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Characterization of a Novel Receptor That Maps Near the Natural Killer Gene Complex: Demonstration of Carbohydrate Binding and Expression in Hematopoietic Cells¹

Thomas Jefferson University, Department of Microbiology and Immunology, Kimmel Cancer Institute, Philadelphia, Pennsylvania 19107 [M. J. F., A. A. F., L. D. S., C. B., B. C.], and The Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, Toronto, M4X 1K9 Canada [N. N. I.]

A novel type II integral membrane protein has been identified in the course of screening for genes overexpressed in a mouse model of chronic myelogenous leukemia blast crisis. This new protein, designated NKCL, consists of a 210-amino acid polypeptide with a short, NH₂-terminal cytoplasmic tail of 17 amino acids preceding a transmembrane domain and a COOH-terminal extracellular region. The COOH-terminal 132 amino acids bear typical features of the C-type animal lectin carbohydrate-recognition domain. The Nkcl gene is unique in that it maps just proximal to the region of the genome that encodes group V members of the C-type animal lectin family near the natural killer gene complex on mouse chromosome 6, but its protein product also has features of several group II C-type animal lectins. Most notably, it has a complete Ca²⁺-binding site 2, which forms part of the sugar-binding site in other members of the family, and binds mannose in a Ca²⁺-dependent manner. Moreover, its expression is not restricted to natural killer cells, as reported for the majority of group V lectins. Nkcl is expressed in pluripotent myeloid precursors, precursor and mature macrophages, and neutrophils.

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