scholarly journals Expression of a Small Heat Shock Protein 27 (HSP27) in Mouse Skin Tumors Induced by UVB-Irradiation.

2001 ◽  
Vol 24 (2) ◽  
pp. 197-200 ◽  
Author(s):  
Misao T. KIRIYAMA ◽  
Mikako OKA ◽  
Makoto TAKEHANA ◽  
Shizuko KOBAYASHI
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Mouse Skin ◽  
Small Heat Shock Protein ◽  
Heat Shock Protein 27 ◽  
Skin Tumors ◽  
Uvb Irradiation

scholarly journals Distal hereditary motor neuropathy in Korean patients with a small heat shock protein 27 mutation

2008 ◽  
Vol 40 (3) ◽  
pp. 304 ◽  
Author(s):  
Ki Wha Chung ◽  
Sang-Beom Kim ◽  
Sun Young Cho ◽  
Su Jin Hwang ◽  
Sun Wha Park ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Heat Shock Protein 27 ◽  
Motor Neuropathy ◽  
Hereditary Motor ◽  
Korean Patients ◽  
Hereditary Motor Neuropathy

Differential Expression of Small Heat Shock Protein 27 (Hsp27) in Ataxia telangiectasia Brains

2009 ◽  
Vol 34 (9) ◽  
pp. 1658-1667 ◽  
Author(s):  
Wenqiang Chen ◽  
Salomon Kuizon ◽  
Bair L. Chiou ◽  
David C. Bolton ◽  
Raju K. Pullarkat ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Differential Expression ◽  
Ataxia Telangiectasia ◽  
Small Heat Shock Protein ◽  
Heat Shock Protein 27

Small heat shock protein 27: An effective adjuvant for enhancement of HIV-1 Nef antigen-specific immunity

2017 ◽  
Vol 191 ◽  
pp. 16-22 ◽  
Author(s):  
Alireza Milani ◽  
Azam Bolhassani ◽  
Sepideh Shahbazi ◽  
Fatemeh Motevalli ◽  
Seyed Mehdi Sadat ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Heat Shock Protein 27 ◽  
Specific Immunity ◽  
Hiv 1

scholarly journals The Small Heat Shock Protein 27 Is a Key Regulator of CD8+CD57+Lymphocyte Survival

2010 ◽  
Vol 184 (10) ◽  
pp. 5582-5588 ◽  
Author(s):  
Karen L. Wood ◽  
Oliver H. Voss ◽  
Qin Huang ◽  
Arti Parihar ◽  
Neeraj Mehta ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Heat Shock Protein 27 ◽  
Lymphocyte Survival

Heat shock protects cardiac cells from doxorubicin-induced toxicity by activating p38 MAPK and phosphorylation of small heat shock protein 27

2006 ◽  
Vol 291 (6) ◽  
pp. H2680-H2691 ◽  
Author(s):  
C. D. Venkatakrishnan ◽  
Arun K. Tewari ◽  
Leni Moldovan ◽  
Arturo J. Cardounel ◽  
Jay L. Zweier ◽  
...  
Keyword(s):  
Heat Shock ◽  
Protein Kinase ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Heat Shock Protein 27 ◽  
Cardiac Cells ◽  
Two Dimensional Gel Electrophoresis ◽  
Actin Remodeling ◽  
Dilative Cardiomyopathy ◽  
Endogenous Antioxidant

Doxorubicin (DOX) and its derivatives are used as chemotherapeutic drugs to treat cancer patients. However, production of DOX-mediated reactive oxygen species (ROS) by prolonged use of these drugs has been found to cause dilative cardiomyopathy and congestive heart failure. Thus various preventive modalities have been developed to avoid this side effect. We have found that the DOX-mediated oxidant-induced toxicity in cardiac cells could be minimized by hyperthermia-induced small heat shock protein 27 (HSP27); that is, this protein acts as an endogenous antioxidant against DOX-derived oxidants such as H2O2. Heat shock-induced HSP27 was found to act as an antiapoptotic protein (reducing ROS and Bax-to-Bcl2 ratio) against DOX, and its phosphorylated isoforms stabilized F-actin remodeling in DOX-treated cardiac cells and, hence, attenuated the toxicity. Protein kinase assays and proteomic analyses suggested that higher expression of HSP27 and its phosphorylation are responsible for the protection in heat-shocked cells. Two-dimensional gel electrophoresis showed six isoforms (nonphosphorylated and phosphorylated) of HSP27. Matrix-assisted laser desorption/ionization time of flight analyses showed α- and β-isoforms of HSP27, which are phosphorylated by various protein kinases. Ser15 and Ser85 phosphorylation of HSP27 by MAPK-assisted protein kinase 2 was found to be the key mechanism in reduction of apoptosis and facilitation of F-actin remodeling. The present study illustrates that hyperthermia protects cells from DOX-induced death through induction and phosphorylation of HSP27 and its antiapoptotic and actin-remodeling activities.

scholarly journals Small heat shock protein 27 (Hsp27) expression is highly induced in rat myometrium during late pregnancy and labour

Reproduction ◽  
2005 ◽  
Vol 129 (1) ◽  
pp. 115-126 ◽  
Author(s):  
B G White ◽  
S J Williams ◽  
K Highmore ◽  
D J MacPhee
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Regulatory Protein ◽  
Circular Muscle ◽  
Small Heat Shock Protein ◽  
Late Pregnancy ◽  
Immunoblot Analysis ◽  
Heat Shock Protein 27 ◽  
Potential Candidate ◽  
Hsp27 Expression

The underlying mechanisms that regulate uterine contractions during labour are still poorly understood. A candidate regulatory protein is heat shock protein 27 (Hsp27). It belongs to the small heat shock protein family and can regulate actin cytoskeleton dynamics, act as a chaperone, and may regulate contractile protein activation. As a result, we hypothesized that Hsp27 expression would be highly induced during late pregnancy and labour. Hsp27 mRNA expression was significantly elevated (P< 0.05) on days 17 to 22 of gestation. In addition, immunoblot analysis demonstrated that detection of total Hsp27 increased (P< 0.05) between day 21 and 1 day post-partum (PP) inclusive. Since phosphorylation of Hsp27 has been reported to be a prerequisite for smooth muscle contraction, we examined the temporal and spatial expression of Ser-15 phosphorylated Hsp27. Immunoblot analysis showed that the detection of Ser-15 phosphorylated Hsp27 significantly increased (P< 0.05) between days 19 and 23 (active labour) inclusive, in parallel with detection of total Hsp27. Immunocytochemical analysis of Ser-15 phosphorylated Hsp27 expressionin situdemonstrated that phosphorylated Hsp27 in circular muscle became detectable in peri-nuclear and membrane regions on days 19 to 22, but was primarily restricted to the cytoplasm on days 23 to PP. In contrast, phosphorylated Hsp27 in longitudinal muscle was primarily detected in myocyte membranes on days 15 to 22, and then also became detectable in the cytoplasm of myocytes on days 23 and PP. Our results demonstrate that Hsp27 expression is highly upregulated during late pregnancy and labour and suggest that Hsp27 is a potential candidate contraction-associated protein.

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