Identification and characterization of the rat homologue of LAIR-1

被引:10
作者
Lebbink, RJ [1 ]
de Ruiter, T [1 ]
Kaptijn, GJA [1 ]
Meyaard, L [1 ]
机构
[1] Univ Med Ctr Utrecht, Dept Immunol, NL-3584 EA Utrecht, Netherlands
关键词
receptors; immunologic; ligands; synteny; leukocytes/immunology; sequence homology; amino acid;
D O I
10.1007/s00251-005-0804-4
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
Leukocyte-associated immunoglobulin-like receptor-1 (LAIR-1) is a cell-surface molecule that functions as an inhibitory receptor on various immune cells in both humans and mice. We have cloned a LAIR-1 homologue from the rat that we have named rat LAIR-1. The LAIR-1 gene maps to rat chromosome 1q12 in a region showing conserved synteny with human chromosome 19q13.4 and mouse chromosome 7, where the leukocyte receptor cluster is located. Rat LAIR-1 shows 40 and 71% protein sequence identity with human LAIR-1 and mouse LAIR-1, respectively, has a single Ig-like domain and contains two immunoreceptor tyrosine-based inhibitory motif-like sequences in its cytoplasmic tail. Soluble rat LAIR-1 fusion proteins bind to the same adherent cell lines as human LAIR-1 and mouse LAIR-1, indicating that a putative ligand for all the LAIR-1 molecules is expressed on these cells. Furthermore, we show that rat and mouse LAIR-1 bind the same molecule expressed on human HT29 cells. Since many autoimmune diseases are studied in rat models, identification of rat LAIR-1 allows for in vivo studies on the function of LAIR molecules in these systems.
引用
收藏
页码:344 / 351
页数:8
相关论文
共 27 条
[1]   INTERACTION BETWEEN HUMAN CD2 AND CD58 INVOLVES THE MAJOR BETA-SHEET SURFACE OF EACH OF THEIR RESPECTIVE ADHESION DOMAINS [J].
ARULANANDAM, ARN ;
KISTER, A ;
MCGREGOR, MJ ;
WYSS, DF ;
WAGNER, G ;
REINHERZ, EL .
JOURNAL OF EXPERIMENTAL MEDICINE, 1994, 180 (05) :1861-1871
[2]   Divergent and convergent evolution of NK-cell receptors [J].
Barten, R ;
Torkar, M ;
Haude, A ;
Trowsdale, J ;
Wilson, MJ .
TRENDS IN IMMUNOLOGY, 2001, 22 (01) :52-57
[3]   Characterization of mouse ALCAM (CD166): The CD6-binding domain is conserved in different homologs and mediates cross-species binding [J].
Bowen, MA ;
Bajorath, J ;
DEgidio, M ;
Whitney, GS ;
Palmer, D ;
Kobarg, J ;
Starling, GC ;
Siadak, AW ;
Aruffo, A .
EUROPEAN JOURNAL OF IMMUNOLOGY, 1997, 27 (06) :1469-1478
[4]  
de Vries ARV, 1999, EUR J IMMUNOL, V29, P3160
[5]   FDF03, a novel inhibitory receptor of the immunoglobulin superfamily, is expressed by human dendritic and myeloid cells [J].
Fournier, N ;
Chalus, L ;
Durand, I ;
Garcia, E ;
Pin, JJ ;
Churakova, T ;
Patel, S ;
Zlot, C ;
Gorman, D ;
Zurawski, S ;
Abrams, J ;
Bates, EEM ;
Garrone, P .
JOURNAL OF IMMUNOLOGY, 2000, 165 (03) :1197-1209
[6]  
Hall T.A., 1999, NUCL ACIDS S SER, V41, P95, DOI DOI 10.1021/BK-1999-0734.CH008
[7]   Cutting edge:: Molecular cloning of a killer cell Ig-like receptor in the mouse and rat [J].
Hoelsbrekken, SE ;
Nylenna, O ;
Saether, PC ;
Slettedal, IÖ ;
Ryan, JC ;
Fossum, S ;
Dissen, E .
JOURNAL OF IMMUNOLOGY, 2003, 170 (05) :2259-2263
[8]   Inhibitory receptors and allergy [J].
Katz, HR .
CURRENT OPINION IN IMMUNOLOGY, 2002, 14 (06) :698-704
[9]   NK cell recognition [J].
Lanier, LL .
ANNUAL REVIEW OF IMMUNOLOGY, 2005, 23 :225-274
[10]   The mouse homologue of the leukocyte-associated Ig-like receptor-1 is an inhibitory receptor that recruits Src homology region 2-containing protein tyrosine phosphatase (SHP)-2, but not SHP-1 [J].
Lebbink, RJ ;
de Ruiter, T ;
Verbrugge, A ;
Bril, WS ;
Meyaard, L .
JOURNAL OF IMMUNOLOGY, 2004, 172 (09) :5535-5543