Heat Shock Protein 70 and Tumor Necrosis Factor Alpha in Taiwanese Patients with Dementia

2005 ◽  
Vol 20 (1) ◽  
pp. 1-7 ◽  
Author(s):  
H.C. Fung ◽  
C.M. Chen ◽  
Y.R. Wu ◽  
W.C. Hsu ◽  
L.S. Ro ◽  
...  
Keyword(s):  
Heat Shock ◽  
Tumor Necrosis Factor ◽  
Heat Shock Protein ◽  
Tumor Necrosis Factor Alpha ◽  
Heat Shock Protein 70 ◽  
Tumor Necrosis ◽  
Necrosis Factor Alpha ◽  
Factor Alpha ◽  
Necrosis Factor

Tumor necrosis factor induces the rapid phosphorylation of the mammalian heat shock protein hsp28

1990 ◽  
Vol 10 (3) ◽  
pp. 1276-1280
Author(s):  
A P Arrigo
Keyword(s):  
Heat Shock ◽  
Tumor Necrosis Factor ◽  
Heat Shock Protein ◽  
Tumor Necrosis Factor Alpha ◽  
Tumor Necrosis ◽  
Tumor Promoter ◽  
Early Event ◽  
Necrosis Factor Alpha ◽  
Factor Alpha ◽  
Necrosis Factor

Tumor necrosis factor alpha was found to rapidly phosphorylate the unique mammalian small heat shock protein hsp28 without impairing its cytoplasmic localization and without inducing the synthesis of the heat shock proteins. In contrast to the C-kinase-dependent phosphorylation of hsp28 in response to the tumor promoter phorbol-12-myristate-13-acetate, the heat- and tumor necrosis factor-mediated phosphorylation of this heat shock protein appears to occur independently of C kinase. These observations suggest that a C-kinase-independent phosphorylation of hsp28 may be an early event in the cellular action of tumor necrosis factor alpha.

scholarly journals Tumor necrosis factor induces the rapid phosphorylation of the mammalian heat shock protein hsp28.

1990 ◽  
Vol 10 (3) ◽  
pp. 1276-1280 ◽  
Author(s):  
A P Arrigo
Keyword(s):  
Heat Shock ◽  
Tumor Necrosis Factor ◽  
Heat Shock Protein ◽  
Tumor Necrosis Factor Alpha ◽  
Tumor Necrosis ◽  
Tumor Promoter ◽  
Early Event ◽  
Necrosis Factor Alpha ◽  
Factor Alpha ◽  
Necrosis Factor

Tumor necrosis factor alpha was found to rapidly phosphorylate the unique mammalian small heat shock protein hsp28 without impairing its cytoplasmic localization and without inducing the synthesis of the heat shock proteins. In contrast to the C-kinase-dependent phosphorylation of hsp28 in response to the tumor promoter phorbol-12-myristate-13-acetate, the heat- and tumor necrosis factor-mediated phosphorylation of this heat shock protein appears to occur independently of C kinase. These observations suggest that a C-kinase-independent phosphorylation of hsp28 may be an early event in the cellular action of tumor necrosis factor alpha.

Differential effects of hyperthermia on macrophage interleukin-6 and tumor necrosis factor-alpha expression

1994 ◽  
Vol 266 (4) ◽  
pp. C967-C974 ◽  
Author(s):  
J. E. Ensor ◽  
S. M. Wiener ◽  
K. A. McCrea ◽  
R. M. Viscardi ◽  
E. K. Crawford ◽  
...  
Keyword(s):  
Heat Shock ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis Factor Alpha ◽  
Interleukin 6 ◽  
Tumor Necrosis ◽  
Elevated Temperatures ◽  
Tnf Alpha ◽  
Necrosis Factor Alpha ◽  
Factor Alpha ◽  
Necrosis Factor

The pyrogenic cytokines tumor necrosis factor-alpha (TNF-alpha) and interleukin-6 (IL-6) appear in the circulation during infections and injuries, but TNF-alpha and IL-6 are regulated differently in macrophages. We compared the effects of elevated temperatures within the usual febrile range on the expression of TNF-alpha and IL-6 in vitro in lipopolysaccharide (LPS)-stimulated human macrophages derived from peripheral blood monocytes (HuMoM phi). During an 18-h incubation at 37 degrees C with 5 ng/ml LPS, these cells released 5,030 +/- 1,460 pg TNF-alpha/10(6) cells (means +/- SE) and 1,380 +/- 280 pg IL-6/10(6) cells. In LPS-stimulated HuMoM phi incubated at 40 degrees C, TNF-alpha release was almost completely inhibited (76 +/- 76 pg TNF-alpha/10(6) cells; P < 0.01 compared with LPS-stimulated HuMoM phi at 37 degrees C), but release of IL-6 was preserved (1,600 +/- 780 pg IL-6/10(6) cells). Western and Northern analyses showed that levels of TNF-alpha mRNA and cell-associated and secreted TNF-alpha protein were decreased, but IL-6 expression was unchanged at 40 degrees C in LPS-stimulated macrophages. Incubating HuMoM phi at 40 degrees did not alter their viability after 18 h but induced a 75-fold increase in levels of the inducible heat-shock protein 72 (HSP-72) mRNA in the face of a 56% inhibition in total protein synthesis. Our results show that IL-6 expression persisted at incubation temperatures in the upper end of the physiological range that induced heat shock and attenuated the expression of functionally active TNF-alpha in LPS-stimulated HuMoM phi.

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