Further Characterization of CD82/IA4 Antigen (Type III Surface Protein): An Activation/Differentiation Marker of Mononuclear Cells
Autor: | Sophie Lebel-Binay, Hélène Conjeaud, Didier Fradelizi, Anne Quillet-Mary, Carmen Marchiol-Fournigault, Manuel Lopez, Maria Luisa Gil, Cécile Lagaudriere, Brigitte Miloux |
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Přispěvatelé: | Institut Cochin (UMR_S567 / UMR 8104), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées, Hôpital Purpan [Toulouse], CHU Toulouse [Toulouse], Matière et Systèmes Complexes (MSC (UMR_7057)), Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS) |
Rok vydání: | 1994 |
Předmět: |
CD53
T-Lymphocytes Immunoblotting Immunology Cell Communication [SDV.BC]Life Sciences [q-bio]/Cellular Biology CD37 Human leukocyte antigen Biology Kangai-1 Protein Lymphocyte Activation Epitope Cell Line Epitopes Mice 03 medical and health sciences 0302 clinical medicine Antigen Antigens CD Proto-Oncogene Proteins Animals Humans Killer Cells Lymphokine-Activated ComputingMilieux_MISCELLANEOUS 030304 developmental biology 0303 health sciences MHC class II Membrane Glycoproteins Cluster of differentiation Macrophages Chromosome Mapping Molecular biology 3. Good health Mice Inbred DBA Cell culture 030220 oncology & carcinogenesis Antigens Surface Leukocytes Mononuclear biology.protein [SDV.IMM]Life Sciences [q-bio]/Immunology |
Zdroj: | Cellular Immunology Cellular Immunology, Elsevier, 1994, 154 (2), pp.468-483. ⟨10.1006/cimm.1994.1092⟩ |
ISSN: | 0008-8749 1090-2163 |
DOI: | 10.1006/cimm.1994.1092 |
Popis: | The mononuclear cell surface protein IA4 was originally identified in our lab using a mAb selected because of its strong reactivity with three lymphoblastoid variant cell lines which are HLA class I deficient, are LAK susceptible, and form a high number of conjugates with LAK effectors. We previously cloned the cDNA of the IA4 protein, coding for a 267-amino-acid type III integral membrane protein, with four transmembrane domains and three possible N-glycosylation sites. The IA4 protein belongs to the tetra span transmembrane (TST) new family of surface molecules, which also includes CD9, CD37, CD53, CD63, and TAPA-1. IA4 antigen was recently recognized as belonging to a new cluster of differentiation CD82 (International CD Workshop, Boston 1993). The IA4 antigen expression pattern at the surface of immune cells from normal donors was studied. On T lymphocytes, IA4 was barely detectable on resting cells and increased 3.5- to 7-fold following PHA or PHA+PMA stimulation. This IA4 increased expression is correlated with the morphologic change in blast cells and with the expression of activation markers such as CD2 and MHC class II antigens, therefore suggesting that IA4 is an activation marker on T lymphocytes. The expression of IA4 was low on circulating resting monocytes collected by elutriation. However, these monocytes, cultured in medium alone or with GM-CSF, acquired the morphology of macrophage and simultaneously overexpressed MHC Class II, CD14, and IA4 antigens, suggesting that IA4 is a differentiation marker for macrophages, whatever the culture conditions, either adherent (plastic culture dishes) or nonadherent (Teflon culture bags). IA4 stable transfectants of the murine mastocytoma cell line P815 were obtained and used to generate a new mAb. Competitive epitope binding studies have shown that IA4 antigen presents a dominant epitope recognized by most of the mAb prepared either in our lab or elsewhere. This dominant epitope is not shared by any of the other antigens of the TST family. Using this new mAb we were able to biochemically characterize the IA4 antigen as a 28-kDa protein, highly N-glycosylated with different patterns on various cells. |
Databáze: | OpenAIRE |
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