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J. Biol. Chem., Vol. 279, Issue 50, 51775-51782, December 10, 2004

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Human P-selectin Glycoprotein Ligand-1 (PSGL-1) Interacts with the Skin-associated Chemokine CCL27 via Sulfated Tyrosines at the PSGL-1 Amino Terminus^*

Takako Hirata¶, Yuko Furukawa, Bo-Gie Yang, Kunio Hieshima||, Minoru Fukuda**, Reiji Kannagi, Osamu Yoshie||, and Masayuki Miyasaka

From the Laboratory of Molecular and Cellular Recognition, Osaka University Graduate School of Medicine, Suita, Osaka 565-0871, Japan, the Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan, the ^||Department of Microbiology, Kinki University School of Medicine, Osaka-Sayama, Osaka 589-8511, Japan, the ^**Glycobiology Program, Cancer Research Center, The Burnham Institute, La Jolla, California 92037, and the Program of Molecular Pathology, Aichi Cancer Center Research Institute, Nagoya, Aichi 464-8681, Japan

P-selectin glycoprotein ligand-1 (PSGL-1), a sialomucin expressed on leukocytes, is a major ligand for P-selectin and mediates leukocyte rolling on the endothelium. Here we show that human PSGL-1 interacts with CCL27 (CTACK/ILC/ESkine), a skin-associated chemokine that attracts skin-homing T lymphocytes. A recombinant soluble form of PSGL-1 (rPSGL-Ig) preferentially bound CCL27 among several chemokines tested. This interaction was abrogated by arylsulfatase treatment of rPSGL-Ig, suggesting that sulfated tyrosines play a critical role. In contrast, removal of either N-glycans or O-glycans by glycosidase treatment of rPSGL-Ig did not affect the interaction. The binding of CCL27 to a recombinant PSGL-1 synthesized in the presence of a sulfation inhibitor was lower than that produced in normal medium. Moreover, mutation of the tyrosines at the amino terminus of PSGL-1 to phenylalanine abolished the binding, further supporting the role of sulfated tyrosines in the CCL27-PSGL-1 interaction. Functionally, rPSGL-Ig reduced the chemotaxis of L1.2 cells expressing CCR10, the receptor for CCL27. In addition, the expression of human PSGL-1 on CCR10-expressing L1.2 cells resulted in reduced chemotaxis to CCL27. These findings suggest a role for PSGL-1 in regulating chemokine-mediated responses, in addition to its role as a selectin ligand.

Received for publication, August 27, 2004 , and in revised form, October 5, 2004.

^* This work was supported by a Grant-in-aid for Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology, Japan, a Grant-in-Aid for the 21st Century Center of Excellence Program from the Ministry of Education, Culture, Sports, Science and Technology, Japan, and in part by National Institutes of Health Grant CA71932. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed: Laboratory of Molecular and Cellular Recognition, Osaka University Graduate School of Medicine C8, 2-2 Yamada-oka, Suita, Osaka 565-0871, Japan. Tel.: 81-6-6879-3974; Fax: 81-6-6879-3979; E-mail: thirata{at}orgctl.med.osaka-u.ac.jp.

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