HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 276, Issue 33, 31202-31208, August 17, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/33/31202    most recent M102789200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Fukushima, K. Articles by Yamashita, K. Search for Related Content PubMed PubMed Citation Articles by Fukushima, K. Articles by Yamashita, K. Social Bookmarking                      What's this?

Carbohydrate Recognition Site of Interleukin-2 in Relation to Cell Proliferation^*

Keiko Fukushima, Sayuri Hara-Kuge, Hiroko Ideo, and Katsuko Yamashita

From the Department of Biochemistry, Sasaki Institute, 2-2 Kanda-Surugadai, Chiyoda-ku, Tokyo 101-0062 and Core Research for Evolutional Science and Technology (CREST) of the Japan Science and Technology Corporation, 2-5 Kanda-Surugadai, Chiyoda-ku, Tokyo 101-0062, Japan

Interleukin-2 (IL-2) is a cytokine with important roles in the immune system. IL-2 initially binds a high mannose-type glycan and a specific peptide sequence of the IL-2 receptor -subunit and sequentially forms a high affinity complex of IL-2·IL-2 receptor -, -, and -subunits. This formation induces cellular signaling and cell proliferation (Fukushima, K., and Yamashita, K. (2001) J. Biol. Chem. 276, 7351-7356). To determine the carbohydrate-binding site of IL-2, we prepared wild-type and point-mutated ³⁵S-IL-2 by an in vitro transcription and translation method. We found that wild-type ³⁵S-IL-2 tends to form a dimer spontaneously, and the dimeric form has both carbohydrate recognition activity and cell proliferation activity. Moreover, substitution of Asn-26 in IL-2 with Gln or Asp conserved the dimeric form and affected the carbohydrate recognition activities in correspondence with the cell proliferation activities, suggesting that Asn-26 in IL-2 is involved in the carbohydrate recognition site. These results suggest that the carbohydrate recognition of IL-2 dimer triggers formation of high affinity complex (IL-2·IL-2R, -, -)₂, and the hetero-octamer stimulates IL-2-dependent T-cell proliferation by intensifying cellular signaling.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				L. E. Wrenshall, J. L. Platt, E. T. Stevens, T. N. Wight, and J. D. Miller Propagation and Control of T Cell Responses by Heparan Sulfate-Bound IL-2 J. Immunol., June 1, 2003; 170(11): 5470 - 5474. [Abstract] [Full Text] [PDF]