Molecular cloning, expression, and chromosomal localization of the human earliest lymphocyte activation antigen AIM/CD69, a new member of the C-type animal lectin superfamily of signal-transmitting receptors.
Open Access
- 1 August 1993
- journal article
- Published by Rockefeller University Press in The Journal of Experimental Medicine
- Vol. 178 (2), 537-547
- https://doi.org/10.1084/jem.178.2.537
Abstract
The activation of T lymphocytes, both in vivo and in vitro, induces the expression of CD69. This molecule, which appears to be the earliest inducible cell surface glycoprotein acquired during lymphoid activation, is involved in lymphocyte proliferation and functions as a signal transmitting receptor in lymphocytes, natural killer (NK) cells, and platelets. To determine the structural basis for CD69 function, the cDNA coding for CD69 was isolated by a polymerase chain reaction-based strategy using oligonucleotides deduced from peptide sequences of the purified protein. The isolated cDNA exhibited a single open reading frame of 597 bp coding for CD69, and predicted a 199-amino acid protein of type II membrane topology, with extracellular (COOH-terminal), transmembrane, and intracellular domains. The CD69 clone hybridized to a 1.7-kb mRNA species, which was rapidly induced and degraded after lymphocyte stimulation, consistent with the presence of rapid degradation signals at the 3' untranslated region. Transient expression of the polypeptide encoded by CD69 cDNA in COS-7 cells demonstrated that it presented properties comparable to native CD69 protein. The CD69 gene was regionally mapped to chromosome 12 p13-p12 by both somatic cell hybrid DNA analysis and fluorescence in situ hybridization coupled with GTG banding (G bands by trypsin using Giemsa). Protein sequence homology search revealed that CD69 is a new member of the Ca(2+)-dependent (C-type) lectin superfamily of type II transmembrane receptors, which includes the human NKG2, the rat NKR-P1, and the mouse NKR-P1 families of NK cell-specific genes. CD69 also has a structural homology with other type II lectin cell surface receptors, such as the T cell antigen Ly49, the low avidity immunoglobulin E receptor (CD23), and the hepatic asialoglycoprotein receptors. The CD69 protein also shares functional characteristics with most members of this superfamily, which act as transmembrane signaling receptors in early phases of cellular activation.Keywords
This publication has 56 references indexed in Scilit:
- Tumor necrosis factor‐α production induced in T lymphocytes through the AIM/CD69 activation pathwayEuropean Journal of Immunology, 1992
- Mapping of the human VLA-α4 gene to chromosome 2q31-q32European Journal of Immunology, 1992
- Structure‐function relationship and immunochemical mapping of external and intracellular antigenic sites on the lymphocyte activation inducer molecule, AIM/CD69European Journal of Immunology, 1991
- NKR-P1, a Signal Transduction Molecule on Natural Killer CellsScience, 1990
- Expression of early activation antigen (CD69) during human thymic developmentClinical and Experimental Immunology, 1990
- FcεRII/CD23: The Low Affinity Receptor for IgEAnnual Review of Immunology, 1990
- Transmission of Signals from the T Lymphocyte Antigen Receptor to the Genes Responsible for Cell Proliferation and Immune Function: The Missing LinkAnnual Review of Immunology, 1990
- Expression and function of AIM, an activation inducer molecule of human lymphocytes, is dependent on the activation of protein kinase CEuropean Journal of Immunology, 1989
- Molecular structure of human lymphocyte receptor for immunoglobulin ECell, 1986
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982