Decoy receptor

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Decoyed signal transduction by decoy receptors

A decoy receptors (in German about, receptor dummy decoy receptor ') is a receptor that its ligand binds, but no signals forwards .

properties

By binding ligands to decoy receptors, the functional receptors have fewer ligands available, which means that the functional receptors are less activated. As a result, decoy receptors act as competitive inhibitors of their respective functional counterparts.

Examples

Interleukin-1 receptor type II

The type II interleukin-1 receptor was described as the first decoy receptor in 1994. Interleukin-1 A and B bind to it , which means that they can no longer bind to interleukin-1 receptor type 1 and thus the interleukin-1 signaling pathway in the immune system is inhibited.

Interleukin-18 binding protein

Interleukin-18 binding protein (IL-18BP) inhibits the effects of interleukin-18 .

Osteoprotegerin

Osteoprotegerin binds the receptor activator of nuclear factor kappa B ligand (RANKL) and inhibits the NF-κB signaling pathway and thus the immune response .

Decoy receptor 3

The decoy receptor 3 (DcR3, synonym TNFRSF6 ) occurs frequently in tumors and inhibits the action of the tumor necrosis factors FasL , LIGHT and TL1A, whereby the initiation of apoptosis via the TNFR is inhibited.

VEGFR-1

VEGFR-1 is a non-functional receptor tyrosine kinase and inhibits the action of VEGF , whereby angiogenesis is regulated via VEGFR-2 .

Applications

A use of decoy receptors to reduce the effects of growth factors in the treatment of cancer is being investigated. Furthermore, decoy receptors for the treatment of Duchenne muscular dystrophy are being investigated.

Individual evidence

  1. ↑ CJ McMahan, JL Slack, B Mosley: A novel IL-1 receptor, cloned from B cells by mammalian expression, is expressed in many cell types . In: The EMBO Journal . . 10, No. 10, 1991, pp. 2821-2832. PMC 452992 (free full text).
  2. ↑ F. Re, M. Muzio, M. De Rossi, N. Poletarutti, JG Giri, A. Mantovani , F. Colotta: The type II "receptor" as a decoy target for interleukin 1 in polymorphonuclear leukocytes: characterization of induction by dexamethasone and ligand binding properties of the released decoy receptor . In: Journal of Experimental Medicine . 179, No. 2, 1994, pp. 739-743. PMC 2191363 (free full text).
  3. ↑ IL1R2 interleukin 1 receptor, type II [Homo sapiens (human) ] . National Center for Biotechnology Information. 2015.
  4. ^ C. Garlanda, CA Dinarello, A. Mantovani: The interleukin-1 family: back to the future. In: Immunity . Volume 39, number 6, December 2013, ISSN  1097-4180 , pp. 1003-1018, doi : 10.1016 / j.immuni.2013.11.010 , PMID 24332029 , PMC 3933951 (free full text).
  5. ↑ Krakauer T: Nuclear factor-kappaB: fine-tuning a central integrator of diverse biological stimuli . In: Int. Rev. Immunol. . 27, No. 5, 2008, pp. 286-92. doi : 10.1080 / 08830180802317957 . PMID 18853340 .
  6. ↑ Avi Ashkenazi: Targeting death and decoy receptors of the tumor-necrosis factor superfamily . In: Nature Reviews Cancer . 2, June 1, 2002, pp. 420-430. doi : 10.1038 / nrc821 .
  7. ↑ Rosana D. Meyer, Moosi Mohammadi, Nader Rahimi: A Single Amino Acid Substitution in the Activation Loop Defines the Decoy Characteristic of VEGFR-1 / FLT-1 * . In: Journal of Biological Chemistry . 281, Jan 13, 2006, pp. 867-875. doi : 10.1074 / jbc.M506454200 .
  8. ↑ UH Weidle, B. Schneider, G. Georges, U. Brinkmann: Genetically engineered fusion proteins for treatment of cancer. In: Cancer Genomics & Proteomics. Volume 9, Number 6, November 2012, ISSN  1790-6245 , pp. 357-372, PMID 23162075 .
  9. ↑ Mihalis S. Kariolis: An engineered Axl 'decoy receptor' effectively silences the Gas6-Axl signaling axis . In: Nature Chemical Biology . 10, September 21, 2014, pp. 977-983. doi : 10.1038 / nchembio.1636 .
  10. ↑ Kenneth M Attie: A single ascending-dose study of muscle regulator ace-031 in healthy volunteers . In: Muscle and Nerve . 47, No. 3, November 21, 2012, pp. 416-423. doi : 10.1002 / mus.23539 .