scholarly journals Spinal heat shock protein 27 participates in PDGFRβ‐mediated morphine tolerance through PI3K/Akt and p38 MAPK signalling pathways

2020 ◽  
Vol 177 (22) ◽  
pp. 5046-5062
Author(s):  
Zheng Li ◽  
Xiaoling Peng ◽  
Xiaoqian Jia ◽  
Peng Su ◽  
Daiqiang Liu ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
P38 Mapk ◽  
Morphine Tolerance ◽  
Heat Shock Protein 27 ◽  
Signalling Pathways ◽  
Mapk Signalling

scholarly journals Helicobacter pylori heat-shock protein 60 induces interleukin-8 via a Toll-like receptor (TLR)2 and mitogen-activated protein (MAP) kinase pathway in human monocytes

2007 ◽  
Vol 56 (2) ◽  
pp. 154-164 ◽  
Author(s):  
Ying Zhao ◽  
Kenji Yokota ◽  
Kiyoshi Ayada ◽  
Yumiko Yamamoto ◽  
Tomayuki Okada ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
P38 Mapk ◽  
Heat Shock Protein 60 ◽  
Human Monocytes ◽  
Toll Like Receptor ◽  
Mapk Signalling ◽  
Mitogen Activated Protein ◽  
H Pylori

Previous reports have indicated that Helicobacter pylori heat-shock protein 60 (H. pylori-HSP60), as an immunodominant antigen, induces interleukin (IL)-8 production in human monocytes. The exact mechanism by which H. pylori-HSP60 induces IL-8 production in monocytes has not been fully elucidated. In the present study, the downstream pathway by which H. pylori-HSP60 induces IL-8 secretion in human monocytic cell lines was investigated. Intact H. pylori, heat-killed H. pylori and H. pylori recombinant HSP60 (rHpHSP60) all induced the secretion of IL-8 and the activation of mitogen-activated protein kinase (MAPK), extracellular signal-regulated kinase (ERK) and p38, but not c-Jun N-terminal kinase (JNK), up to 24 h in NOMO1 cells. The specific inhibitors PD98059 and U0126 (for ERK1/2 signalling) and SB203580 (for p38 MAPK signalling) down-regulated IL-8 secretion from rHpHSP60-treated NOMO1 cells. An anti-Toll-like receptor (TLR)2 antibody or TLR2 small interfering RNA (siRNA) partially inhibited the secretion of IL-8, and anti-TLR2 antibody also suppressed activation of ERK and p38 MAPK in rHpHSP60-treated NOMO1 cells. These reactions were associated with nuclear factor-κB (NF-κB)-mediated transcriptional activation, since U0126, SB203580 and the anti-TLR2 antibody decreased NF-κB activation. Taken together, the results suggest that ERK and p38 MAPK signalling linked to the TLR2 recognition receptor in human monocytes may be an important pathway in H. pylori-HSP60-induced IL-8 secretion.

scholarly journals Arachidonic Acid Stimulates Cell Adhesion through a Novel p38 MAPK-RhoA Signaling Pathway That Involves Heat Shock Protein 27

2009 ◽  
Vol 284 (31) ◽  
pp. 20936-20945 ◽  
Author(s):  
Melissa C. Garcia ◽  
Denise M. Ray ◽  
Brad Lackford ◽  
Mark Rubino ◽  
Kenneth Olden ◽  
...  
Keyword(s):  
Arachidonic Acid ◽  
Cell Adhesion ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Signaling Pathway ◽  
P38 Mapk ◽  
Heat Shock Protein 27 ◽  
Rhoa Signaling

scholarly journals MAPK and heat shock protein 27 activation are associated with respiratory syncytial virus induction of human bronchial epithelial monolayer disruption

2007 ◽  
Vol 293 (2) ◽  
pp. L436-L445 ◽  
Author(s):  
Divyendu Singh ◽  
Kelly L. McCann ◽  
Farhad Imani
Keyword(s):  
Respiratory Syncytial Virus ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
P38 Mapk ◽  
Membrane Integrity ◽  
A549 Cells ◽  
Heat Shock Protein 27 ◽  
Fluid Extravasation ◽  
P38 Mapk Inhibitors ◽  
Syncytial Virus

Respiratory syncytial virus (RSV) is the major cause of bronchiolitis in infants, and a common feature of RSV infections is increased lung permeability. The accumulation of fluid in the infected lungs is caused by changes in the endothelial and epithelial membrane integrity. However, the exact mechanisms of viral-induced fluid extravasation remain unclear. Here, we report that infection of human epithelial cells with RSV results in significant epithelial membrane barrier disruption as assessed by a decrease in transepithelial electrical resistance (TEpR). This decrease in TEpR, which indicates changes in paracellular permeability, was mediated by marked cellular cytoskeletal rearrangement. Importantly, the decrease in TEpR was attenuated by using p38 MAPK inhibitors (SB-203580) but was partially affected by JNK inhibitor SP-600125. Interestingly, treatment of A549 cells with MEK1/2 inhibitor (U-0126) led to a decrease in TEpR in the absence of RSV infection. The changes in TEpR were concomitant with an increase in heat shock protein 27 (Hsp27) phosphorylation and with actin microfilament rearrangement. Thus our data suggest that p38 MAPK and Hsp27 are required for RSV induction of human epithelial membrane permeability.

765: Modified Expression of Heat Shock Protein 27 in Renal Cell Carcinoma

2004 ◽  
Vol 171 (4S) ◽  
pp. 203-203
Author(s):  
Cecilia Sarto ◽  
Paolo Favini ◽  
Cristina Valsecchi ◽  
Stefano Casellato ◽  
Fulvio Magni ◽  
...  
Keyword(s):  
Renal Cell Carcinoma ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cell Carcinoma ◽  
Renal Cell ◽  
Heat Shock Protein 27

Protektive Wirkung von Heat Shock Protein 27 in der Magenmukosa

2005 ◽  
Vol 43 (05) ◽  
Author(s):  
M Ebert ◽  
C Schäfer ◽  
J Hoffmann ◽  
C Kubisch ◽  
G Treiber ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 27 ◽  
Protektive Wirkung

scholarly journals Involvement of Reductive Stress in the Cardiomyopathy in Transgenic Mice With Cardiac-Specific Overexpression of Heat Shock Protein 27

Hypertension ◽  
2010 ◽  
Vol 55 (6) ◽  
pp. 1412-1417 ◽  
Author(s):  
Xia Zhang ◽  
Xiaoyan Min ◽  
Chuanfu Li ◽  
Ivor J. Benjamin ◽  
Bo Qian ◽  
...  
Keyword(s):  
Heat Shock ◽  
Transgenic Mice ◽  
Heat Shock Protein ◽  
Heat Shock Protein 27 ◽  
Reductive Stress
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