P.168 Role of chaperonin-containing TCP complex (CCT) and heat shock cognate protein 70 (Hsc70) in the HCV RNA replication

2006 ◽  
Vol 36 ◽  
pp. S112-S113
Author(s):  
T. Suzuki ◽  
Y. Inoue ◽  
H. Aizaki ◽  
M. Matsuda ◽  
M. Shirakura ◽  
...  
Keyword(s):  
Heat Shock ◽  
Rna Replication ◽  
Hcv Rna ◽  
Heat Shock Cognate Protein ◽  
Cognate Protein

Different combinations of the heat-shock cognate protein 70 (hsc70) C-terminal functional groups are utilized to interact with distinct tetratricopeptide repeat-containing proteins

2001 ◽  
Vol 359 (2) ◽  
pp. 419-426 ◽  
Author(s):  
Shin-Jen WU ◽  
Fu-Hwa LIU ◽  
Su-Ming HU ◽  
Chung WANG
Keyword(s):  
Heat Shock ◽  
Functional Groups ◽  
Luciferase Activity ◽  
Inhibitory Effect ◽  
Tetratricopeptide Repeat ◽  
Interacting Protein ◽  
C Terminus ◽  
Heat Shock Cognate Protein ◽  
Cognate Protein

A group of tetratricopeptide repeat (TPR)-containing proteins has been shown to interact with the C-terminal domain of the 70kDa heat-shock cognate protein (hsc70). In the present study, the effect of the TPR-containing proteins, including the C-terminus of hsc70-interacting protein (CHIP), TPR1 and human glutamine-rich TPR-containing protein (hSGT), on refolding of luciferase by DnaJ and hsc70 was investigated. These proteins inhibited the restoration of luciferase activity by the chaperones. The inhibitory effect exerted by TPR1 and hSGT depended upon their binding to hsc70. However, the interaction with hsc70 did not appear to be required for the inhibition of luciferase refolding by CHIP. We also demonstrate that the peptide, GPTIEEVD, corresponding to the C-terminal end of hsc70, abolished the association of [3H]hsc70 with CHIP, TPR1 and hSGT. This implied that the GPTIEEVD motif of hsc70 was responsible for interacting with these TPR-containing proteins. However, the GGXP-repeats (where X is any aliphatic residue), another C-terminal conserved motif of vertebrate hsc70s, were not essential for interacting with the TPR-containing proteins. On the basis of mutagenesis studies, it was clear that a unique combination of the functional groups in the GPTIEEVD motif were utilized to interact with each TPR-containing protein, suggesting that inhibitors can be designed and used to elucidate the functional role of these interactions.

Abstract 1055: The 70 kDa Heat Shock Cognate Protein Plays A Novel Role In Myocardial Chemokine Expression And Cardiac Dysfunction Following Ischemia And Reperfusion Injury

Circulation ◽  
2007 ◽  
Vol 116 (suppl_16) ◽  
Author(s):  
Ning Zou ◽  
Lihua Ao ◽  
Xiaoping Yang ◽  
Xin Su ◽  
David A Fullerton ◽  
...  
Keyword(s):  
Heat Shock ◽  
Inflammatory Response ◽  
Cardiac Dysfunction ◽  
Substrate Binding ◽  
Binding Domain ◽  
Chemokine Expression ◽  
Heat Shock Cognate Protein ◽  
Substrate Binding Domain ◽  
Cognate Protein

Myocardial ischemia and reperfusion (I/R) causes the release of cellular proteins including heat shock proteins (HSPs). The inducible HSP70 induces cytokine production in monocytes and dendritic cells through Toll-like receptor 4 (TLR4) signaling. In evaluation of the role of HSPs in myocardial inflammatory response in a mouse heart global I/R model, we found that the 70 kDa heat shock cognate protein (HSC70), but not HSP70, was released into the extracellular space and the coronary effluent during I/R. These observations prompted us to hypothesize that HSC70 plays a novel role in postischemic myocardial inflammatory response and cardiac dysfunction. Methods: We subjected mouse hearts to global I/R (20 min/60 min) or perfusion using the Langendorff method. We examined: the effect of HSC70 antibody on myocardial chemokine expression and cardiac functional recovery following I/R, the effect of recombinant HSC70 on myocardial chemokine expression and cardiac function and the role of TLR4 and the HSC70 substrate-binding domain in the effect of HSC70 on the heart. Results: In comparison with non-immune IgG, anti-HSC70 reduced myocardial expression of KC and MCP-1 mRNAs and proteins following I/R. Moreover, treatment with anti-HSC70 improved postischemic cardiac functional recovery (66±5.4% of baseline vs. 28±5.1% of baseline in hearts treated with non-immune IgG, p<0.01). Recombinant HSC70 induced myocardial expression of KC and MCP-1 mRNAs and proteins and caused cardiac dysfunction (72±2.6% of baseline vs. 98±3.9% of baseline in perfusion controls, p<0.001) in hearts with competent TLR4 (C3H/HeN). Interestingly, these effects of HSC70 were abrogated in hearts with defective TLR4 (C3H/HeJ). The potency of HSC70 was completely lost in the absence of its substrate-binding domain. Conclusions: Taken together, our studies demonstrate, for the first time, that HSC70 plays an important role in the induction of myocardial chemokines and cardiac dysfunction during I/R. The effect of HSC70 is dependent on TLR4 and requires the presence of the substrate-binding domain. The results suggest that the release of HSC70 into the extracellular space elicits an inflammatory response and causes mechanic dysfunction in the heart.

scholarly journals Exogenous heat shock cognate protein Hsc70 prevents axotomy-induced death of spinal sensory neurons

1996 ◽  
Vol 1 (3) ◽  
pp. 161 ◽  
Author(s):  
Lucien J. Houenou ◽  
Linxi Li ◽  
Ming Lei ◽  
Carol R. Kent ◽  
Michael Tytell
Keyword(s):  
Heat Shock ◽  
Sensory Neurons ◽  
Heat Shock Cognate Protein ◽  
Cognate Protein

Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70)

2021 ◽  
Vol 1869 (12) ◽  
pp. 140719
Author(s):  
Noeli Soares Melo Silva ◽  
Luiz Fernando de Camargo Rodrigues ◽  
Paulo Roberto Dores-Silva ◽  
Carlos Alberto Montanari ◽  
Carlos Henrique Inácio Ramos ◽  
...  
Keyword(s):  
Heat Shock ◽  
Functional Studies ◽  
Heat Shock Cognate Protein ◽  
Cognate Protein

scholarly journals Exogenous Heat Shock Cognate Protein 70 Suppresses LPS-Induced Inflammation by Down-Regulating NF-κB through MAPK and MMP-2/-9 Pathways in Macrophages

Molecules ◽  
2018 ◽  
Vol 23 (9) ◽  
pp. 2124 ◽  
Author(s):  
Erna Sulistyowati ◽  
Mei-Yueh Lee ◽  
Lin-Chi Wu ◽  
Jong-Hau Hsu ◽  
Zen-Kong Dai ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Heat Shock ◽  
Critical Role ◽  
Matrix Metalloproteinase 2 ◽  
No Production ◽  
Raw 264.7 ◽  
Tnf Α ◽  
Heat Shock Cognate Protein ◽  
Anti Inflammatory ◽  
Cognate Protein

Heat shock cognate protein 70 (HSC70), a molecular chaperone, is constitutively expressed by mammalian cells to regulate various cellular functions. It is associated with many diseases and is a potential therapeutic target. Although HSC70 also possesses an anti-inflammatory action, the mechanism of this action remains unclear. This current study aimed to assess the anti-inflammatory effects of HSC70 in murine macrophages RAW 264.7 exposed to lipopolysaccharides (LPS) and to explain its pathways. Mouse macrophages (RAW 264.7) in 0.1 µg/mL LPS incubation were pretreated with recombinant HSC70 (rHSC70) and different assays (Griess assay, enzyme-linked immune assay/ELISA, electrophoretic mobility shift assay/EMSA, gelatin zymography, and Western blotting) were performed to determine whether rHSC70 blocks pro-inflammatory mediators. The findings showed that rHSC70 attenuated the nitric oxide (NO) generation, tumor necrosis factor α (TNF-α) and interleukin 6 (IL-6) expressions in LPS-stimulated RAW264.7 cells. In addition, rHSC70 preconditioning suppressed the activities and expressions of matrix metalloproteinase-2 (MMP-2) and MMP-9. Finally, rHSC70 diminished the nuclear translocation of nuclear factor-κB (NF-κB) and reduced the phosphorylation of extracellular-signal regulated kinases 1/2 (ERK1/2), c-Jun N-terminal kinase (JNK), p38 mitogen-activated protein kinases (MAPK), and phosphatidylinositol-3-kinase (PI3K/Akt). We demonstrate that rHSC70 preconditioning exerts its anti-inflammatory effects through NO production constriction; TNF-α, and IL-6 suppression following down-regulation of inducible nitric oxide synthase (iNOS), cyclooxygenase 2 (COX-2), and MMP-2/MMP-9. Accordingly, it ameliorated the signal transduction of MAPKs, Akt/IκBα, and NF-κB pathways. Therefore, extracellular HSC70 plays a critical role in the innate immunity modulation and mechanisms of endogenous protective stimulation.

Psychophysiological stress induces heat shock cognate protein (HSC)70 mRNA in the cerebral cortex and stomach of rats

1995 ◽  
Vol 675 (1-2) ◽  
pp. 98-102 ◽  
Author(s):  
Shin Fukudo ◽  
Koji Abe ◽  
Michio Hongo ◽  
Atsushi Utsumi ◽  
Yasuto Itoyama
Keyword(s):  
Cerebral Cortex ◽  
Heat Shock ◽  
Psychophysiological Stress ◽  
Hsc 70 ◽  
Heat Shock Cognate Protein ◽  
Cognate Protein
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