cDNA Expression Cloning of the IL-1 Receptor, a Member of the Immunoglobulin Superfamily

Sims, John E.; March, Carl J.; Cosman, David; Widmer, Michael B.; MacDonald, H. Robson; McMahan, Catherine J.; Grubin, Catherine E.; Wignall, J; Jackson, J L; Call, S M

doi:10.1126/science.2969618

Cited by 854 publications

(333 citation statements)

References 38 publications

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“…EL-4 6.1 Cl0 express type I IL-l receptor that is structurally different from the type II IL-1 receptor expressed on 7OZ/3 cells [26,27]. Neither type I nor type II IL-1 receptor is a tyrosine kinase [26,27], but as in the case of the IL-2 receptor ut the surface immunoglobulin our study shows that IL-1 receptors can nonetheless stimulate protein tyrosine kinase activity. It remains to be determined whether or not the same protein tyrosine kinase(s) are activated by IL-la in 7CW3 and EL4 6.1 Cl0 cells.…”

Section: Resultsmentioning

confidence: 53%

“…Some receptors, like the insulin, PDGF or EGF receptors are tyrosine kinases, while others like the IL-2 receptor or the surface immunoglobulin increase tyrosine phosphorylation even though they are not tyrosine kinases [24,25]. EL-4 6.1 Cl0 express type I IL-l receptor that is structurally different from the type II IL-1 receptor expressed on 7OZ/3 cells [26,27]. Neither type I nor type II IL-1 receptor is a tyrosine kinase [26,27], but as in the case of the IL-2 receptor ut the surface immunoglobulin our study shows that IL-1 receptors can nonetheless stimulate protein tyrosine kinase activity.…”

Section: Resultsmentioning

confidence: 99%

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Herbimycin A blocks IL‐1‐induced NF‐κB DNA‐binding activity in lymphoid cell lines

Iwasaki

Uehara²,

Graves

et al. 1992

FEBS Letters

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The mechanism by which interlcukin-lor (IL-lo) activates NF-~13 DNA-binding activity is not completely understood. While it is well established Lhat protein kinase C can activate NF-~13, neither protein kinase C nor protein kinase A appears to be critical in the induction of NF-h-B by IL-la. Since a number of growth factors signal via protein tyrosine kinusc, in this study WC examined a possible involvement of protein tyrosine kinase in the IL-la-induced NF--KB. The results showed that in the murine pre-B cell line 7Oi?/3 and in the murine T cell line EL-4 6.1 ClO.iL-1 a-induced NF-xB was associated with transient increase in protein tyrosine kinasc activity. Pre-treatment of these cell lines with herbimycin A, an inhibitor of tyrosine kinase activity. blocked the IL-la-enhanced protein tyrosine kinasc activity and the IL-la-induced NF-KB DNA-binding activity. Herbimycin A at concentrations sufficient to block IL-la-induced NF-KB did not block the phorbol l2-myristate 13-ncetare(PMA)-induced NF-KB.The data suggest that IL-la and PMA activate NF-XB by different pathways and that induction of NF-KB DNA-binding activity by IL-1 might be dependent on protein tyrosine phosphotylation.

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Section: Resultsmentioning

confidence: 53%

Section: Resultsmentioning

confidence: 99%

Herbimycin A blocks IL‐1‐induced NF‐κB DNA‐binding activity in lymphoid cell lines

Iwasaki

Uehara²,

Graves

et al. 1992

FEBS Letters

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“…5 The two forms of IL-1, IL-1␣ and IL-1␤, together with the structurally related antagonist (IL-1ra) are all distinct gene products, but bind to a common receptor composed of two type I integral membrane proteins (IL1RI and IL1RacP). 6,7 The interleukin 1 type 1 receptor (IL1-RI) (MIM 147810) is the signal-transducing receptor for IL-1. 8 The receptor is found on most cells, including T lymphocytes and beta cells.…”

Section: Introductionmentioning

confidence: 99%

Characterization of new polymorphisms in the 5′UTR of the human interleukin-1 receptor type 1 (IL1R1) gene: linkage to type 1 diabetes and correlation to IL-1RI plasma level

et al. 2000

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The human interleukin-1 type I receptor (IL-1RI) is the signal transducing receptor for IL-1, a principal proinflammatory cytokine, which is cytotoxic to pancreatic islet beta cells. The IL-1RI gene, IL1R1, maps to chromosome 2q12. We have previously examined part of the IL1R1 promoter region and in the present study we further characterized the promoter region demarcating exon 1B and 1C by sequencing and mutation scanning. New sequence was obtained 1762 bp upstream and 1609 bp downstream the known region. Within this sequence, we identified four frequent single nucleotide polymorphisms (SNPs). PCR-based RFLP assays were established and three of the polymorphisms were typed in a Danish Type 1 (insulin-dependent) diabetes mellitus (T1DM) family collection comprising 103 simplex and 150 sib-pair affected families. Linkage was evaluated by the sib-TDT (transmission disequilibrium test). One of the polymorphisms, defined by a HinfI RFLP assay, demonstrated linkage to T1DM, P(sTDT) = 0.026. Random transmission was observed to unaffected offspring from heterozygous parents, P = 0.87. No evidence for positive linkage was seen for the other tested polymorphisms, P = 0.14 and P = 0.21, respectively. To evaluate the possible functional significance of the HinfI polymorphism, we measured circulating IL-1RI plasma level in 30 T1DM patients and in 30 control subjects -10 with each genotype in both groups. Significant differences in plasma levels in relation to genotype -independent of disease status -were found (P = 0.04). In both diabetic and non-diabetic subjects, the wt/wt genotype correlated with the highest IL-1RI plasma level, whereas the plasma levels were lowest for the mt/mt genotype. Genes and Immunity (2000) 1, 495-500.

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“…Although they are only poorly homologous in their primary sequences, the two IL-1 isoforms have been reported to bind a common class of receptors on a variety of cell types including T and B cells [2] and fibroblasts [3]. The sequence of a cDNA encoding an 80 kDa polypeptide responsible for the binding of IL-1 on routine EL4-6.1 thymoma has been recently reported [4]. In the same study, COS cells expressing this recombinant IL-1R polypeptide have been shown to bind IL-lo< and IL-IB with markedly different affinities [4].…”

Section: Introductionmentioning

confidence: 99%

Differential binding of IL‐ 1α and IL‐ 1β to receptors on B and T cells

Scapigliati¹,

Ghiara²,

Bartalini³

et al. 1989

FEBS Letters

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cDNA Expression Cloning of the IL-1 Receptor, a Member of the Immunoglobulin Superfamily

Cited by 854 publications

References 38 publications

Herbimycin A blocks IL‐1‐induced NF‐κB DNA‐binding activity in lymphoid cell lines

Herbimycin A blocks IL‐1‐induced NF‐κB DNA‐binding activity in lymphoid cell lines

Characterization of new polymorphisms in the 5′UTR of the human interleukin-1 receptor type 1 (IL1R1) gene: linkage to type 1 diabetes and correlation to IL-1RI plasma level

Differential binding of IL‐ 1α and IL‐ 1β to receptors on B and T cells

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