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Originally published In Press as doi:10.1074/jbc.M010095200 on March 14, 2001

J. Biol. Chem., Vol. 276, Issue 23, 20597-20602, June 8, 2001
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Cloning and Characterization of IL-1HY2, a Novel Interleukin-1 Family Member*

Haishan Lin, Alice S. Ho, Dana Haley-Vicente, Jun Zhang, Juanita Bernal-Fussell, Ann M. PaceDagger , Derek Hansen, Kathi Schweighofer, Nancy K. Mize, and John E. Ford§

From the Functional Genomics Department, Hyseq Inc., Sunnyvale, California 94086

The interleukin-1 (IL-1) family members play an important role in the process of inflammation and host defense. We describe here the identification and characterization of a novel member of the IL-1 family, IL-1HY2. The human IL-1HY2 protein shares significant amino acid sequence similarity (37%) with the IL-1 receptor antagonist and has a predicted three-dimensional structure similar to that of the IL-1 receptor antagonist. The IL-1HY2 gene is located in close proximity to other IL-1 family genes on human chromosome 2, and the genomic organization of the IL-1HY2 gene is highly conserved with other IL-1 family members. IL-1HY2 protein is secreted from mammalian cells, and the purified recombinant IL-1HY2 protein binds soluble IL-1 receptor type I. IL-1HY2 is expressed in human skin, spleen, and tonsil. Immunohistochemical analysis showed that the IL-1HY2 protein is expressed in the basal epithelia of skin and in proliferating B cells of the tonsil. These data suggest that IL-1HY2 is a novel IL-1 family member and that it may participate in a network of IL-1 family members to regulate adapted and innate immune responses.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF334755 and AF334756.

Dagger Present address: Center for Biomolecular Science and Engineering, University of California, Santa Cruz, CA 95064.

§ To whom correspondence should be addressed: Functional Genomics Dept., Hyseq Inc., 670 Almanor Ave., Sunnyvale, CA 94086. Tel.: 408-524-8100; Fax: 408-524-8141; E-mail: ford@sbh.com.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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