نتایج جستجو برای: heat shock protein 27 hsp27 inhibitors

تعداد نتایج: 1741445  

Journal: :Anticancer research 2016
Daimei Eto Toru Hisaka Hiroyuki Horiuchi Shinji Uchida Hiroto Ishikawa Yusuke Kawashima Tetsushi Kinugasa Osamu Nakashima Hirohisa Yano Koji Okuda Yoshito Akagi

BACKGROUND/AIM Heat-shock protein 27 (HSP27), a low molecular weight stress protein, is recognized as a molecular chaperone. The expression of HSP27 has been detected in some human tumors and while HSP27 is phosphorylated as a reresponse to stress, the function of phosphorylated HSP27 (p-HSP27) is not known. The aim of this study was to investigate what kind of effect expression of HSP27 and p-...

Journal: :American journal of physiology. Heart and circulatory physiology 2008
Gefeng Li Imtiaz S Ali R William Currie

Six hours after insulin treatment, hearts express heat shock protein 70 (Hsp70) and have improved contractile function after ischemia-reperfusion injury. In this study we examined hearts 1 h after insulin treatment for contractile function and for expression of Hsp70 and Hsp27. Adult, male Sprague-Dawley rats were assigned to groups: 1) sham, 2) control, 3) insulin injected (200 microU/g body w...

Journal: :The Biochemical journal 2007
Anton L Bryantsev Svetlana Yu Kurchashova Sergey A Golyshev Vladimir Yu Polyakov Herman F Wunderink Bart Kanon Karina R Budagova Alexander E Kabakov Harm H Kampinga

In vitro, small Hsps (heat-shock proteins) have been shown to have chaperone function capable of keeping unfolded proteins in a form competent for Hsp70-dependent refolding. However, this has never been confirmed in living mammalian cells. In the present study, we show that Hsp27 (HspB1) translocates into the nucleus upon heat shock, where it forms granules that co-localize with IGCs (interchro...

2011
Sanjib Banerjee Chuen-Fu L. Lin Kristin A. Skinner Linda M. Schiffhauer James Peacock David G. Hicks Eileen M. Redmond David Morrow Alissa Huston Michelle Shayne Howard N. Langstein Carol L. Miller-Graziano Jennifer Strickland Asit K. De

Tumor cells release several factors that can help the progression of the tumor by directly supporting tumor growth and/or suppressing host antitumor immunity. Here, we report that human primary breast tumor cells not only express elevated levels of heat shock protein 27 (Hsp27) at the intracellular level but also release extremely high levels of Hsp27 compared with the same patients’ serum Hsp2...

Journal: :Molecular medicine reports 2010
Zhijin Yu Junli Zhi Xiaofeng Peng Xuhui Zhong Angao Xu

The heat shock protein 27-kDa (HSP27) has been found overexpressed in several types of human cancer and is associated with treatment resistance and poor prognosis. Recent proteomic studies demonstrate that HSP27 is significantly overexpressed in colorectal cancer (CRC). However, the relationship between HSP27 expression and patient prognosis remains nascent. In the present study, we aimed to in...

Journal: :American journal of physiology. Gastrointestinal and liver physiology 2002
Khalil N Bitar

We have investigated the role of heat shock protein 27 (HSP27) phosphorylation and the association of HSP27 with contractile proteins actin, myosin, and tropomyosin. Smooth muscle cells were labeled with [(32)P]orthophosphate. C2-ceramide (0.1 microM), an activator of protein kinase C (PKC), induced a sustained increase in HSP27 phosphorylation that was inhibited by calphostin C. C2-ceramide-in...

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