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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Identification and Characterization of a Novel Human Collectin CL-K1.

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.[1]

References

  1. Identification and Characterization of a Novel Human Collectin CL-K1. Keshi, H., Sakamoto, T., Kawai, T., Ohtani, K., Katoh, T., Jang, S.J., Motomura, W., Yoshizaki, T., Fukuda, M., Koyama, S., Fukuzawa, J., Fukuoh, A., Yoshida, I., Suzuki, Y., Wakamiya, N. Microbiol. Immunol. (2006) [Pubmed]
 
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