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HSPB1 — IL6

Text-mined interactions from Literome

Santell et al., Biochem J 1992 : Down-regulation of protein kinase C-alpha by prolonged treatment with phorbol esters eliminated the ability of phorbol 12-myristate 13-acetate, dioctanoylglycerol, thrombin and histamine to phosphorylate HSP27 above background levels and deceased interleukin-1 stimulated HSP27 phosphorylation by 60 %
Wilhelmus et al., Neurobiol Aging 2009 (Cerebral Amyloid Angiopathy, Familial) : In addition, we demonstrated that Hsp20, HspB2 and HspB8 induced interleukin-6 production in cultured pericytes and astrocytes, which could be antagonized by dexamethasone, whereas other sHsps and A beta were inactive, suggesting that sHsps may be among the key mediators of the local inflammatory response associated with HCHWA-D and AD lesions
Katalinić et al., Chem Biol Interact 2013 : Namely, secretion of IL-6 decreased to 53 % and the level of HSP 27 increased by 34 % compared to the control level
Kondo et al., Mol Med Report 2013 : It has previously been demonstrated that HSP27 regulated the synthesis of osteocalcin and interleukin-6 in osteoblast-like MC3T3-E1 cells
Cuenda et al., FEBS Lett 1995 : We now show that one of these compounds ( SB 203580 ) inhibits RK in vitro ( IC50 = 0.6 microM ), suppresses the activation of MAPKAP kinase-2 and prevents the phosphorylation of heat shock protein (HSP) 27 in response to interleukin-1 , cellular stresses and bacterial endotoxin in vivo
Belka et al., Leukemia 1995 (Leukemia, Monocytic, Acute) : Interleukin (IL)-6 signaling leads to phosphorylation of the small heat shock protein (Hsp)27 through activation of the MAP kinase and MAPKAP kinase 2 pathway in monocytes and monocytic leukemia cells ... These findings suggest that IL-6 mediated phosphorylation of Hsp27 results from activation of MAPKAP kinase 2, a serine/threonine kinase which is activated by MAP kinase