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Relevant bibliographies by topics / Leukaemia Inhibitory Factor Receptor

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Academic literature on the topic 'Leukaemia Inhibitory Factor Receptor'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

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Journal articles on the topic "Leukaemia Inhibitory Factor Receptor"

1

CICHY, Joanna, Stefan ROSE-JOHN та James TRAVIS. "Oncostatin M, leukaemia-inhibitory factor and interleukin 6 trigger different effects on α1-proteinase inhibitor synthesis in human lung-derived epithelial cells". Biochemical Journal 329, № 2 (1998): 335–39. http://dx.doi.org/10.1042/bj3290335.

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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

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Schäfer-Somi, S., D. Klein, HB Beceriklisoy, et al. "Uterine Progesterone Receptor and Leukaemia Inhibitory Factor mRNA Expression in Canine Pregnancy." Reproduction in Domestic Animals 44 (July 2009): 109–14. http://dx.doi.org/10.1111/j.1439-0531.2009.01390.x.

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Fry, RC. "The effect of leukaemia inhibitory factor (LIF) on embryogenesis." Reproduction, Fertility and Development 4, no. 4 (1992): 449. http://dx.doi.org/10.1071/rd9920449.

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Leukaemia inhibitory factor (LIF) was originally identified as a haemopoetic factor that induced the differentiation of certain myeloid leukaemia cell lines. In contrast to this action, LIF was subsequently shown to inhibit the spontaneous differentiation of murine embryonic stem cells in culture, thus maintaining their pluripotency and ability to contribute to the germline of chimaeric mice. In the mouse, mRNA for LIF is expressed by the endometrial glands of the uterus coincident with the time of blastocyst implantation and receptors have been found on the preimplantation blastocyst. The sig

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THIEL, Stefan, Iris BEHRMANN, Andreas TIMMERMANN, et al. "Identification of a Leu-Ile internalization motif within the cytoplasmic domain of the leukaemia inhibitory factor receptor." Biochemical Journal 339, no. 1 (1999): 15–19. http://dx.doi.org/10.1042/bj3390015.

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Leukaemia inhibitory factor (LIF) signals via a heterodimeric receptor complex comprised of the LIF receptor (LIFR) and the interleukin (IL)-6 signal transducer gp130. Upon binding to its cognate receptor LIF is internalized. In this study, we show that the LIFR is endocytosed independently of gp130. By using a heterochimaeric receptor system we identified a dileucine-based internalization motif within the cytoplasmic domain of the LIFR. Our findings suggest that a heterodimeric LIFR/gp130 complex and homodimeric gp130/gp130 complex are endocytosed via distinct internalization signals.

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Hirai, Hiroyuki, Peter Karian, and Nobuaki Kikyo. "Regulation of embryonic stem cell self-renewal and pluripotency by leukaemia inhibitory factor." Biochemical Journal 438, no. 1 (2011): 11–23. http://dx.doi.org/10.1042/bj20102152.

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LIF (leukaemia inhibitory factor) is a key cytokine for maintaining self-renewal and pluripotency of mESCs (mouse embryonic stem cells). Upon binding to the LIF receptor, LIF activates three major intracellular signalling pathways: the JAK (Janus kinase)/STAT3 (signal transducer and activator of transcription 3), PI3K (phosphoinositide 3-kinase)/AKT and SHP2 [SH2 (Src homology 2) domain-containing tyrosine phosphatase 2]/MAPK (mitogen-activated protein kinase) pathways. These pathways converge to orchestrate the gene expression pattern specific to mESCs. Among the many signalling events downst

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KASZA, Aneta, Krzysztof ROGOWSKI, Witold KILARSKI, et al. "Differential effects of oncostatin M and leukaemia inhibitory factor expression in astrocytoma cells." Biochemical Journal 355, no. 2 (2001): 307–14. http://dx.doi.org/10.1042/bj3550307.

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The effects of the production of two closely related cytokines, oncostatin M (OSM) and leukaemia inhibitory factor (LIF), by astrocytoma cells were investigated using the stable cell line human U373-MG, which expressed and secreted both biologically active polypeptides. The expression of LIF by these cells caused resistance to this cytokine due to loss of the LIF receptor (LIFR), from the cell surface, suggesting its retention. In contrast, cells expressing OSM were stimulated by this cytokine, utilizing an autocrine mechanism, and possessed receptors for OSM, but not LIF, on the cell surface.

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Owczarek, C. M., M. J. Layton, D. Metcalf, et al. "Inter-species chimeras of leukaemia inhibitory factor define a major human receptor-binding determinant." EMBO Journal 12, no. 9 (1993): 3487–95. http://dx.doi.org/10.1002/j.1460-2075.1993.tb06023.x.

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ZHANG, Jian-Guo, Catherine M. OWCZAREK, Larry D. WARD, et al. "Evidence for the formation of a heterotrimeric complex of leukaemia inhibitory factor with its receptor subunits in solution." Biochemical Journal 325, no. 3 (1997): 693–700. http://dx.doi.org/10.1042/bj3250693.

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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 a

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Harvey, M. B., K. J. Leco, M. Y. Arcellana-Panlilio, X. Zhang, D. R. Edwards, and G. A. Schultz. "Proteinase expression in early mouse embryos is regulated by leukaemia inhibitory factor and epidermal growth factor." Development 121, no. 4 (1995): 1005–14. http://dx.doi.org/10.1242/dev.121.4.1005.

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Several proteinases from different multigene families have been implicated in the uterine invasion required for establishment of pregnancy in some mammals. In this study, the expression of matrix metalloproteinase gelatinase B (MMP-9), urokinase-type plasminogen activator (uPA) and their inhibitors was investigated during early mouse embryo development. Transcripts for tissue inhibitors of metalloproteinases (TIMP-1,-2,-3) and uPA receptor were detected throughout pre- and peri-implantation development whilst MMP-9 and uPA mRNAs were first detected in peri-implantation blastocysts associated w

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CHAMBERS, Ian, Alison COZENS, Joanne BROADBENT, et al. "Structure of the mouse leukaemia inhibitory factor receptor gene: regulated expression of mRNA encoding a soluble receptor isoform from an alternative 5′ untranslated region." Biochemical Journal 328, no. 3 (1997): 879–88. http://dx.doi.org/10.1042/bj3280879.

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The low-affinity leukaemia inhibitory factor receptor (LIF-R) is a component of cell-surface receptor complexes for the multifunctional cytokines leukaemia inhibitory factor, ciliary neurotrophic factor, oncostatin M and cardiotrophin-1. Both soluble and transmembrane forms of the protein have been described and several LIF-R mRNAs have been reported previously. In order to determine the coding potential of LIF-R mRNAs we have isolated and characterized the mouse LIF-R gene. mRNA encoding soluble LIF-R (sLIF-R) is formed by inclusion of an exon in which polyadenylation signals are provided by

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Dissertations / Theses on the topic "Leukaemia Inhibitory Factor Receptor"

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Chobotova, Katya. "Ligand binding determinants of LIF receptor." Thesis, University of Oxford, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.244596.

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Hill, Eric J. "Polarised secretion of leukaemia inhibitory factor." Thesis, Aston University, 2004. http://publications.aston.ac.uk/11019/.

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Leukaemia inhibitory factor (LIF) is a cytokine that is active on a wide variety of cells. Multiple LIF transcripts have been described. The transcripts LIF-D and LIF-M encode different signal peptides, which in mouse have been associated with differential localisation of the mature protein. LIF-D is associated with a freely diffusible protein, whereas the LIF-M is associated with the extracellular matrix. The polarity of LIF secretion has yet to be described and could illuminate the mechanisms of LIF localisation. Here the polarised endogenous secretion of human LIF and IL-6 in Caco-2 cells w

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Grey, Laura M. "Structure and function of leukaemia inhibitory factor." Thesis, University of Oxford, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.359460.

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Sherwin, James Robert Alexander. "The role of leukaemia inhibitory factor in endometrial receptivity." Thesis, University of Cambridge, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.619897.

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Muthukumarana, Poorni Apsara de Silva. "Stem cell factors, axotrophin and leukaemia inhibitory factor in immune regulation." Thesis, University of Cambridge, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.611884.

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Voyle, Roger Bruce. "Mechanisms of intracellular and extracellular cytokine production from the human leukaemia inhibitory factor gene." Title page, contents and summary only, 1999. http://web4.library.adelaide.edu.au/theses/09PH/09phv975.pdf.

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Addendum attached to back facing leaves. Includes bibliographical references (leaves 172-199). The findings establish leukemia inhibitory factor, and possibly oncostatin M, as new members of a small but growing class of cytokines produced in an intracellularly active form and also suggest that the production of alternate transcripts and intercellularly-retained proteins may be a common and important feature of cytokines of the IL-6 and other families.

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Wiest, Stephanie. "Mutationen im Leukaemia-inhibitory-factor-(LIF)-Gen bei wiederholtem Implantationsversagen nach extrakorporaler Befruchtung." [S.l.] : [s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=975102621.

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Segrave, Alicia Maree. "An investigation of the pharmacokinetics and lymphatic transport of recombinant human leukaemia inhibitory factor." Monash University, Dept. of Pharmaceutics, 2004. http://arrow.monash.edu.au/hdl/1959.1/9389.

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Schiemann, William Paul. "Determination and characterization of leukemia inhibitory factor receptor signal transduction systems /." Thesis, Connect to this title online; UW restricted, 1996. http://hdl.handle.net/1773/6277.

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West, Peter William. "The regulation of Toll-like receptor signalling by macrophage migration inhibitory factor." Thesis, University of Sheffield, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.505343.

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Toll-like receptors (TLRs) fonn a vital part of the innate immune response to infection through the recognition of diverse molecular patterns leading to the generation of an inflammatory reaction. The resulting cytokines act on both tissue and immune cells to coordinate the response to infection. Cytokine networks also play an important role in the modulation of an increasing number of diseases which we now understand to have an inflammatory basis. TLR activation has been implicated in both chronic and acute diseases, and understanding and modulation of these responses may be central to th'e m

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Books on the topic "Leukaemia Inhibitory Factor Receptor"

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Gregory, Bock, Marsh Joan, and Widdows Kate, eds. Polyfunctional cytokines: IL-6 and LIF. Wiley, 1992.

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Book chapters on the topic "Leukaemia Inhibitory Factor Receptor"

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Hilton, Douglas J., Nicos A. Nicola, and Donald Metcalf. "Distribution and Binding Properties of Receptors for Leukaemia Inhibitory Factor." In Novartis Foundation Symposia. John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514269.ch14.

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Gearing, David P., Tim VandenBos, M. Patricia Beckmann, et al. "Reconstitution of High Affinity Leukaemia Inhibitory Factor (LIF) Receptors in Haemopoietic Cells Transfected with the Cloned Human LIF Receptor." In Novartis Foundation Symposia. John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514269.ch15.

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Martin, T. J., E. H. Allan, R. S. Evely, and I. R. Reid. "Leukaemia Inhibitory Factor and Bone Cell Function." In Novartis Foundation Symposia. John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514269.ch9.

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Gough, Nicholas M., Tracy A. Willson, Jürgen Stahl, and Melissa A. Brown. "Molecular Biology of the Leukaemia Inhibitory Factor Gene." In Novartis Foundation Symposia. John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514269.ch3.

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Stewart, Colin L. "Leukaemia Inhibitory Factor and the Regulation of Blastocyst Implantation." In Endocrinology of Embryo—Endometrium Interactions. Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-1881-5_22.

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Graham, Amanda, and Warren B. Nothnick. "Concurrent Immunohistochemical Localization and Western Blot Analysis of the MIF Receptor, CD74, in Formalin-Fixed, Paraffin-Embedded Tissue." In Macrophage Migration Inhibitory Factor. Springer US, 2019. http://dx.doi.org/10.1007/978-1-4939-9936-1_11.

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Metcalf, D., P. Waring, and N. A. Nicola. "Actions of Leukaemia Inhibitory Factor on Megakaryocyte and Platelet Formation." In Novartis Foundation Symposia. John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514269.ch11.

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Lotem, Joseph, and Leo Sachs. "Regulation of Leukaemic Cells by Interleukin 6 and Leukaemia Inhibitory Factor." In Novartis Foundation Symposia. John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514269.ch6.

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Baumann, H., S. Marinkovic-Pajovic, K. A. Won, et al. "The Action of Interleukin 6 and Leukaemia Inhibitory Factor on Liver Cells." In Novartis Foundation Symposia. John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514269.ch7.

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Hunt, Liam C., and Jason White. "The Role of Leukemia Inhibitory Factor Receptor Signaling in Skeletal Muscle Growth, Injury and Disease." In Growth Factors and Cytokines in Skeletal Muscle Development, Growth, Regeneration and Disease. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-27511-6_3.

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Conference papers on the topic "Leukaemia Inhibitory Factor Receptor"

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Heinrichs, D., TH Wirtz, A. Saal, et al. "Macrophage Migration Inhibitory Factor promotes HCC progression in vivo via the receptor CD74." In 36. Jahrestagung der Deutschen Arbeitsgemeinschaft zum Studium der Leber. Georg Thieme Verlag KG, 2020. http://dx.doi.org/10.1055/s-0039-3402219.

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Chang, Xiaofei, Yong G. Cho, Il-Seok Park, et al. "Abstract 4799: Promoter methylation of leukemia inhibitory factor receptor gene in colorectal carcinoma." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4799.

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Bell, H., S. Lalnunhlimi, M. Green, F. Van Delft, and A. Krippner-Heidenreich. "Tumour Necrosis Factor receptor (TNFR)-signalling dependent killing in T-cell acute lymphoblastic leukaemia (T-ALL)." In 32. Jahrestagung der Kind-Philipp-Stiftung für pädiatrisch onkologische Forschung. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1687172.

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Zhu, Y. M., and P. S. Daugherty. "Identification of potential inhibitory peptide drugs for vascular endothelial growth factor receptor 2 (VEGFR2, KDR) using bacteria display methods." In 2009 IEEE 35th Annual Northeast Bioengineering Conference. IEEE, 2009. http://dx.doi.org/10.1109/nebc.2009.4967802.

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Iorns, Elizabeth J., Toby M. Ward, Sonja Dean, et al. "Abstract 4979: Whole genome in vivo RNA interference screening identifies the leukemia inhibitory factor receptor as a novel breast tumor suppressor." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4979.

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Iorns, E., T. Ward, S. Dean, et al. "Abstract P5-05-02: Whole Genome In Vivo RNA Interference Screening Identifies the Leukemia Inhibitory Factor Receptor as a Novel Breast Tumor Suppressor." In Abstracts: Thirty-Third Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 8‐12, 2010; San Antonio, TX. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/0008-5472.sabcs10-p5-05-02.

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Simmons, Andrew D., Sarah Jaw-Tsai, Henry J. Haringsma, Andrew Allen, and Thomas C. Harding. "Abstract 793: Insulin-like growth factor 1 (IGF1R)/insulin receptor (INSR) inhibitory activity of rociletinib (CO-1686) and its metabolites in nonclinical models." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-793.

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Saksela, O., D. Moscatelli, and D. B. Rifkin. "THE OPPOSING OF BASIC FIBROBLAST GROWTH FACTOR AND TRANSFORMING GROWTH FACTOR BETA ON THE REGULATION OF PLASMINOGEN ACTIVATOR ACTIVITY IN CAPILLARY ENDOTHELIAL CELLS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644660.

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Basic fibroblast growth factor (bFGF), a potent inducer of angio-genesis in vivo, stimulates the production of both the cell-associated and the secreted forms of urokinase-and tissue-type plasminogen activators (PA) in cultured bovine capillary endothelial cells. This stimulation was counteracted by picogram amounts of transforming growth factor beta The stimulatory effect of bFGF was not completely abolished by increasing the amount of TGFb However, the inhibition by TGFb was greatly enhanced if the cells were pretreated for 1-3 hours with TGFb before addition of bFGF, and the inhibition was

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Dempsey, NG, P. Miller, and M. Lippman. "Abstract P2-06-03: Leukemia inhibitory factor receptor as a tumor suppressor: A study on migration and invasion of breast cancer cells upon LIFR stimulation." In Abstracts: Thirty-Eighth Annual CTRC-AACR San Antonio Breast Cancer Symposium; December 8-12, 2015; San Antonio, TX. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.sabcs15-p2-06-03.

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Kang, Hyung-Gyoo, and Timothy J. Triche. "Abstract 4336: Macrophage migration inhibitory factor (MIF) plays roles in proliferation, survival and migration of Ewing tumor cells by activation of a CD74-CD44 receptor complex." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4336.

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