Gene expression of tumour necrosis factor-? (TNF-?) and heat-shock protein (HSP) 70 in patients with Beh�et's disease

1993 ◽  
Vol 285 (8) ◽  
pp. 505-508 ◽  
Author(s):  
Y. Yamakawa ◽  
Y. Sugita ◽  
Y. Takahashi ◽  
T. Yamakawa ◽  
S. -i. Tanaka ◽  
...  
Keyword(s):  
Gene Expression ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Hsp 70 ◽  
Necrosis Factor

scholarly journals Phosphorylation of the small heat-shock protein is regulated by interleukin 1, tumour necrosis factor, growth factors, bradykinin and ATP

1991 ◽  
Vol 277 (3) ◽  
pp. 635-642 ◽  
Author(s):  
J Saklatvala ◽  
P Kaur ◽  
F Guesdon
Keyword(s):  
Growth Factor ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Interleukin 1 ◽  
Small Heat Shock Protein ◽  
Prolonged Treatment ◽  
Hsp 27 ◽  
Necrosis Factor

Interleukin 1 (IL1) increased phosphorylation of the small heat-shock protein (hsp 27) in MRC5 fibroblasts. The increase was maintained for at least 30 min, but levels had returned to pre-stimulation values by 2 h. When hsp 27 was metabolically labelled with [3H]leucine, about 15% was phosphorylated in resting confluent cells; this rose to 90% upon stimulation by IL1. Peptide maps of the three differently charged phosphorylated forms were consistent with their arising by phosphorylation of increasing numbers of serine residues. IL1 had the same effect on hsp 27 in pig articular chondrocytes, endothelial cells from human umbilical vein and an epidermoid carcinoma cell line (KB). Certain other agents were found selectively to increase phosphorylation of hsp 27 in MRC5 cells besides IL1 [and tumour necrosis factor (TNF)]. Platelet-derived growth factor had a similar effect to that of IL1; bradykinin, acid fibroblast growth factor and ATP caused an intermediate effect; phorbol myristate acetate (PMA) and 1-oleoyl-2-acetylglycerol had smaller effects. Dibutyryl cyclic AMP and forskolin had no effects on hsp 27 phosphorylation. When cells had been depleted of protein kinase C (PKC) by prolonged treatment with PMA, stimulation by IL1, TNF or bradykinin still increased hsp 27 phosphorylation. The stimulation by all three agents was also unaffected by the PKC inhibitor staurosporine. IL1, TNF and bradykinin each caused hsp 27 phosphorylation by a pathway independent of PKC. The results are consistent with IL1 activating a serine kinase which remains to be identified.

Endogenous tumour necrosis factor regulates heat-inducible heat shock protein 72 synthesis

1998 ◽  
Vol 14 (3) ◽  
pp. 309-317 ◽  
Author(s):  
N. Watanabe ◽  
N. Tsuji ◽  
S. Akiyama ◽  
H. Sasaki ◽  
T. Okamoto ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Heat Shock Protein 72 ◽  
Necrosis Factor
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