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- Table of Contents
68 Citations 11 Q&As
45 Citations 9 Q&As
3 Citations 18 Q&As
4 Citations 5 Q&As
6 Q&As
9 Citations
Facts about Interleukin-18.
Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells and natural killer (NK) cells (Probable) (PubMed:10653850). .
Human | |
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Gene Name: | IL18 |
Uniprot: | Q14116 |
Entrez: | 3606 |
Belongs to: |
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IL-1 family |
Iboctadekin; IFN-gamma-inducing factor; IGIF; IGIFIL-1 gamma; IL18; IL-18; IL-18MGC12320; IL-1F4; IL1F4iboctadekin; IL-1g; Interferon gamma-inducing factor; interleukin 18 (interferon-gamma-inducing factor); Interleukin-1 gamma; interleukin-18
Mass (kDA):
22.326 kDA
Human | |
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Location: | 11q23.1 |
Sequence: | 11; NC_000011.10 (112143251..112164104, complement) |
Secreted.
This article focuses on the pleiotropic cytokine IL-18 as a biomarker for acute renal injury (AKI). We also discuss how this cytokine may be useful in the detection of other inflammatory diseases like diabetes, hepatitis C and cancer. This article is not meant to provide a complete guide to the IL-18. This article will only focus on the most prominent uses of this marker.
Interleukin 18 (IL-18) is an pleiotropic chemokine that regulates the innate and acquired immune response. This cytokine, which is produced by hematopoietic cells hemopoietic cells, performs a variety functions. It regulates immune responses and encourages the production of IL-4, IgE and IL-13. In vivo, IL-18 stimulates Th2 responses. However, it requires high concentrations to produce the cytokine’s effects.
While IL-18 doesn't trigger the TH2 reaction, it is essential for this response. Without IL-12 IL-18 will not induce the TH2 response. This cytokine was identified in intestinal mRNAs using quantitative RNase protection analysis prior to IL-12. Incredibly, IL-12 induces IL-18 activation but not the effect on IFNg secretion.
The role of the IL-18 protein in atopic dermatology is not clear. Although the production of IL-18 occurs in a variety of types of immune cells it is believed to play a part in modulating the immune response in times of stress. In addition to being found in a variety of tissues, IL-18 is elevated during stress acute or through adrenocorticotropic hormonal treatment. The skin lesions that cause inflammation associated with atopic dermatitis may be due to elevated levels of IL-18.
Expression of IL-18 is not well understood in the context of atherosclerosis, despite these benefits. A new study has shown that fIL-18 levels in patients undergoing heart surgery are raised. IL-18, also referred to as pleiotropic cytokine, promotes IFN-g. FIL-18 may be the ideal drug to control inflammation in patients with heart failure.
Despite its pleiotropic function in inflammatory conditions, IL-18 has been linked with the development of acute Ischamic syndromes. This is due in part to IL-18's function as a degrader of the atherosclerotic plaque. In addition to contributing to atherosclerosis, IL-18 has several other roles in the cardiovascular system. A significant role in the prevention of cardiovascular diseases and stroke is played by regulating the inflammatory processes.
IL-18 inhibits IL-13 production by polarized Th2 cells. Moreover, it is the major inhibitor of IL-13 release in MLN-derived cultures. Therefore, IL-18 may be involved in the immunopathogenesis of myositis. Studies have shown that IL-18 exhibits anti-inflammatory properties. Furthermore, rIL-18 blocks Ag specific IL-13 release from MLN cells.
Moreover, the ability to suppress host immune responses is essential for developing effective anti-poxvirus treatments and vaccines. It is a potent interleukin-18 inhibitor, which is produced by various types of poxviruses such as monkeypox and vaccinia viruses. Its full functional characterization will aid in the development of new vaccines and therapies to combat the disease.
Patients suffering from critical illness are increasingly using the IL-18 biomarker to detect AKI. It has been found to be reliable in patients suffering from serious illness or who undergo bypass surgery for cardiopulmonary disease. It is being investigated to determine its clinical value and the effectiveness. This biomarker could be used to help doctors recognize AKI earlier. Find out more about how it can assist doctors recognize AKI.
The team of researchers analyzed the results from the phase II clinical trial of a biomarker used for AKI called Boster Bio IL18. The study involved a sample of patients with AKI that was classified using the RIFLE classification. The definition of AKI is the serum creatinine increases 50% or more over baseline. Researchers also assessed serum cystatin C levels.
The levels of urine and serum levels of IL-18 and NGAL were also evaluated. These biomarkers can assist doctors identify those patients at high risk of developing AKI. In addition the biomarker will also provide information on other kidney-related cytokines. The results of this study are in line with other research studies. Although there are some limitations in the present study however, further research is required. Particularly, further study should examine the role of the IL-8 biomarker as a marker for AKI.
BUN and serum creatinine are not reliable biomarkers for AKI. There are many variables that could influence the levels of these biomarkers. However it is the more sensitive biomarker for AKI than serum creatinine. In translational research on biomarkers for AKI, IL-18 was more accurate than serum creatinine.
The results of this study have implications for the treatment of AKI. This study also highlights the need to define AKI more specifically. For instance, if a patient have AKI and have a high serum cystatin C level must be at minimum 50% higher than those who don't. However this group did not have other difference from the non-AKI group. They had the same serum creatinine levels and pre-operative MELD scores. Their postoperative urine NGAL and IL-6 levels, however, were higher than those of patients who had not been diagnosed with AKI.
The study suggests a link between urinary NGAL levels and the treatment response. It is not clear how IL-18 affects treatment for AKI. It is usually associated with the presence of parenchymal renal disease. This includes hemodynamic imbalances. Its role in the treatment and prevention of AKI is still being researched. Its use in diagnosing AKI is still the subject of intensive research.
However it has been demonstrated that IL-18 is able to affect inflammation in a variety of renal diseases that include AKI. In the case of experimental animal models, IL-18 has been shown to play a key role in inflammation. The ability of IL-18 to influence inflammation is expected to be helpful in diagnosing the disease, assessing severity of the disease and making decisions on treatment. Once the test has been developed and validated, it should be able to detect those suffering from AKI.
IL-18 is a pleiotropic molecule that has both peripheral and central actions. It stimulates the action of the cytokine IL-12 that promotes differentiation within TH2 lines. It also triggers the production of prostaglandin E2 and the GM-CSF cytokine, two that play an important role in the immune response.
The molecule IL-18 is pleiotropic. This means that it regulates both the innate and acquired immune responses. It has been shown to be a diagnostic marker in many disorders and plays an important role in the inflammatory response. The gene is located on chromosome 11 in humans and chromosome 9 in mice. It has seven exons as well as two distinct promoters. IL-18 also has PU.1 binding locations.
Although the role of IL-18 during immune responses isn't completely understood however, it has been demonstrated that mRNA levels of IL-18 are elevated in macrophages, dendritic cells, and intestinal epithelial cells. Although the production of IL-18 isn't yet understood, it has been shown that it is linked to bacterial infections and continues after the inflammatory event is over.
Early studies highlighted IL-18's IFN-g-inducing capabilities. Recent research suggests that it could also enhance Th2 cytokine creation and IgE synthesis. However, the majority of research suggests that IL-18 is predominantly a TH2 cytokine. It mediates the immune response to Listeria and Trichuris. The absence of IL-18 in B6 mice causes a highly resistant state.
An analysis of RT-PCR has shown the expression of IL-18 in the brain. It was also shown that IL-18 protein is produced by brain cells, including microglia. Experiments on mice expressing I-18 in the brain have revealed that IL-18's levels are elevated following LPS treatment and hypoxic-ischemic injury. This cytokine plays an important role in the nervous system.
IL-18 increases the production of IL-2, IL-13 and other Th2 cytokines. Several researches have linked IL-18 with numerous inflammatory-associated conditions, including auto-immune disease, metabolic disorders, cancer, and autoimmune diseases. It also has anti-tumorigenic effects and induces tumor regression in animal models.
IL-18 plays a key role in the pathogenesis and treatment of type 2 metabolic syndrome and diabetes. The immune system is mediated by IL-18 and stimulates TH2 cells, natural killer cells (NKT) and the established TH2 cell. It also triggers downstream signaling through IL-1b. It binds to the IL-18Ra receptor and then recruits IL-18Rb, IL-18RAcP to the signaling pathway. In addition, IL-18 is negatively regulated by the secreted antagonist receptor IL-18BP. It could also interact with IL-37 and IL-12 to cause synergy between them.
IL-18, a pleiotropic inflammatory cell cytokine was first identified as a factor that triggers IFN-g. Its structure is similar to that of IL-1, and its receptor. IL-18 is activated through TNF receptor-associated factor and nuclear factor kB. It is produced by an inactive precursor that is degraded by the enzyme caspase-1.
PMID: 8666798 by Ushio S., et al. Cloning of the cDNA for human IFN-gamma-inducing factor, expression in Escherichia coli, and studies on the biologic activities of the protein.
PMID: 15326478 by Gaggero A., et al. A novel isoform of pro-interleukin-18 expressed in ovarian tumors is resistant to caspase-1 and -4 processing.
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