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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
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, bec...
Autores principales: | , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1999
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2195632/ https://www.ncbi.nlm.nih.gov/pubmed/10499918 |
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author | Falco, Michela Biassoni, Roberto Bottino, Cristina Vitale, Massimo Sivori, Simona Augugliaro, Raffaella Moretta, Lorenzo Moretta, Alessandro |
author_facet | Falco, Michela Biassoni, Roberto Bottino, Cristina Vitale, Massimo Sivori, Simona Augugliaro, Raffaella Moretta, Lorenzo Moretta, Alessandro |
author_sort | Falco, Michela |
collection | PubMed |
description | 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 NH(2)-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. |
format | Text |
id | pubmed-2195632 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1999 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21956322008-04-16 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 Falco, Michela Biassoni, Roberto Bottino, Cristina Vitale, Massimo Sivori, Simona Augugliaro, Raffaella Moretta, Lorenzo Moretta, Alessandro J Exp Med Original Article 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 NH(2)-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. The Rockefeller University Press 1999-09-20 /pmc/articles/PMC2195632/ /pubmed/10499918 Text en © 1999 The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Original Article Falco, Michela Biassoni, Roberto Bottino, Cristina Vitale, Massimo Sivori, Simona Augugliaro, Raffaella Moretta, Lorenzo Moretta, Alessandro 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 |
title | 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 |
title_full | 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 |
title_fullStr | 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 |
title_full_unstemmed | 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 |
title_short | 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 |
title_sort | 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 |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2195632/ https://www.ncbi.nlm.nih.gov/pubmed/10499918 |
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