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Title: Interleukin-4  
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Subject: Mosquito, T helper cell, Immunotherapy, Interleukin, Interleukin 2, Index of oncology articles, Ionomycin, Ellen Vitetta, CD23, CD40 (protein)
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Interleukin 4

Crystal structure of human IL-4 (2INT)
Available structures
PDB Ortholog search: RCSB
IL4 Gene
RNA expression pattern
Interleukin 4
analysis of the solution structure of human interleukin 4 determined by heteronuclear three-dimensional nuclear magnetic resonance techniques
Symbol IL4
Pfam Pfam clan InterPro PROSITE PDOC00655

Interleukin 4, abbreviated IL-4, is a cytokine that induces differentiation of naive helper T cells (Th0 cells) to Th2 cells. Upon activation by IL-4, Th2 cells subsequently produce additional IL-4. The cell that initially produces IL-4, thus inducing Th0 differentiation, has not been identified, but recent studies suggest that basophils may be the effector cell.[1] It is closely related and has functions similar to Interleukin 13.

Its receptor is the Interleukin-4 receptor.


It has many biological roles, including the stimulation of activated B-cell and T-cell proliferation, and the differentiation B cells into plasma cells.

It is a key regulator in humoral and adaptive immunity.

IL-4 induces B-cell class switching to IgE, and up-regulates MHC class II production. IL-4 decreases the production of Th1 cells, macrophages, IFN-gamma, and dendritic cell IL-12.

Overproduction of IL-4 is associated with allergies.[2]

In inflammation and wound repair

Tissue macrophages play an important role in chronic inflammation and wound repair. The presence of IL-4 in extravascular tissues promotes alternative activation of macrophages into M2 cells and inhibits classical activation of macrophages into M1 cells. An increase in repair macrophages (M2) is coupled with secretion of IL-10 and TGF-β that result in a diminution of pathological inflammation. Release of arginase, proline, polyaminases and TGF-β by the activated M2 cell is tied with wound repair and fibrosis.[3]

Clinical significance

IL-4 also has been shown to drive mitogenesis, dedifferentiation, and metastasis in rhabdomyosarcoma.[4]


IL-4 has a compact, globular fold (similar to other cytokines), stabilised by 3 disulphide bonds.[5] One half of the structure is dominated by a 4 alpha-helix bundle with a left-handed twist.[6] The helices are anti-parallel, with 2 overhand connections, which fall into a 2-stranded anti-parallel beta-sheet.[6]


This cytokine was co-discovered by Maureen Howard and William Paul[7] and by Dr. Ellen Vitetta and her research group in 1982.

The nucleotide sequence for human IL-4 was isolated four years later confirming its similarity to a mouse protein called B-cell stimulatory factor-1 (BCSF-1).[8]

See also


Further reading

External links

  • Medical Subject Headings (MeSH)
  • Interleukin-4 from Gentaur at Gentaur
  • Cornell University
  • Health On the Net Foundation

This article incorporates text from the IPR002354

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