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interleukin-5 (IL5; eosinophil differentiation factor) 403 interleukin-6 (IL6)<br />

2–8 Days<br />

12 Hours<br />

12 Hours<br />

3 H-Thy<br />

Induction of Interleukin-4 response in short-term culture.<br />

COOH<br />

p140<br />

α-chain<br />

Interleukin-4.<br />

COOH<br />

of IL4, the IL2 receptor γ chain associates with the ILRα<br />

chain. This complex comprises the type I IL4 receptor. The<br />

IL13 low affinity binding chain (IL13Rα) can also associate<br />

with IL4Rα. The IL4 receptor containing the IL13Rα is<br />

termed type II.<br />

interleukin-5 (IL5; eosinophil differentiation factor)<br />

A 20-kDa cytokine synthesized by some activated CD4 +<br />

T h2 lymphocytes and activated mast cells. A part of the<br />

hematopoietic family, human IL5 is 150-amino acids in<br />

γ c<br />

Interleukin-5 crystal structure.<br />

length and murine IL5 is 133-amino acids long. The IL5<br />

gene is located on chromosome 11 in mice and on chromosome<br />

5 in humans. Formerly, it was called T cell-replacing<br />

factor or B cell growth factor II. It facilitates B cell growth<br />

and differentiation into cells that secrete immunoglobulin A<br />

(IgA). It is a costimulator with IL2 and IL4 of B cell growth<br />

and differentiation. IL5 also stimulates eosinophil growth<br />

and differentiation. It activates mature eosinophils to render<br />

them capable of killing helminths. Through IL5, T lymphocytes<br />

exert a regulatory effect on inflammation mediated by<br />

eosinophils. Because of its action in promoting eosinophil<br />

differentiation, it has been called eosinophil differentiation<br />

factor (EDF). IL5 can facilitate B cell differentiation into<br />

plaque-forming cells of the immunoglobulin M (IgM) and<br />

IgG classes. It is associated with various allergic diseases<br />

including allergic rhinitis and asthma, in which large numbers<br />

of eosinophils are observed in the tissues and sputum.<br />

In parasitic diseases, IL5 leads to eosinophilia.<br />

interleukin-5 receptor complex<br />

A structure comprised of an α chain and a β chain, both<br />

of which resemble members of the hematopoietin receptor<br />

superfamily. The α chain is a 415-amino acid glycoprotein<br />

and binds with low affinity to IL5. Even though the β chain<br />

does not bind to IL5, it associates with the α chain to form<br />

the high-affinity receptor. The β chain is common to IL3<br />

and granulocyte–macrophage colony-stimulating factor<br />

(GM-CSF) receptors. The IL5 receptor is a member of the<br />

type 1 cytokine receptor family, comprised of a heterodimer<br />

containing an α subunit that binds IL5 and confers<br />

cytokine receptor specificity and a β subunit that contains<br />

the signal transduction domains. Eosinophils, whose principal<br />

function is to eliminate antibody bound parasites from<br />

the body through release of cytotoxic granule proteins, are<br />

the main IL5Rα expressing cells, which permits them to<br />

respond to IL5.<br />

interleukin-6 (IL6)<br />

A 26-kDa cytokine produced by vascular endothelial cells,<br />

mononuclear phagocytes, fibroblasts, activated T lymphocytes,<br />

and various neoplasms such as cardiac myxomas,<br />

bladder cancer, and cervical cancer. A cytokine synthesized<br />

by T cells and macrophages that is proinflammatory and<br />

activates immune responses to trauma, specifically burns<br />

amd other tissue injuries resulting in inflammation. It is<br />

required for murine resistance against Streptococcus pneumoniae.<br />

IL6 is produced by muscle, osteoblasts, and tunica<br />

I

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