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interleukin-2 receptor α subunit (IL2Rα) 401 interleukin-4 (IL4; B cell growth factor)<br />

required for stimulation are effective when both receptors<br />

are present on cell surfaces. Antibodies against p55 or p70<br />

can block IL2 binding. Powerful antigenic stimulation such<br />

as in transplant rejection may lead to the shedding of p55<br />

IL2 receptors into the serum. The gene encoding the p55<br />

chain is located on chromosome 10p14 in humans. IL2, IL1,<br />

IL6, IL4, and TNF may induce IL2R expression.<br />

interleukin-2 receptor subunit (IL2R)<br />

The 55-kDa polypeptide subunit of IL2R with a K d of 10 –8<br />

M. The α subunit is responsible for increasing the affinity<br />

between cytokine and receptor; however, it has no role in<br />

signal transduction. It is expressed only on antigen stimulation<br />

of T cells, usually within 2 hours. Following long-term<br />

T cell activation, the α subunit is shed, making it a potential<br />

candidate as a serum marker of strong or prolonged antigen<br />

stimulation. The gene encoding IL2Rα is located on chromosome<br />

10p14 in humans.<br />

α<br />

1<br />

cys 192<br />

Interleukin-2.<br />

β γ<br />

1<br />

: Cysteine<br />

: Motif<br />

WSXWS<br />

Motif<br />

251 Serine-rich<br />

Region<br />

Acidic<br />

SH2<br />

Homology<br />

Subdomain<br />

Region<br />

347<br />

Schematic representation of interleukin-2 receptor αβγ subunit (IR-2Rαβγ.)<br />

525<br />

interleukin-2 receptor subunit (IL2R)<br />

The complete IL2 receptor consists of two distinct polypeptides:<br />

IL2α, induced upon activation, and IL2βγ, present on<br />

:<br />

:<br />

1<br />

resting T cells. Upon expression of all three proteins, affinity<br />

increases to 10 –11 M and very low (physiologic) levels<br />

of IL2 are capable of stimulating cells. IL2R is found on T<br />

lymphocytes, natural killer (NK) cells, and B lymphocytes,<br />

although NK cells do not express IL2Rα. IL2, IL1, IL6,<br />

IL4, and TNF may induce IL2R expression.<br />

interleukin-2 receptor subunit (IL2R)<br />

The 70- to 74-kDa subunit of IL2R with a K d of 10 –9 M.<br />

The β subunit is a member of the cytokine receptor family<br />

type I due to its tryptophan–serine–X–tryptophan–serine<br />

(WSXWS) domain. It is a constitutive membrane protein<br />

coordinately expressed with IL2Rγ.<br />

interleukin-2 receptor subunit (IL2R)<br />

A heterodimer found on resting T cells. Only T cells expressing<br />

IL2R are capable of growth in response to IL2, as this is<br />

the portion of the receptor responsible for signal transduction.<br />

interleukin-2 receptor subunit (IL2R)<br />

This subunit is also a type I (WSXWS) receptor associated<br />

with IL4 and IL7 receptors as well as IL2Rγ. Mutations in the<br />

γ subunit have been found in some cases of severe combined<br />

immunodefiency syndrome (SCIDS) with X-linked inheritance,<br />

resulting in decreased proliferation of B and T cells.<br />

interleukin-3 (IL3)<br />

A 20-kDa lymphokine synthesized by activated CD4 + T<br />

helper lymphocytes that acts as a colony-stimulating factor<br />

by facilitating proliferation of some hematopoietic cells and<br />

promoting proliferation and differentiation of other lymphocytes.<br />

It acts by binding to high and low affinity receptors,<br />

inducing tyrosine phosphorylation and colony formation<br />

of erythroid, myeloid, megakaryocytic, and lymphoid<br />

hematopoietic cells. It also facilitates mast cell proliferation,<br />

the release of histamine, and T lymphocyte maturation<br />

through induction of 20α-hydroxysteroid dehydrogenase.<br />

The gene encoding IL3 is situated on the long arm of chromosome<br />

5. The IL3 gene in humans encodes a 152-amino<br />

acid long protein, and the naturally occurring form of IL3<br />

is glycosolated. IL3 facilitates natural immune defenses<br />

against disease.<br />

interleukin-3 receptor<br />

A low-affinity IL3-binding α subunit (IL3α; CD123)<br />

that associates with a β subunit to produce a high affinity<br />

IL3 receptor. The IL3α subunit has an N terminal region<br />

consisting of 100-amino acid residues, a cytokine receptor<br />

domain, and a fibronectin III domain containing the<br />

WSXWS motif. The truncated cytoplasmic domain is<br />

associated with the inability to signal. The β subunit has<br />

two homologous segments in the extracellular region. A<br />

cytokine receptor domain followed by a fibronectin domain<br />

is present in each segment. The human α chain contains six<br />

potential N-linked glycosylation sites, whereas the β chain<br />

has three. Tyrosine and serine/threonine phosphorylation of<br />

numerous cellular proteins occurs rapidly following union<br />

of IL3 with its receptor. The β subunit is requisite for signal<br />

transduction.<br />

interleukin-4 (IL4; B cell growth factor)<br />

A 20-kDa cytokine that induces differentiation of naïve<br />

helper T (Th0) cells to Th2 cells, subsets of CD4 + helper T<br />

lymphocytes, that subsequently become the main producers<br />

of the cytokine and may also be synthesized by activated<br />

mast cells. Among its numerous biological functions are<br />

the stimulation of activated B cell and T cell proliferation<br />

and the differentiation of CD4 + T cells into Th2 cells. It is a<br />

I

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