Molecular cloning of a cDNA encoding the human interleukin 4 receptor

Galizzl, Jean-Pierre; Zuber, Caroline E.; Harada, Nobuyuki; Gorman, Daniel M.; Djossou, Odile; Kastelein, Robert A.; Banchereau, Jacques; Howard, Maureen; Miyajima, Atsushi

doi:10.1093/intimm/2.7.669

Cited by 109 publications

(54 citation statements)

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“…Amino acid sequence analysis of the purified IL4-BP established the N-terminal sequence GNMKLQ. Thus, the mature protein starts two residues earlier than originally proposed (Idzerda et al, 1990;Galizzi et al, 1990).…”

Section: Cho Cellsmentioning

confidence: 77%

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Global and Local Determinants for the Kinetics of Interleukin‐4/Interleukin‐4 Receptor α Chain Interaction

Shen

Hage

Sebald

1996

European Journal of Biochemistry

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An engineered interleukin-4-binding protein (IL4-BP) representing the extracellular domain of the human interleukin-4 (IL-4) receptor a chain was expressed in Sf9 cells. The purified IL4-BP was immobilized via a single biotinylated SH group near the carboxyl end to a biosensor matrix and analysed in real time for interaction with IL-4 and IL-4 variants. IL-4 was bound to IL4-BP at a molar ratio of approximately 1 : l . The association and dissociation at pH 7.4 and 150 mM NaCl had rate constants of 1.9 2 0.3 X 10' M-' s-I and 2 ? 1 X lo-' s-', respectively. Glycosylation and engineered amino acid substitutions of IL4-BP did not alter the kinetic constants as shown by a parallel analysis of IL4-BP variants produced in Eschevichia coli or Chinese hamster ovary cells. The rate of association was only slighly affected in binding-deficient variants [E9Q]IL-4 and [R88Q]IL-4 and by acidic pH down to values of 4.5, but it was reduced up to fivefold at higher ionic strength. The rate of dissociation was increased 70-fold and 150-fold with the 1L-4 variants and fivefold at an acidic pH of 4.5, but it was not affected by high ionic strength. Temperatures between 6°C and 37°C yielded similar rates of IL-4 dissociation and only a marginally reduced rate of IL-4 association at 6°C.These results indicate that the high-affinity binding of IL-4 to its receptor (Kd=lOO pM) is mainly the result of an unusually high association rate. The IL-4/IL4-BP interaction appears to be dominated by charge effects. The exceedingly high rate of IL-4IIU-BP association is augmented by the overall electrostatic potentials of both proteins (electrostatic steering). Localized charges and the formation of ion pairs may control the rate of complex dissociation.

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Section: Cho Cellsmentioning

confidence: 77%

“…Amino acid residues in all IL4-BP variants are numbered as in the original cloning papers (Idzerda et al, 1990;Galizzi et al, 1990).…”

Section: Methodsmentioning

confidence: 99%

Global and Local Determinants for the Kinetics of Interleukin‐4/Interleukin‐4 Receptor α Chain Interaction

Shen

Hage

Sebald

1996

European Journal of Biochemistry

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“…At present, only one IL-4 receptor molecule is fully charact.erized, comprising a. single polypeptide chain of ~ 800 amino acid residues (Mosley et al, 1989;Galizzi et al, 1990;Harada et al, 1990;Idzerda et al, 1990). It occurs at the relatively low flgure of 150 to 2500 molecules per target cell (CabriJlat et al, 1987;Park et al, 1987).…”

mentioning

confidence: 99%

Aspects of Receptor Binding and Signalling of Interleukin-4 Investigated by Site-directed Mutagenesis and NMR Spectroscopy

Müller

Dieckmann

Sebald

et al. 1994

Journal of Molecular Biology

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Cytokines are hormones that carry information from ceJI to ceH. This information is read from their surface upon binding to transmembrane receptors and by the subsequent initiation of receptor oligomerization. An inftuence on this process through mutagenesis on the hormone surface is highly desirab)e for medical reasons.However, an understanding of hormone-receptor interactions requires insight into the structural changes introduced by the mutations. In this line structural studies on human TL-4 and the medically important IL-4 antagonists YI24D and Y124G are presented. The site a.round YI24 is an important epitope responsible for the a.bility of 11-4 t.o ca.use a signal in the target cells. It is shown that the local main-chain structure around residue 124 in the variants remains unchanged. A strategy is presented here which allows the study of these types of proteins and their variants by NMR which does not require carbon Iabeiied sa.mples.

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“…Human and mouse IL-4 receptors show a broad distribution on hematopoietic and non-hematopoietic cells , Lowenthal, et al, 1988, generally expressed at low levels (20-4000 receptors per cell).The IL-4R cDNAwas cloned from the mouse cytotoxic T-lymphocytic (CTLL-2) cell line (Mosley, et al, 1989) and from the human myeloid cell line, TF-1 (Galizzi, et al, 1990). Sequence analysis demonstrated that the IL-4R belongs to the hematopoeitin receptor superfamily.…”

Section: Il-4rmentioning

confidence: 99%

The Type I and Type II Receptor Complexes for IL-4 and IL-13 Differentially Regulate Allergic Lung Inflammation

Heller¹,

Dasgupta²,

Dorsey³

et al. 2012

Allergic Diseases - Highlights in the Clinic, Mechanisms and Treatment

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Molecular cloning of a cDNA encoding the human interleukin 4 receptor

Cited by 109 publications

References 0 publications

Global and Local Determinants for the Kinetics of Interleukin‐4/Interleukin‐4 Receptor α Chain Interaction

Global and Local Determinants for the Kinetics of Interleukin‐4/Interleukin‐4 Receptor α Chain Interaction

Aspects of Receptor Binding and Signalling of Interleukin-4 Investigated by Site-directed Mutagenesis and NMR Spectroscopy

The Type I and Type II Receptor Complexes for IL-4 and IL-13 Differentially Regulate Allergic Lung Inflammation

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