Molecular characterization of receptors for human interleukin-8, GRO/melanoma growth-stimulatory activity and neutrophil activating peptide-2

Cerretti, Douglas Pat; Kozlosky, Carl J.; Bos, Tim Vanden; Nelson, Nicole; Gearing, David P.; Beckmann, M P

doi:10.1016/0161-5890(93)90065-j

Cited by 118 publications

(50 citation statements)

References 40 publications

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“…The present findings are in agreement with previous observations in transiently transfected E293 cells [13]. Two distinct recombinant IL-8 receptors were also expressed in COS cells [14]. In this case, however, GROcc or NAP-2 did not compete for 1251-IL-8 binding to IL-8Rl and bound to IL-8R2 with markedly lower affinity than IL-8, suggesting that COS cells may be less convenient for the study of recombinant IL-8 receptors.…”

Section: Chemokine Binding To Jurkat Transfectantssupporting

confidence: 83%

Both interleukin‐8 receptors independently mediate chemotaxis

et al. 1994

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Neutrophil leukocytes, the target cells for interleukin-8 and related CXC chemokines, bear high numbers of two types of IL-8 receptors (IL-8Rl and IL-8R2). By cDNA transfection Jurkat cell lines were generated that stably express either IL-8Rl or IL-8R2 (J-IL8Rl and J-IL8R2). J-IL8Rl expressed 4,000 + 1,000 copies of IL-8R1, and bound IL-8 with high affinity (Kd l-4 nM) and GROcl and NAP-2 with low affinity (Kd 200-500 nM). J-IL8R2 expressed 17,000 f 3,000 copies of IL-8R2, and bound all three chemokines with high affinity. Both transfectants showed a similar degree of chemotactic migration after stimulation with IL-8, GROa and NAP-2. All three chemokines were equally potent as attractants of J-IL8R2, whereas IL-8 was 300 to l,OOO-fold more potent than GROcl or NAP-2 as attractant of J-IL8Rl. The potencies, therefore, agree with the affinities of the ligands to IL-8Rl and IL-8R2. Our results demonstrate that both IL-8 receptors function independently, and mediate chemotaxis in response to IL-8 and other CXC chemokines.

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Section: Chemokine Binding To Jurkat Transfectantssupporting

confidence: 83%

Both interleukin‐8 receptors independently mediate chemotaxis

et al. 1994

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“…Stimulation of these neutrophil functions is mediated by the interaction of IL-8 with two membrane receptors, CXCR1 and CXCR2 [11]. Although IL-8 binds with high affinity to both CXCR1 and CXCR2, only CXCR2 binds other members of the CXC chemokine family (e.g., MGSA/GRO␣, ENA-78, and NAP-2) with high affinity [12]. Both IL-8 receptors are members of the seven-transmembrane-spanning, G-protein-coupled receptor family that, following binding of chemokines, become desensitized resulting in the loss of receptor function [13].…”

Section: Introductionmentioning

confidence: 99%

Heterologous desensitization of IL-8-mediated chemotaxis in human neutrophils by a cell-binding fragment of fibronectin

Stanton

Frewin

Gudewicz

1999

Journal of Leukocyte Biology

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“…Molecularly, CXCL8 binds to the seven-transmembrane G-protein coupled receptors, CXC chemokine receptor (CXCR) 1 and CXCR2 (or CXCL8R2), with different expression and affinity to different chemokines (Cerretti et al 1993). For example, CXCL6 (granulocyte chemoattractant protein-2; GCP-2) and CXCL8 can bind to CXCR1 with high affinity, while all of the Glu-Leu-Arg (ELR)-CXC chemokines can bind to CXCR2 with lower affinity (Holmes et al 1991;Murphy and Tiffany 1991).…”

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confidence: 99%