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Originally published In Press as doi:10.1074/jbc.M011650200 on January 29, 2001

J. Biol. Chem., Vol. 276, Issue 17, 14451-14458, April 27, 2001
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Molecular Cloning of MIS, a Myeloid Inhibitory Siglec, That Binds Protein-tyrosine Phosphatases SHP-1 and SHP-2*

Tatiana UlyanovaDagger , Dulari D. Shah, and Matthew L. Thomas§

From the § Howard Hughes Medical Institute, Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, Missouri 63110

We describe the molecular cloning and characterization of a novel myeloid inhibitory siglec, MIS, that belongs to the family of sialic acid-binding immunoglobulin-like lectins. A full-length MIS cDNA was obtained from murine bone marrow cells. MIS is predicted to contain an extracellular region comprising three immunoglobulin-like domains (V-set amino-terminal domain followed by two C-set domains), a transmembrane domain and a cytoplasmic tail with two immunoreceptor tyrosine-based inhibitory motif (ITIM)-like sequences. The closest relative of MIS in the siglec family is human siglec 8. Extracellular regions of these two siglecs share 47% identity at the amino acid level. Southern blot analysis suggests the presence of one MIS gene. MIS is expressed in the spleen, liver, heart, kidney, lung and testis tissues. Several isoforms of MIS protein exist due to the alternative splicing. In a human promonocyte cell line, MIS was able to bind Src homology 2-containing protein-tyrosine phosphatases, SHP-1 and SHP-2. This binding was mediated by the membrane-proximal ITIM of MIS. Moreover, MIS exerted an inhibitory effect on Fcgamma RI receptor-induced calcium mobilization. These data suggest that MIS can play an inhibitory role through its ITIM sequences.

* This work was supported by the National Institutes of Health Grant GM56455 (to M. L. T.) and the Human Frontiers Science Program (to M. L. T.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

This paper is dedicated to the memory of Dr. Matthew L. Thomas.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF329269.

Dagger To whom correspondence should be addressed: Washington University School of Medicine, Department of Internal Medicine, Rheumathology Division, P.O. Box 8045 S. Euclid Ave., St. Louis, MO 63110. Tel.: 314-362-9013; Fax: 314-454-0175; E-mail: ulyanova@pathology.wustl.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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