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© The Rockefeller University Press, 0022-1007/1999/9/793/ $5.00
The Journal of Experimental Medicine, Volume 190, Number 6, September 20, 1999 793-802

Original Article

Identification and Molecular Cloning of P75/Airm1, a Novel Member of the Sialoadhesin Family That Functions as an Inhibitory Receptor in Human Natural Killer Cells

Michela Falcoa,b, Roberto Biassonia, Cristina Bottinoa, Massimo Vitalea, Simona Sivorib, Raffaella Augugliarob, Lorenzo Morettaa,b, and Alessandro Morettab

a Istituto Nazionale per la Ricerca sul Cancro, 16132 Genova, Italy
b Dipartimento di Medicina Sperimentale, Università degli Studi di Genova, 16132 Genova, Italy

In this study, by the generation of a specific monoclonal antibody, we identified p75/AIRM1 (for adhesion inhibitory receptor molecule 1), a novel inhibitory receptor that is mostly confined to human natural killer cells. p75/AIRM1 is a 75-kD glycoprotein that, upon sodium pervanadate treatment, becomes tyrosine phosphorylated and associates to src homology 2 domain–bearing protein tyrosine phosphatase (SHP)-1. The p75/AIRM1 gene is located on human chromosome 19 and encodes a novel member of the sialoadhesin family characterized by three immunoglobulin-like extracellular domains (one NH2-terminal V-type and two C2-type) and a classical immunoreceptor tyrosine–based inhibitory motif (ITIM) in the cytoplasmic portion. The highest amino acid sequence similarity has been found with the myeloid-specific CD33 molecule and the placental CD33L1 protein. Similar to other sialoadhesin molecules, p75/AIRM1 appears to mediate sialic acid–dependent ligand recognition.

Key Words: molecular cloning • natural killer cells • sialoadhesin • inhibitory receptor • immunoglobulin superfamily

1used in this paper: aa, amino acid(s); AIRM1, adhesion inhibitory receptor molecule 1; Ig-SF, immunoglobulin superfamily; ILT, Ig-like transcript; ITIM, immunoreceptor tyrosine–based inhibitory motif; KIR, killer inhibitory receptor; LIR, leukocyte Ig-like receptor; MAG, myelin-associated glycoprotein; RT, reverse transcriptase; SH, src homology domain; SHP, SH2 domain–bearing protein tyrosine phosphatase

© 1999 The Rockefeller University Press


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