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Identification and characterization of a novel human collectin CL-K1.

Hiroyuki H Keshi, Takashi T Sakamoto, Takao T Kawai, Katsuki K Ohtani, Tsuyoshi T Katoh, Seong-Jae SJ Jang, Wataru W Motomura, Takayuki T Yoshizaki, Mitsuko M Fukuda, Satoshi S Koyama, Jun J Fukuzawa, Atsushi A Fukuoh, Itsuro I Yoshida, Yasuhiko Y Suzuki, and Nobutaka N Wakamiya

Microbiol Immunol 50(12):1001-13 (2006) PMID 17179669

Collectins are a family of C-type lectins with two characteristic structures, collagen like domains and carbohydrate recognition domains. They recognize carbohydrate antigens on microorganisms and act as host-defense. Here we report the cloning and characterization of a novel collectin CL-K1. RT-PCR analyses showed CL-K1 mRNA is present in all organs. The deduced amino acid sequence and the data from immunostaining of CL-K1 cDNA expressing CHO cells revealed that CL-K1 is expressed as a secreted protein. CL-K1 is found in blood by immunoblotting and partial amino acid analyses. CL-K1 showed Ca(2+)-dependent sugar binding activity of fucose and weakly mannose but not N-acetyl-galactosamine, N-acetyl-glucosamine, or maltose, though mannose-binding lectin (MBL) containing similar amino acid motif. CL-K1 can recognize specially several bacterial saccharides due to specific sugar-binding character. Elucidation of the role of two ancestor collectins of CL-K1 and CL-L1 could lead to see the biological function of collectin family.

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