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Macrophage inhibitory factor

Release of larger amounts of macrophage inhibitory factor (MIF) by homogeneous suspensions of DCs isolated from patients with colitis ulcerosa, due to the effect of Thl lymphocyte cytokines, in comparison with healthy human DC. It was observed that in an in vitro test MIF blocks the flow of mononuclear cells and granulocytes, while in in vivo it is released not only by lymphocytes but also by dendritic cells and leads to cell accumulation— occurrence of inflammatory infiltration. Disease development is also the result of the effect of TNFa, IL 1, IL 6, IL 8, and other cytokines released by macrophages and lymphocytes (Murakami et al., 2002). Thus, it has been proved that DCs can release MIF. [Pg.12]

Receptors for cytokines including those involved in macrophage activation (e.g. interferon-y — IFN-y) or limiting macrophage mobility (e.g. macrophage inhibitory factor—MIF) and hence increasing cell retention at a site of infection. [Pg.122]

A number of adipokines are linked to inflammation and immunity (Fig. 1). This includes both leptin and adiponectin, and also a number of other key inflammatory proteins, particularly cytokines and chemokines [1]. The cytokines and chemokines encompass interleukin-1(3 (EL-1 (3), IL-6, DL-10, TNFa, monocyte chemoattractant protein-1 (MCP-1), and macrophage migration inhibitory factor (MIF). Other major inflammation-related adipokines include nerve growth factor (NGF), and acute phase proteins such as serum amyloid A and haptoglobin. In addition, adipocytes secrete plasminogen activator inhibitor-1 (PAI-1), which is an important thrombotic factor as well as an acute phase protein. [Pg.39]

A macrophage migration inhibitory factor (MIF) which encourages the maerophages to remain in the area. [Pg.295]

Suzuki, M., et al., Xenopus laevis macrophage migration inhibitory factor is essential for axis formation and neural development, J. Biol. Chem., 279, 21406, 2004. [Pg.397]

Macrophage migration inhibitory factor Monocyte colony-stimulating factor Tumor necrosis factor- a Tumor necrosis factor- P... [Pg.393]

IL-10 A cytokine inhibitory factor synthesized by TH2 cells, macrophages, and B cells. IL-10 inhibits the formation of inflammatory cytokines. Its synthesis is most reliably determined by means of IL-10 mRNA expression in mononuclear cells. [Pg.21]

Haematopoietins Interleukins 2-7, -9, -13 Granulocyte colony stimulating factor Granulocyte-macrophage colony stimulating factor Leukaemia inhibitory factor Erythropoietin Ciliary neurotrophic factor... [Pg.192]

Kofoed, K., et al. (2007) Use of plasma C-reactive protein, procalcitonin, neutrophils, macrophage migration inhibitory factor, soluble urokinase-type plasminogen activator receptor, and soluble triggering receptor expressed on myeloid cells-1 in combination to diagnose infections a prospective study. Crit Care. 11, R38. [Pg.214]

Figure 25-5 shows the principal catabolic pathways, as well as a few biosynthetic reactions, of phenylalanine and tyrosine in animals. Transamination to phenylpyruvate (reaction a) occurs readily, and the product may be oxidatively decarboxylated to phen-ylacetate. The latter may be excreted after conjugation with glycine (as in Knoop s experiments in which phenylacetate was excreted by dogs after conjugation with glycine, Box 10-A). Although it does exist, this degradative pathway for phenylalanine must be of limited importance in humans, for an excess of phenylalanine is toxic unless it can be oxidized to tyrosine (reaction b, Fig. 25-5). Formation of phenylpyruvate may have some function in animals. The enzyme phenylpyruvate tautomerase, which catalyzes interconversion of enol and oxo isomers of its substrate, is also an important immunoregulatory cytokine known as macrophage migration inhibitory factor.863... Figure 25-5 shows the principal catabolic pathways, as well as a few biosynthetic reactions, of phenylalanine and tyrosine in animals. Transamination to phenylpyruvate (reaction a) occurs readily, and the product may be oxidatively decarboxylated to phen-ylacetate. The latter may be excreted after conjugation with glycine (as in Knoop s experiments in which phenylacetate was excreted by dogs after conjugation with glycine, Box 10-A). Although it does exist, this degradative pathway for phenylalanine must be of limited importance in humans, for an excess of phenylalanine is toxic unless it can be oxidized to tyrosine (reaction b, Fig. 25-5). Formation of phenylpyruvate may have some function in animals. The enzyme phenylpyruvate tautomerase, which catalyzes interconversion of enol and oxo isomers of its substrate, is also an important immunoregulatory cytokine known as macrophage migration inhibitory factor.863...
Rodriguez-Sosa, M., Rosas, L.E., David, J.R., Bojalil, R., Satoskar, A.R. and Terrazas, L.l. (2003b) Macrophage migration inhibitory factor plays a critical role in mediating protection against the helminth parasite Taenia crassiceps. Infection and Immunity 71, 1247-1254. [Pg.208]

Tofaris, G. K., Patterson, P. H., Jessen, K. R., and Mirsky, R. (2002). Denervated Schwann cells attract macrophages by secretion of leukemia inhibitory factor (LIF) and monocyte chemoattractant protein-1 in a process regulated by interleukin-6 and LIF. J. Neurosci. 22, 6696-6703. [Pg.189]

Murakami, H., Akbar, S. M. F., Matsui, H., Horiike, N., and Onji M. 2002. Macrophage migration inhibitory factor activates antigen-presenting dendritic cells and induces inflammatory cytokines in ulcerative colitis. Clin Exp Immunol 128 504—510. [Pg.39]

Cytokine subfamily 2 includes proteins with heterodimeric a—(3 or ct-gpl30 receptors. Thus, granulocyte macrophage colony stimulating factor (GM-GSF), IL-3 and IL-5 act via a—(3 receptors and share (3 receptors. Cardiotrophin-1 (GT-1), ciliary neurotrophic factor (CTNF), IL-6, IL-1, leukaemia inhibitory factor (LIF) and oncostatin M (OSM) act via heterodimeric a-gpl30 receptors with a shared gpl30 receptor subunit. Leucocyte-derived cytokines of this family have immunomodulatory and haematopoietic effects. [Pg.302]

Metz, C. N., and Bucala, R. (1997). Role of macrophage migration inhibitory factor in the regulation of the immune response. Adv. Immunol. 66, 197-223. [Pg.11]

Swope, M. D., and Lolis, E. (1999). Macrophage migration inhibitory factor cytokine, hormone, or enzyme Rev. Physiol. Biochem. Pharmacol. 139, 1-32. [Pg.11]


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See also in sourсe #XX -- [ Pg.12 ]




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