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J. Biol. Chem., Vol. 276, Issue 20, 17497-17506, May 18, 2001

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A Macrophage Protein, Ym1, Transiently Expressed during Inflammation Is a Novel Mammalian Lectin^*

Nan-Chi A. Chang^§¶, Shuen-Iu Hung, Kuo-Yuan Hwa, Ikunoshin Kato^**, Ju-Eng Chen, Cheng-Hsiun Liu, and Alice Chien Chang^§

From the  Institute of Microbiology and Immunology,  Institute of Neuroscience, and ^§ Center for Neuroscience, School of Life Science, National Yang-Ming University, Taipei, Taiwan 112, Republic of China, the  Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan 115, Republic of China, and ^** Biomedical Group, Takara Shuzo Co., Ltd., Otsu, Shiga 520-21, Japan

Oral infections of mice with Trichinella spiralis induce activation of peritoneal exudate cells to transiently express and secrete a crystallizable protein Ym1. Purification of Ym1 to homogeneity was achieved. It is a single chain polypeptide (45 kDa) with a strong tendency to crystallize at its isoelectric point (pI 5.7). Co-expression of Ym1 with Mac-1 and scavenger receptor pinpoints macrophages as its main producer. Protein microsequencing data provide information required for full-length cDNA cloning from libraries constructed from activated peritoneal exudate cells. A single open reading frame of 398 amino acids with a leader peptide (21 residues) typical of secretory protein was deduced and later deposited in GenBank^TM (accession number M94584) in 1992. By means of surface plasmon resonance analyses, Ym1 has been shown to exhibit binding specificity to saccharides with a free amine group, such as GlcN, GalN, or GlcN polymers, but it failed to bind to other saccharides. The interaction is pH-dependent but Ca²⁺ and Mg²⁺ ion-independent. The binding avidity of Ym1 to GlcN oligosaccharides was enhanced by more than 1000-fold due to the clustering effect. Specific binding of Ym1 to heparin suggests that heparin/heparan sulfate may be its physiological ligand in vivo during inflammation and/or tissue remodeling. Although it shares ~30% homology with microbial chitinases, no chitinase activity was found associated with Ym1. Genomic Southern blot analyses suggest that Ym1 may represent a member of a novel lectin gene family.

This paper is dedicated to Dr. William Zimmermann, a memorable mentor to N. C. Chang, for support and encouragement during the initial pursuit of this work.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) M94584.

The amino acid sequence of this protein can be accessed through NCBI Protein Database under NCBI accession number AAB62394.

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