Annual Review of Immunology Volume 16 1998 by Annual Reviews

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Extra resources for Annual Review of Immunology Volume 16 1998

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However, the cloned cDNA coded for a protein of 177 amino acids, prompting these authors to conclude that the signal peptide for sIL-1Ra in the rabbit was larger than in other studied species. However, the amino terminal sequence for this purified rabbit IL-1Ra protein was MQAFRI, corresponding to the hypothesized amino terminal sequence for the smaller molecular weight species of icIL-1Ra found in human neutrophils (12). Subsequent genomic and cDNA cloning of rabbit IL-1Ra indicated the presence of two species corresponding to 17-kDa sIL-1Ra and 18-kDa icIL-1Ra in the human (58).

The mechanism of IL1RN∗ 2 association with diseases remains unknown. icIL-1Ra mRNA levels were not altered in keratinocytes from individuals possessing different intron 2 alleles, although protein production was not measured in these studies (31). It was hypothesized that IL1RN∗ 2 is a marker for a linked disease-associated locus and may not be a direct diseaseassociated allele. Crystal Structure and Mechanism of Action The results of studies published through 1992 on the structures of IL-1 and IL-1Ra are summarized in a previous review (5) and include the possible mechanism whereby IL-1Ra binds to IL-1 receptors with avidity nearly equal to the two agonists, yet which fails to activate cells.

Subsequent studies demonstrated the presence of one inhibitory LPS response element (LRE) within the proximal 294 bp of the sIL-1Ra promoter between bases −250 and −200 (16). In addition, three positive-acting elements for LPS-induced responses were also present, between bases −250 and −200 (LRE3), −200 and −148 (LRE2), and −148 and −31 (LRE1). LRE1 was further identified as an NF-κB binding site located at bases −93 to −84 overlapping with a C/EBP site. The three positive elements in the proximal sIL-1Ra promoter exhibited cooperativity in mediating responses to LPS.

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