Up-regulation of leukaemia inhibitory factor and interleukin-6 in transected sciatic nerve and muscle following denervation

1996 ◽  
Vol 6 (2) ◽  
pp. 105-114 ◽  
Author(s):  
J.B. Kurek ◽  
L. Austin ◽  
S.S. Cheema ◽  
P.F. Bartlett ◽  
M. Murphy
Keyword(s):  
Sciatic Nerve ◽  
Interleukin 6 ◽  
Inhibitory Factor ◽  
Leukaemia Inhibitory Factor

scholarly journals R-200. Endometrial interleukin-6 and leukaemia inhibitory factor—regulation by oestradiol, progesterone, and cytokines

1999 ◽  
Vol 14 (Suppl_3) ◽  
pp. 368-368
Author(s):  
T. Strowitzki ◽  
M. von Wolff ◽  
C.J. Thaler ◽  
S. Stieger ◽  
C. Zepf ◽  
...  
Keyword(s):  
Interleukin 6 ◽  
Inhibitory Factor ◽  
Leukaemia Inhibitory Factor

scholarly journals Oncostatin M, leukaemia-inhibitory factor and interleukin 6 trigger different effects on α1-proteinase inhibitor synthesis in human lung-derived epithelial cells

1998 ◽  
Vol 329 (2) ◽  
pp. 335-339 ◽  
Author(s):  
Joanna CICHY ◽  
Stefan ROSE-JOHN ◽  
James TRAVIS
Keyword(s):  
Epithelial Cells ◽  
Interleukin 6 ◽  
Proteinase Inhibitor ◽  
Human Lung ◽  
Biological Activities ◽  
Oncostatin M ◽  
Inhibitory Factor ◽  
Leukaemia Inhibitory Factor ◽  
Common Signal

Interleukin 6 (IL-6), oncostatin M (OSM) and leukaemia-inhibitory factor (LIF) share a common signal-transducing subunit in each of their receptors and thus mediate an overlapping spectrum of biological activities. Although all of these cytokines stimulate the production of α1-proteinase inhibitor (α1-PI) in hepatocyte-derived cells, only OSM is able to up-regulate levels of this inhibitor in epithelial cells originating from the lung. In this study we characterized human lung-derived epithelial-like HTB58 cells for their ability to synthesize α1-PI after treatment with IL-6, OSM and LIF. The results demonstrate that the resistance of HTB58 cells to the effects of IL-6 and LIF was not because of a lack of their individual functional receptors and suggest that OSM utilizes two different receptors, gp130/LIF receptor and gp130/OSM receptor, in lung-derived epithelial cells.

scholarly journals Evidence for the formation of a heterotrimeric complex of leukaemia inhibitory factor with its receptor subunits in solution

1997 ◽  
Vol 325 (3) ◽  
pp. 693-700 ◽  
Author(s):  
Jian-Guo ZHANG ◽  
Catherine M. OWCZAREK ◽  
Larry D. WARD ◽  
Geoffrey J. HOWLETT ◽  
Louis J. FABRI ◽  
...  
Keyword(s):  
Interleukin 6 ◽  
Equilibrium Analysis ◽  
Inhibitory Factor ◽  
Sedimentation Equilibrium ◽  
Leukaemia Inhibitory Factor ◽  
Mouse Serum ◽  
Stable Complex ◽  
Resonance Spectroscopy ◽  
High Affinity ◽  
Α Chain

Leukaemia inhibitory factor (LIF) is a polyfunctional cytokine that is known to require at least two distinct receptor components (LIF receptor α-chain and gp130) in order to form a high-affinity, functional, receptor complex. Human LIF binds with unusually high affinity to a naturally occurring mouse soluble LIF receptor α-chain, and this property was used to purify a stable complex of human LIF and mouse LIF receptor α-chain from pregnant-mouse serum. Recombinant soluble human gp130 was expressed, with a FLAG® epitope (DYKDDDDK) at the N-terminus, in the methylotropic yeast Pichia pastoris and purified using affinity chromatography. The formation of a trimeric complex in solution was established by native gel electrophoresis, gel-filtration chromatography, sedimentation equilibrium analysis, surface plasmon resonance spectroscopy and chemical cross-linking. The stoichiometry of this solution complex was 1:1:1, in contrast with that of the complex of interleukin-6, the interleukin-6-specific low-affinity receptor subunit and gp130, which is 2:2:2.

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