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Cytokine. 1997 Jan;9(1):1-8.

Molecular characterization of the bovine type II IL-1 receptor.

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Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin-Madison 53706, USA.


The purpose of this study was to clone and characterize the bovine IL-1rII. Using a human IL-1rII probe, three putative exons of the bovine IL-1rII were identified from a bovine genomic library. The full length cDNA for bovine IL-1rII was cloned from a bovine endometrial cDNA library using oligonucleotides designed from those exons. The nucleotide sequence of the bovine IL-1rII cDNA has 79, 69 and 69% identity with those of human, mouse, and rat IL-1rII, respectively. The bovine IL-1rII cDNA contains an open reading frame encoding 400 amino acids with a predicted amino acid sequence of 71, 58, and 59% identity with those of human, mouse and rat IL-1rII, respectively. Transient transfection of COS cells with the cloned bovine IL-1rII cDNA resulted in specific binding of bovine IL-1 beta, with a Kd of 1.82 x 10(-10) M. At least two transcripts of bovine IL-1rII were identified from bovine peripheral blood mononuclear cells (PBMCs), liver, and fetal thymocytes by Northern blot analysis. The relative proportion of these transcripts varied with cell type. In addition, bovine IL-1rII transcripts were detected by RT-PCR in stimulated and unstimulated neutrophils, fibroblasts, and splenocytes. The results of this study provide the first characterization of bovine IL-1rII at a molecular level.

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