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Activation of natural killer cells and dendritic cells upon recognition of a novel CD99-like ligand by paired immunoglobulin-like type 2 receptor.

Shiratori I, Ogasawara K, Saito T, Lanier LL, Arase H - J. Exp. Med. (2004)

Bottom Line: Transcripts of PILR ligand are present in many tissues, including some T cell lines.Cells expressing the PILR ligand specifically activated NK cells and dendritic cells that express the activating PILRbeta.Our findings reveal a new regulatory mechanism of innate immunity by PILR and its CD99-like ligand.

View Article: PubMed Central - PubMed

Affiliation: Department of Molecular Genetics, Chiba University Graduate School of Medicine, 1-8-1 Inohana, Chuoku, 260-8670, Japan.

ABSTRACT
Paired receptors that consist of highly related activating and inhibitory receptors are widely involved in the regulation of the immune system. Here, we report a mouse orthologue of the human activating paired immunoglobulin-like type 2 receptor (PILR) beta, which was cloned from a cDNA library of natural killer (NK) cells based on its ability to associate with the DAP12 signaling adaptor protein. The activating PILRbeta was expressed not only on NK cells but also on dendritic cells and macrophages. Furthermore, we have identified a novel CD99-like molecule as a ligand for the activating PILRbeta and inhibitory PILRalpha receptors. Transcripts of PILR ligand are present in many tissues, including some T cell lines. Cells expressing the PILR ligand specifically activated NK cells and dendritic cells that express the activating PILRbeta. Our findings reveal a new regulatory mechanism of innate immunity by PILR and its CD99-like ligand.

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Amino acid comparison between mouse PILRα and PILRβ. Amino acid alignment of mouse PILRα and PILRβ is shown. Signal sequence and transmembrane region are indicated by double and single underline, respectively. A charged residue (K, bold and italicized) in transmembrane domain of PILRβ and the ITIM sequence in the cytoplasmic domain of PILRα are indicated (bold letters). Identical amino acids between PILRβ and PILRα are indicated by asterisks. GenBank/EMBL/DDBJ accession nos. of mouse PILRα and PILRβ are NM_153510 and AB122024/NM_133209, respectively.
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fig1: Amino acid comparison between mouse PILRα and PILRβ. Amino acid alignment of mouse PILRα and PILRβ is shown. Signal sequence and transmembrane region are indicated by double and single underline, respectively. A charged residue (K, bold and italicized) in transmembrane domain of PILRβ and the ITIM sequence in the cytoplasmic domain of PILRα are indicated (bold letters). Identical amino acids between PILRβ and PILRα are indicated by asterisks. GenBank/EMBL/DDBJ accession nos. of mouse PILRα and PILRβ are NM_153510 and AB122024/NM_133209, respectively.

Mentions: Human and mouse PILRα (also called FDF03; references 15, 16) have been identified as an ITIM-containing inhibitory receptor that is highly related to PILRβ. Fig. 1 demonstrates the amino acid comparison between mouse PILRα and mouse PILRβ. PILRβ, but not PILRα, contains a positively charged amino acid in the transmembrane region that is required for association with DAP12 (25). Amino acid homology of the extracellular domain between mouse PILRα and PILRβ is 83%, with the NH2 terminus of the extracellular domain showing very high similarity. This suggested that PILRα and PILRβ might recognize a common ligand.


Activation of natural killer cells and dendritic cells upon recognition of a novel CD99-like ligand by paired immunoglobulin-like type 2 receptor.

Shiratori I, Ogasawara K, Saito T, Lanier LL, Arase H - J. Exp. Med. (2004)

Amino acid comparison between mouse PILRα and PILRβ. Amino acid alignment of mouse PILRα and PILRβ is shown. Signal sequence and transmembrane region are indicated by double and single underline, respectively. A charged residue (K, bold and italicized) in transmembrane domain of PILRβ and the ITIM sequence in the cytoplasmic domain of PILRα are indicated (bold letters). Identical amino acids between PILRβ and PILRα are indicated by asterisks. GenBank/EMBL/DDBJ accession nos. of mouse PILRα and PILRβ are NM_153510 and AB122024/NM_133209, respectively.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2211832&req=5

fig1: Amino acid comparison between mouse PILRα and PILRβ. Amino acid alignment of mouse PILRα and PILRβ is shown. Signal sequence and transmembrane region are indicated by double and single underline, respectively. A charged residue (K, bold and italicized) in transmembrane domain of PILRβ and the ITIM sequence in the cytoplasmic domain of PILRα are indicated (bold letters). Identical amino acids between PILRβ and PILRα are indicated by asterisks. GenBank/EMBL/DDBJ accession nos. of mouse PILRα and PILRβ are NM_153510 and AB122024/NM_133209, respectively.
Mentions: Human and mouse PILRα (also called FDF03; references 15, 16) have been identified as an ITIM-containing inhibitory receptor that is highly related to PILRβ. Fig. 1 demonstrates the amino acid comparison between mouse PILRα and mouse PILRβ. PILRβ, but not PILRα, contains a positively charged amino acid in the transmembrane region that is required for association with DAP12 (25). Amino acid homology of the extracellular domain between mouse PILRα and PILRβ is 83%, with the NH2 terminus of the extracellular domain showing very high similarity. This suggested that PILRα and PILRβ might recognize a common ligand.

Bottom Line: Transcripts of PILR ligand are present in many tissues, including some T cell lines.Cells expressing the PILR ligand specifically activated NK cells and dendritic cells that express the activating PILRbeta.Our findings reveal a new regulatory mechanism of innate immunity by PILR and its CD99-like ligand.

View Article: PubMed Central - PubMed

Affiliation: Department of Molecular Genetics, Chiba University Graduate School of Medicine, 1-8-1 Inohana, Chuoku, 260-8670, Japan.

ABSTRACT
Paired receptors that consist of highly related activating and inhibitory receptors are widely involved in the regulation of the immune system. Here, we report a mouse orthologue of the human activating paired immunoglobulin-like type 2 receptor (PILR) beta, which was cloned from a cDNA library of natural killer (NK) cells based on its ability to associate with the DAP12 signaling adaptor protein. The activating PILRbeta was expressed not only on NK cells but also on dendritic cells and macrophages. Furthermore, we have identified a novel CD99-like molecule as a ligand for the activating PILRbeta and inhibitory PILRalpha receptors. Transcripts of PILR ligand are present in many tissues, including some T cell lines. Cells expressing the PILR ligand specifically activated NK cells and dendritic cells that express the activating PILRbeta. Our findings reveal a new regulatory mechanism of innate immunity by PILR and its CD99-like ligand.

Show MeSH