The two sequences are homologous; the dnaK gene could encode a 69,121-Da polypeptide, 48% identical to the hsp70 protein of Drosophila. The hom...

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