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Glycobiology Advance Access published online on July 25, 2006
Glycobiology, doi:10.1093/glycob/cwl028
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
Received June 5, 2006
Revised July 19, 2006
Accepted July 23, 2006

Communication

Galectin-8 and galectin-9 are novel substrates for thrombin

Nozomu Nishi 1 *, Aiko Itoh 2, Hiroki Shoji 1, Hiroshi Miyanaka 3, and Takanori Nakamura 1

1 Department of Endocrinology, Faculty of Medicine, Kagawa University, 1750-1 Ikenobe, Miki-cho, Kita-gun, Kagawa 761-0793, Japan
2 GalPharma Co., Ltd., 2217-44 Hayashimachi, Takamatsu, Kagawa 761-0301, Japan
3 Life Science Research Center, Kagawa University, 1750-1 Ikenobe, Miki-cho, Kita-gun, Kagawa 761-0793, Japan

* To whom correspondence should be addressed.
Nozomu Nishi, E-mail: nnishi{at}med.kagawa-u.ac.jp


  Abstract

Galectin-8 and galectin-9, which each consist of two carbohydrate recognition domains joined by a linker peptide, belong to the tandem-repeat-type subclass of the galectin family. Alternative splicing leads to the formation of at least two and three distinct splice variants (isoforms) of galectin-8 and galectin-9, respectively, with tandem-repeat-type structures. The isoforms share identical carbohydrate recognition domains and differ only in the linker region. In a search for differences in biological activity among the isoforms, we found that their isoforms with the longest linker peptide, i.e., galectin-8L and galectin-9L, are highly susceptible to thrombin cleavage. While the predominant isoforms, galectin-8M and galectin-9M, and other members of human galectin family so far examined were resistant to thrombin. Amino acid sequence analysis of proteolytic fragments and site-directed mutagenesis showed that the thrombin cleavage sites (-IAPRT- and -PRPRG- for galectin-8L and galectin-9L, respectively) resided within the linker peptides. Although intact galectin-8L stimulated neutrophil adhesion to substrate more efficiently than galectin-8M, the activity of galectin-8L but not that of galectin-8M decreased on thrombin digestion. Similarly, thrombin treatment almost completely abolished eosinophil chemoattractant activity of galectin-9L. These observations suggest that galectin-8L and galectin-9L play unique roles in relation to coagulation and inflammation.

Keywords: galectin/linker peptide/proteolysis/thrombin.
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