Interleukin 3

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Interleukin 3
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols IL3 ; IL-3; MCGF; MULTI-CSF
External IDs OMIM147740 HomoloGene47938 GeneCards: IL3 Gene
RNA expression pattern
PBB GE IL3 207906 at tn.png
More reference expression data
Species Human Mouse
Entrez 3562 n/a
Ensembl ENSG00000164399 ENSMUSG00000018914
UniProt P08700 n/a
RefSeq (mRNA) NM_000588 n/a
RefSeq (protein) NP_000579 n/a
Location (UCSC) Chr 5:
132.06 – 132.06 Mb
PubMed search [1] n/a

Interleukin 3, also known as IL-3, is a protein that in humans is encoded by the IL3 gene.[1][2]


Interleukin-3 (IL-3) is an interleukin, a type of biological signal (cytokine) that can improve the body's natural response to disease as part of the immune system. It acts by binding to the interleukin-3 receptor.

IL-3 stimulates the differentiation of multipotent hematopoietic stem cells into myeloid progenitor cells or, with the addition of IL-7, into lymphoid progenitor cells. In addition, IL-3 stimulates proliferation of all cells in the myeloid lineage (granulocytes, monocytes, and dendritic cells), in conjunction with other cytokines, e.g., Erythropoietin (EPO), Granulocyte macrophage colony-stimulating factor (GM-CSF), and IL-6. It is secreted by basophils and activated T cells to support growth and differentiation of T cells from the bone marrow in an immune response. Activated T cells can either induce their own proliferation and differentiation (autocrine signalling), or that of other T cells (paracrine signalling) - both involve IL-2 binding to the IL-2 receptor on T cells (upregulated upon cell activation, under the induction of macrophage-secreted IL-1). The human IL-3 gene encodes a protein 152 amino acids long, and the naturally occurring IL-3 is glycosylated. The human IL-3 gene is located on chromosome 5, only 9 kilobases from the GM-CSF gene, and its function is quite similar to GM-CSF.


Interleukin-3 originally was discovered by JN Ihle in mice. He found a T cell derived factor that induced the synthesis of 20alpha-hydroxysteroid dehydrogenase in hematopoietic cells and termed it interleukin-3.[3][4]


Interleukin 3 has been shown to interact with IL3RA.[5][6]

See also[edit]


  1. ^ "Entrez Gene: IL3 interleukin 3 (colony-stimulating factor, multiple)". 
  2. ^ Yang YC, Ciarletta AB, Temple PA, Chung MP, Kovacic S, Witek-Giannotti JS, Leary AC, Kriz R, Donahue RE, Wong GG (October 1986). "Human IL-3 (multi-CSF): identification by expression cloning of a novel hematopoietic growth factor related to murine IL-3". Cell 47 (1): 3–10. doi:10.1016/0092-8674(86)90360-0. PMID 3489530. 
  3. ^ Ihle JN, Pepersack L, Rebar L (June 1981). "Regulation of T cell differentiation: in vitro induction of 20 alpha-hydroxysteroid dehydrogenase in splenic lymphocytes from athymic mice by a unique lymphokine". J. Immunol. 126 (6): 2184–9. PMID 6971890. 
  4. ^ Ihle JN, Weinstein Y, Keller J, Henderson L, Palaszynski E (1985). "Interleukin 3". Meth. Enzymol. Methods in Enzymology 116: 540–52. doi:10.1016/S0076-6879(85)16042-8. ISBN 978-0-12-182016-9. PMID 3003517. 
  5. ^ Stomski FC, Sun Q, Bagley CJ, Woodcock J, Goodall G, Andrews RK, Berndt MC, Lopez AF (June 1996). "Human interleukin-3 (IL-3) induces disulfide-linked IL-3 receptor alpha- and beta-chain heterodimerization, which is required for receptor activation but not high-affinity binding". Mol. Cell. Biol. 16 (6): 3035–46. PMC 231298. PMID 8649415. 
  6. ^ Woodcock JM, Zacharakis B, Plaetinck G, Bagley CJ, Qiyu S, Hercus TR, Tavernier J, Lopez AF (November 1994). "Three residues in the common beta chain of the human GM-CSF, IL-3 and IL-5 receptors are essential for GM-CSF and IL-5 but not IL-3 high affinity binding and interact with Glu21 of GM-CSF". EMBO J. 13 (21): 5176–85. PMC 395466. PMID 7957082. 

Further reading[edit]