Interleukin 3

From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
IL3
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesIL3, interleukin 3, IL-3, MCGF, MULTI-CSF
External IDsOMIM: 147740 HomoloGene: 47938 GeneCards: IL3
Gene location (Human)
Chromosome 5 (human)
Chr.Chromosome 5 (human)[1]
Chromosome 5 (human)
Genomic location for IL3
Genomic location for IL3
Band5q31.1Start132,060,529 bp[1]
End132,063,204 bp[1]
RNA expression pattern
PBB GE IL3 207906 at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000588

n/a

RefSeq (protein)

NP_000579

n/a

Location (UCSC)Chr 5: 132.06 – 132.06 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

Interleukin 3 (IL-3) is a protein that in humans is encoded by the IL3 gene.[3][4]

Function[edit]

Interleukin 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.

Interleukin 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.

Discovery[edit]

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.[5][6]

Interactions[edit]

Interleukin 3 has been shown to interact with IL3RA.[7][8]

See also[edit]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000164399 - Ensembl, May 2017
  2. ^ "Human PubMed Reference:".
  3. ^ "Entrez Gene: IL3 interleukin 3 (colony-stimulating factor, multiple)".
  4. ^ 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.
  5. ^ 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.
  6. ^ Ihle JN, Weinstein Y, Keller J, Henderson L, Palaszynski E (1985). Interleukin 3. Meth. Enzymol. Methods in Enzymology. 116. pp. 540–52. doi:10.1016/S0076-6879(85)16042-8. ISBN 978-0-12-182016-9. PMID 3003517.
  7. ^ 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. doi:10.1128/MCB.16.6.3035. PMC 231298. PMID 8649415.
  8. ^ 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. doi:10.1002/j.1460-2075.1994.tb06848.x. PMC 395466. PMID 7957082.

Further reading[edit]