Pregnancy-dependent Expression of Leukaemia Inhibitory Factor (LIF), LIF Receptor-β and Interleukin-6 (IL-6) Messenger Ribonucleic Acids in the Porcine Female Reproductive Tract

Placenta ◽  
2000 ◽  
Vol 21 (4) ◽  
pp. 345-353 ◽  
Author(s):  
T. Modrić ◽  
A.A. Kowalski ◽  
M.L. Green ◽  
R.C.M. Simmen ◽  
F.A. Simmen
Keyword(s):  
Interleukin 6 ◽  
Reproductive Tract ◽  
Female Reproductive Tract ◽  
Inhibitory Factor ◽  
Leukaemia Inhibitory Factor ◽  
Ribonucleic Acids

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 Leukaemia inhibitory factor in implantation and uterine biology

Reproduction ◽  
2005 ◽  
Vol 130 (2) ◽  
pp. 131-145 ◽  
Author(s):  
Susan J Kimber
Keyword(s):  
Knockout Mouse ◽  
Reproductive Tract ◽  
Inhibitory Factor ◽  
Glandular Epithelium ◽  
Leukaemia Inhibitory Factor ◽  
Luminal Epithelium

Leukaemia inhibitory factor (LIF) is one of the most important cytokines in the reproductive tract. Without expression of LIF in the uterus, implantation of a blastocyst cannot begin. Yet, 13 years after publication of the phenotype of the LIF knockout mouse we are only just beginning to understand how LIF functions in the uterus. This review addresses our knowledge of the role of LIF in regulating implantation through its influence on the luminal epithelium and stromal decidualization, but also its influence on reproductive tract cells such as leukocytes and glandular epithelium, during the pre-implantation phase of pregnancy.

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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