A cyclophilin-related protein involved in the function of natural killer cells

Proc Natl Acad Sci U S A. 1993 Jan 15;90(2):542-6. doi: 10.1073/pnas.90.2.542.

S K Anderson ¹, S Gallinger, J Roder, J Frey, H A Young, J R Ortaldo

Affiliations

Affiliation

1 Division of Molecular Immunology and Neurobiology, Mount Sinai Hospital Research Institute, Toronto, Ontario, Canada.

PMID: 8421688 DOI: 10.1073/pnas.90.2.542

Abstract

Natural killer cells are non-major histocompatibility complex-restricted large granular lymphocytes that can recognize and destroy tumor cells without prior stimulation. A 150-kDa molecule on the surface of human natural killer cells was identified as a component of a putative tumor-recognition complex. We report here the isolation of cDNAs coding for the 150-kDa tumor-recognition molecule from human and mouse cDNA libraries. The amino terminus of the predicted protein contains a large hydrophobic region followed by a domain that is highly homologous to Cyclophilin/peptidylprolyl cis-trans isomerase. The remainder of the protein is extremely hydrophilic and contains three homologous positively charged clusters. There are also three regions that contain extensive arginine- and serine-rich repeats. Comparison of the human and mouse predicted amino acid sequences revealed > 80% homology.

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