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An Error has occurred retrieving Wikidata item for infobox Interleukin 24 (IL-24) is a protein that in humans is encoded by the IL24 gene.
IL-24 is a cytokine belonging to the IL-10 family of cytokines that signals through two heterodimeric receptors: IL-20R1/IL-20R2 and IL-22R1/IL-20R2. This interleukin is also known as melanoma differentiation-associated 7 (mda-7) due to its discovery as a tumour suppressing protein. IL-24 appears to control in cell survival and proliferation by inducing rapid activation of particular transcription factors called STAT1 and STAT3. This cytokine is predominantly released by activated monocytes, macrophages and T helper 2 (Th2) cells[1] and acts on non-haematopoietic tissues such as skin, lung and reproductive tissues. IL-24 performs important roles in wound healing, arthritis, psoriasis and cancer.[2][3][4] Several studies have shown that cell death occurs in cancer cells/cell lines following exposure to IL-24.[5][6] The gene for IL-24 is located on chromosome 1 in humans.[7]
Structure
[edit]IL-24 is a secreted protein that is highly conserved throughout evolution with sequence homology between species including yeast, dog, cat, monkey and cow. It is located on chromosome 1q32-33 in humans along with several other IL-10 cytokine family gene members. IL-24 encompasses seven exons and six introns. The cDNA of IL-24 is 1,718 base pairs in length and encodes a protein of 206 amino acid with a predicted molecular size of ˜24 kDa. IL-24 also contains an IL-10 signature motif at amino acids 101–121 shared by other IL-10 family member cytokines. IL-24 possibly can form functionally active dimers due to the presence of potential disulfide bonds. Researchers identified a number of splice variants of IL-24 lacking one or more exons.[8]
Function
[edit]At low concentrations, IL-24 predominantly functions as a cytokine. IL-24 is normally expressed in humans in tissues of the immune system such as the thymus, spleen, peripheral blood leukocytes (PBL) and normal melanocytes. IL-24 plays a role in wound healing, in autoimmune diseases such as psoriasis, rheumatoid arthritis and spondyloarthropathy, and protection against infectious diseases caused by bacteria such as Pseudomonas aeruginosa, Salmonella typhimurium and Mycobacterium tuberculosis.[9] In normal skin cells, it suppress keratinocyte proliferation during wound healing. [10]
Besides the normal physiological role that IL-24 plays in the immune system, IL-24 has been studied in great detail for its role in cancer.[9]
Cancer
[edit]IL-24 is an immunomodulatory cytokine which can also display broad cancer-specific suppressor effects. The tumor suppressor activities of IL-24 include inhibition of angiogenesis, sensitization to chemotherapy, and induction of cancer-specific apoptosis. Given its ubiquitous apoptotic effect on malignant cells, lack of an effect on normal cells, and absence of significant side effects, IL-24 is an important candidate for cancer therapy.[11]
IL-24 is able to induce apoptosis via both intracellular and extracellular signaling mechanisms. Secreted IL-24 protein induces a robust expression of endogenous IL-24 and subsequent induction of tumor-specific killing through an ER stress-mediated pathway as well as by ROS production. The ER stress is the initial pathway in IL-24-induced apoptosis.[11]
An important question, which remained unresolved, is why IL-24 has the abilities to selectively induce apoptosis in a large spectrum of human cancer-derived cell lines without harming normal cells. One possible reason for this differential killing effect involves inherent biochemical differences between normal and cancer cells (ER stress, ROS production and ceramide), another possibility is that IL-24 is able to target a molecule that only triggers apoptosis in cancer cells. The third option for this differential killing effect is that both of the above hypotheses are correct.[11]
References
[edit]- ^ Poindexter NJ, Walch ET, Chada S, Grimm EA (September 2005). "Cytokine induction of interleukin-24 in human peripheral blood mononuclear cells". J. Leukoc. Biol. 78 (3): 745–52. doi:10.1189/jlb.0205116. PMID 16000394.
- ^ Wang M, Liang P (February 2005). "Interleukin-24 and its receptors". Immunology. 114 (2): 166–70. doi:10.1111/j.1365-2567.2005.02094.x. PMC 1782067. PMID 15667561.
- ^ Kragstrup, TW; Otkjaer, K; Holm, C; Jørgensen, A; Hokland, M; Iversen, L; Deleuran, B (January 2008). "The expression of IL-20 and IL-24 and their shared receptors are increased in rheumatoid arthritis and spondyloarthropathy" (PDF). Cytokine. 41 (1): 16–23. doi:10.1016/j.cyto.2007.10.004. PMID 18061474.
- ^ Kragstrup, Tue Wenzel; Greisen, Stinne Ravn; Nielsen, Morten Aagaard; Rhodes, Christopher; Stengaard-Pedersen, Kristian; Hetland, Merete Lund; Hørslev-Petersen, Kim; Junker, Peter; Østergaard, Mikkel; Hvid, Malene; Vorup-Jensen, Thomas; Robinson, William H.; Sokolove, Jeremy; Deleuran, Bent (11 March 2016). "The interleukin-20 receptor axis in early rheumatoid arthritis: novel links between disease-associated autoantibodies and radiographic progression". Arthritis Research & Therapy. 18 (1): 61. doi:10.1186/s13075-016-0964-7. PMC 4788924. PMID 26968800.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Fisher PB, Gopalkrishnan RV, Chada S, Ramesh R, Grimm EA, Rosenfeld MR, Curiel DT, Dent P (2003). "mda-7/IL-24, a novel cancer selective apoptosis inducing cytokine gene: from the laboratory into the clinic". Cancer Biol. Ther. 2 (4 Suppl 1): S23–37. doi:10.4161/cbt.458. PMID 14508078.
- ^ Sauane M, Lebedeva IV, Su ZZ, Choo HT, Randolph A, Valerie K, Dent P, Gopalkrishnan RV, Fisher PB (May 2004). "Melanoma differentiation associated gene-7/interleukin-24 promotes tumor cell-specific apoptosis through both secretory and nonsecretory pathways". Cancer Res. 64 (9): 2988–93. doi:10.1158/0008-5472.CAN-04-0200. PMID 15126330.
- ^ IL24 GeneCard
- ^ Emdad, Luni; Bhoopathi, Praveen; Talukdar, Sarmistha; Pradhan, Anjan K.; Sarkar, Devanand; Wang, Xiang-Yang; Das, Swadesh K.; Fisher, Paul B. (2019-7). "Recent insights into apoptosis and toxic autophagy: The roles of MDA-7/IL-24, a multidimensional anti-cancer therapeutic". Seminars in Cancer Biology. doi:10.1016/j.semcancer.2019.07.013.
{{cite journal}}: Check date values in:|date=(help) - ^ a b Menezes, Mitchell E.; Bhatia, Shilpa; Bhoopathi, Praveen; Das, Swadesh K.; Emdad, Luni; Dasgupta, Santanu; Dent, Paul; Wang, Xiang-Yang; Sarkar, Devanand (2014), Grimm, Stefan (ed.), "MDA-7/IL-24: Multifunctional Cancer Killing Cytokine", Anticancer Genes, vol. 818, Springer London, pp. 127–153, doi:10.1007/978-1-4471-6458-6_6, ISBN 9781447164579, PMC 4633013, PMID 25001534
- ^ Whitaker, Erin L.; Filippov, Valery A.; Duerksen-Hughes, Penelope J. (2012-12). "Interleukin 24: Mechanisms and therapeutic potential of an anti-cancer gene". Cytokine & Growth Factor Reviews. 23 (6): 323–331. doi:10.1016/j.cytogfr.2012.08.004. PMID 22981288.
{{cite journal}}: Check date values in:|date=(help) - ^ a b c Persaud, Leah; De Jesus, Dayenny; Brannigan, Oliver; Richiez-Paredes, Maria; Huaman, Jeannette; Alvarado, Giselle; Riker, Linda; Mendez, Gissete; Dejoie, Jordan (2016-06-02). "Mechanism of Action and Applications of Interleukin 24 in Immunotherapy". International Journal of Molecular Sciences. 17 (6): 869. doi:10.3390/ijms17060869. ISSN 1422-0067. PMC 4926403. PMID 27271601.
{{cite journal}}: CS1 maint: unflagged free DOI (link)
External links
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References
[edit]- ^ Otáhal, Pavel; Angelisová, Pavla; Hrdinka, Matouš; Brdička, Tomáš; Novák, Petr; Drbal, Karel; Hořejší, Václav (04/01/2010). "A New Type of Membrane Raft-Like Microdomains and Their Possible Involvement in TCR Signaling". The Journal of Immunology. 184 (7): 3689–3696. doi:10.4049/jimmunol.0902075. ISSN 0022-1767. PMID 20207997.
{{cite journal}}: Check date values in:|date=(help) - ^ Hrdinka, Matouš; Dráber, Peter; Štěpánek, Ondřej; Ormsby, Tereza; Otáhal, Pavel; Angelisová, Pavla; Brdička, Tomáš; Pačes, Jan; Hořejší, Václav (06/03/2011). "PRR7 Is a Transmembrane Adaptor Protein Expressed in Activated T Cells Involved in Regulation of T Cell Receptor Signaling and Apoptosis". Journal of Biological Chemistry. 286 (22): 19617–19629. doi:10.1074/jbc.M110.175117. ISSN 0021-9258. PMID 21460222.
{{cite journal}}: Check date values in:|date=(help)CS1 maint: unflagged free DOI (link) - ^ Kriehuber, E.; Breiteneder-Geleff, S.; Groeger, M.; Soleiman, A.; Schoppmann, S. F.; Stingl, G.; Kerjaschki, D.; Maurer, D. (Sep 17, 2001). "Isolation and characterization of dermal lymphatic and blood endothelial cells reveal stable and functionally specialized cell lineages". The Journal of Experimental Medicine. 194 (6): 797–808. ISSN 0022-1007. PMC 2195953. PMID 11560995.
- ^ Hrdinka, Matous; Dráber, Peter; Stepánek, Ondrej; Ormsby, Tereza; Otáhal, Pavel; Angelisová, Pavla; Brdicka, Tomás; Paces, Jan; Horejsí, Václav (Jun 3, 2011). "PRR7 is a transmembrane adaptor protein expressed in activated T cells involved in regulation of T cell receptor signaling and apoptosis". The Journal of Biological Chemistry. 286 (22): 19617–19629. doi:10.1074/jbc.M110.175117. ISSN 1083-351X. PMC 3103341. PMID 21460222.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Wu, Hong; Wang, Jun; Wang, Zhemin; Fisher, Darrell R.; Lin, Yuehe (2008-05). "Apoferritin-templated yttrium phosphate nanoparticle conjugates for radioimmunotherapy of cancers". Journal of Nanoscience and Nanotechnology. 8 (5): 2316–2322. ISSN 1533-4880. PMID 18572643.
{{cite journal}}: Check date values in:|date=(help) - ^ Fibronectin type iii repeat based protein scaffolds with alternative binding surfaces, retrieved 2015-06-04
- ^ Gowda, D. C. (2002-07). "Structure and activity of glycosylphosphatidylinositol anchors of Plasmodium falciparum". Microbes and Infection. 4 (9): 983–990. ISSN 1286-4579.
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