نتایج جستجو برای: hsp70

تعداد نتایج: 7202  

Journal: :Arteriosclerosis, thrombosis, and vascular biology 2003
Jianhui Zhu Arshed A Quyyumi Hongsheng Wu Gyorgy Csako David Rott Alexandra Zalles-Ganley Jibike Ogunmakinwa Julian Halcox Stephen E Epstein

OBJECTIVE Previous studies suggest that heat shock protein (HSP) 60 has a contributory role in atherosclerosis development. We examined whether circulating HSP70 protein and anti-HSP70 antibodies are associated with coronary artery disease (CAD). METHODS AND RESULTS Blood samples from 421 patients (62% men, mean age 57 years) evaluated for CAD by coronary angiography were tested. Serum HSP70 ...

Journal: :Arthritis Research & Therapy 2009
Eun Ha Kang Dong Jo Kim Eun Young Lee Yun Jong Lee Eun Bong Lee Yeong Wook Song

INTRODUCTION Heat shock protein 70 (Hsp70) is a well-known anti-apoptotic protein that blocks multiple steps in the stress-induced apoptotic pathway. Enhanced Hsp70 expression has previously been demonstrated in rheumatoid arthritis (RA) fibroblast-like synoviocytes (FLSs). The authors investigated the role of Hsp70 in the survival of RA FLSs in a sodium nitroprusside (SNP)-treated environment....

Journal: :Cancer letters 2012
Anastasia R Goloudina Oleg N Demidov Carmen Garrido

HSP70 is a chaperone that accumulates in the cells after many different stresses promoting cell survival in response to the adverse conditions. In contrast to normal cells, most cancer cells abundantly express HSP70 at the basal level to resist to various insults at different stages of tumorigenesis and during anti-cancer treatment. This cancer cells addiction for HSP70 is the rational for its ...

Journal: :The Japanese journal of veterinary research 2005
Ja-Ryong Jeong Masahiro Yamasaki Tomohiko Komatsu Mutsumi Inaba Osamu Yamato Yoshimitsu Maede

In the present study, we demonstrated that heat shock protein 70 (Hsp70) was present in both canine reticulocytes and mature erythrocytes, and that the canine Hsp70 in reticulocytes was decreased along with the maturation of the cells into erythrocytes. These results suggest that the Hsp70 in canine reticulocytes might act as a chaperone to remove unnecessary proteins during reticulocyte matura...

Journal: :Cell 2008
Sigrun Polier Zdravko Dragovic F. Ulrich Hartl Andreas Bracher

Protein folding by Hsp70 is tightly controlled by cochaperones, including J-domain proteins that trigger ATP hydrolysis and nucleotide exchange factors (NEFs) that remove ADP from Hsp70. Here we present the crystal structure of the yeast NEF Sse1p (Hsp110) in complex with the nucleotide-binding domain (NBD) of Hsp70. Hsp110 proteins are homologous to Hsp70s and consist of an NBD, a beta sandwic...

Journal: :Cancer research 2014
Teresa A Colvin Vladimir L Gabai Jianlin Gong Stuart K Calderwood Hu Li Suryaram Gummuluru Olga N Matchuk Svetlana G Smirnova Nina V Orlova Irina A Zamulaeva Mikel Garcia-Marcos Xiaokai Li Z T Young Jennifer N Rauch Jason E Gestwicki Shinichi Takayama Michael Y Sherman

Bag3, a nucleotide exchange factor of the heat shock protein Hsp70, has been implicated in cell signaling. Here, we report that Bag3 interacts with the SH3 domain of Src, thereby mediating the effects of Hsp70 on Src signaling. Using several complementary approaches, we established that the Hsp70-Bag3 module is a broad-acting regulator of cancer cell signaling by modulating the activity of the ...

Journal: :The Journal of biological chemistry 1986
S S Banerji L Berg R I Morimoto

Transient incubation of chicken lymphoblastoid (MSB) cells at elevated temperatures induces the synthesis of three heat shock proteins of 89,000 Da (HSP89), 70,000 Da (HSP70), and 23,000 Da (HSP23). We have examined the effects of heat shock on the transcription and post-transcriptional regulation of the chicken HSP70 and beta-actin genes. The rate of HSP70 transcription is rapidly induced by h...

Journal: :Molecular cell 2008
Andrea V Gómez Danny Galleguillos Juan Cristóbal Maass Elena Battaglioli Manuel Kukuljan María Estela Andrés

The stress response in cells involves a rapid and transient transcriptional activation of stress genes. It has been shown that Hsp70 limits its own transcriptional activation functioning as a corepressor of heat shock factor 1 (HSF1) during the attenuation of the stress response. Here we show that the transcriptional corepressor CoREST interacts with Hsp70. Through this interaction, CoREST repr...

Journal: :Arteriosclerosis, thrombosis, and vascular biology 2001
A Pirillo G D Norata T Zanelli A L Catapano

Oxidized low density lipoproteins (OxLDLs) are believed to play a central role in atherogenesis and to possess a wide variety of biological properties; among them, OxLDLs are cytotoxic to cultured vascular cells in that they induce necrosis and apoptosis. Moreover, OxLDLs are known to induce the expression of heat shock protein 70 (Hsp70), a protein that protects cells from several cytotoxic st...

Journal: :Journal of applied physiology 2009
E Bombardier C Vigna S Iqbal P M Tiidus A R Tupling

This study examined the influence of the ovarian sex hormones, estrogen and progesterone, on the fiber-type-specific response of the inducible 70-kDa heat shock protein (HSP70) to damaging exercise in rat soleus. Ovariectomized female rats were divided into three treatment groups (n = 16 per group): sham (S), progesterone (P; 25 mg pellet), and estrogen (E; 0.25 mg pellet). Each treatment group...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید