The cell surface receptors for interleukin-1α and interleukin-1β are identical

Dower, Steven K.; Kronheim, С.; Hopp, Thomas P.; Cantrell, Michael A.; Deeley, M C; Gillis, Steven; Henney, Christopher S.; Urdal, David L.

doi:10.1038/324266a0

Cited by 406 publications

(142 citation statements)

References 21 publications

Supporting

Mentioning

133

Contrasting

Unclassified

Order By: Relevance

“…Dower et al [13] have shown that IL-l receptor(s) distributed on T and B lymphocytes, fibroblasts, and epithelial cells, and have suggested that the apparently diverse biological activities of IL-l are presumably mediated by its specific cell surface receptor(s). Although we have not yet determined whether the IL-l receptor(s) is present on osteoblastic MC3T3-El cells, it is a very attractive proposal that some of the effects of IL-l on DNA synthesis, cell growth, and/or alkaline phosphatase activity in MC3T3-El may result from interaction between IL-l and its receptor on the cells.…”

Section: Resultsmentioning

confidence: 99%

Human purified interleukin‐1 inhibits DNA synthesis and cell growth of osteoblastic cell line (MC3T3‐E1), but enhances alkaline phosphatase activity in the cells

Hanazawa¹,

Ohmori²,

Amano³

et al. 1986

FEBS Letters

View full text Add to dashboard Cite

We examined the effects of human purified interleukin-1 (IL-l) on DNA synthesis, cell growth, and alkaline phosphatase activity in the osteoblastic cell line MC3T3-El under both preconfluent and confluent culture conditions. Addition of IL-l to the cells markedly inhibited their DNA synthesis and growth over the range l-10 U/ml. Such significant inhibitory effects were observed in cells cultivated in 1 or 5% fetal calf serum (FCS)-containing alpha modification Eagle's medium (alpha-MEM), but not in alpha-MEM containing 10% FCS. In contrast, alkaline phosphatase activity was enhanced significantly by IL-l in the cell line cultivated in 1% FCS-containing alpha-MEM. These results demonstrate that human purified IL-l is effective in inducing the differentiation of osteoblastic cell MC3T3-E 1.

show abstract

Section: Resultsmentioning

confidence: 99%

Human purified interleukin‐1 inhibits DNA synthesis and cell growth of osteoblastic cell line (MC3T3‐E1), but enhances alkaline phosphatase activity in the cells

Hanazawa¹,

Ohmori²,

Amano³

et al. 1986

FEBS Letters

View full text Add to dashboard Cite

show abstract

“…For dissociation kinetics, cells were incubated in 150 l of binding medium containing 125 I-sCD4-OX40L (4.6 nM) for 2 h. The cells were then pelleted and resuspended in 1.2 ml of binding medium with or without unlabeled sCD4-OX40L (350 nM). Samples (180 l) were removed at various times, and cell-bound radioactivity was determined as described (28). The values given for the dissociation and association rates are the mean of two independent experiments.…”

Section: Preparation Of Constructs For Expression Of Soluble Forms Ofmentioning

confidence: 99%

Affinity and Kinetics of the Interaction between Soluble Trimeric OX40 Ligand, a Member of the Tumor Necrosis Factor Superfamily, and Its Receptor OX40 on Activated T Cells

Al‐Shamkhani

Mallett

Brown

et al. 1997

Journal of Biological Chemistry

View full text Add to dashboard Cite

OX40 ligand (OX40L) and OX40 are members of the tumor necrosis factor and tumor necrosis factor receptor superfamilies, respectively. OX40L is expressed on activated B and T cells and endothelial cell lines, whereas OX40 is expressed on activated T cells. A construct for mouse OX40L was expressed as a soluble protein with domains 3 and 4 of rat CD4 as a tag (sCD4-OX40L). It formed a homotrimer as assessed by chemical cross-linking and gel filtration chromatography. Radiolabeled sCD4-OX40L bound to activated mouse T cells with a high affinity (K D ‫؍‬ 0.2-0.4 nM) and dissociated slowly (k off ‫؍‬ 4 ؋ 10 ؊5 s ؊1 ). The affinity and kinetics of the OX40L/OX40 interactions were studied using the BIAcore™ biosensor, which measures macromolecular interactions in real time. The extracellular part of the OX40 antigen was expressed as a soluble monomeric protein and immobilized on the BIAcore sensor chip. sCD4-OX40L bound the OX40 with a high affinity (K D ‫؍‬ 3.8 nM), although this was lower than that determined on the surface of activated T cells (K D ‫؍‬ 0.2-0.4 nM), where there is likely to be less restriction in mobility of the receptor. In the reverse orientation, sOX40 bound to immobilized sCD4-OX40L with a stoichiometry of 3.1 receptors to one ligand, with low affinity (K D ‫؍‬ 190 nM) and had a relatively fast dissociation rate constant (k off ‫؍‬ 2 ؋ 10 ؊2 s ؊1 ). Thus if the OX40 receptor is cleaved by proteolysis, it will release any bound ligand and is unlikely to block re-binding of ligand to cell surface OX40 because of the low monomeric affinity.

show abstract

“…Two cell surface receptors for IL-1 have been defined (7)(8)(9), designated IL-1RI and ILlP, II. Mature IL-la and IL-lJ3 bind similarly to these two defined receptors (10) and, consequently, demonstrate the same activities in a broad range of in vitro and in vivo biological systems.…”

mentioning

confidence: 99%

Mice deficient in IL-1beta manifest impaired contact hypersensitivity to trinitrochlorobenzone.

Shornick

Togni

Mariathasan

et al. 1996

The Journal of Experimental Medicine

227

133

View full text Add to dashboard Cite

SummaryMice rendered deficient in IL-1[3 by gene targeting in embryonic stem cells develop and grow normally in a protected laboratory environment. Endotoxin-stimulated peritoneal macrophages from IL-l~-deficient mice showed normal synthesis and cellular release of IL-lct after treatment with 5 mM ATP demonstrating that IL-113 is not necessary for expression and release of the IL-lot isoform. Mice deficient in IL-I~ showed unaltered sensitivity to endotoxic shock, with or without pretreatment with D-galactosamine. In contrast, IL-lJ3-deficient mice showed defective contact hypersensitivity responses to topically applied trinitrochlorobenzene (TNCB). This defect could be overcome either by application of very high doses of sensitizing antigen, or by local intradermal injection of recombinant IL-1[3 immediately before antigen application. These data demonstrate an essential role for IL-1[3 in contact hypersensitivity and suggest that IL-1{3 acts early during the sensitization phase of the response. They suggest an important role for 1I.-1(3 in initiation of the host response at the epidermal barrier.

show abstract

The cell surface receptors for interleukin-1α and interleukin-1β are identical

Cited by 406 publications

References 21 publications

Human purified interleukin‐1 inhibits DNA synthesis and cell growth of osteoblastic cell line (MC3T3‐E1), but enhances alkaline phosphatase activity in the cells

Human purified interleukin‐1 inhibits DNA synthesis and cell growth of osteoblastic cell line (MC3T3‐E1), but enhances alkaline phosphatase activity in the cells

Affinity and Kinetics of the Interaction between Soluble Trimeric OX40 Ligand, a Member of the Tumor Necrosis Factor Superfamily, and Its Receptor OX40 on Activated T Cells

Mice deficient in IL-1beta manifest impaired contact hypersensitivity to trinitrochlorobenzone.

Contact Info

Product

Resources

About