Expression of low-, intermediate-, and high-affinity IL-2 receptors on B cell lines derived from patients with undifferentiated lymphoma of Burkitt's and non-Burkitt's types

Journal Article · Wed Aug 01 04:00:00 EDT 1990 · Cellular Immunology; (USA)

DOI:https://doi.org/10.1016/0008-8749(90)90191-S· OSTI ID:6870261

Benjamin, D; Rosolen, A; Wormsley, S B; DeBault, L E; Colamonici, O R ^[1]

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1. Saint Francis Research Institute, Oklahoma City, OK (USA)

IL-2 receptors on T cells exist in at least three forms which differ in their ligand-binding affinity. The low-affinity IL-2 receptor (IL-2R) consists of the 55-kDa Tac protein (p55 alpha), the intermediate-affinity site corresponds to the 70-kDa molecule (p70 beta), and the high-affinity IL-2R consists of a noncovalent heterodimeric structure involving both p55 alpha and p70 beta. We studied 24 B cell lines (8 EBV-negative and 16 EBV-positive) for IL-2R expression in the presence or absence of the tumor promoter, teleocidin. 125I-IL-2 radioreceptor binding assays and crosslinking studies demonstrated the sole expression of p55 alpha in EBV-negative cell lines only, whereas p55 alpha present in EBV-positive cell lines was always associated with p70 beta to construct high-affinity IL-2R. p70 beta was not detected in any of the EBV-negative cell lines, but was expressed on most of the EBV-positive cell lines (13 of 16). Our data also indicate that the expression of p55 alpha and p70 beta by radiolabeling correlates with their expression in flow cytometry, and that a large excess of p55 alpha is required to construct high-affinity IL-2R. Coexpression of p55 alpha and p70 beta on human B cells contributed to constructing high-affinity IL-2R hybrid complex as shown by rapid association rate contributed by p55 alpha and slow dissociation rate by p70 beta; teleocidin's ability to induce p55 alpha on cell lines which express p70 beta only, resulting in appearance of high-affinity IL-2R; and blocking p55 alpha by anti-Tac mAb in cell lines which constitutively express high-affinity IL-2R eliminated both high- and low-affinity components. The existence of low, intermediate, and high IL-2R on human B cells bears important future implications for understanding the mechanism of IL-2 signaling and the role of IL-2 in B cell activation, proliferation, and differentiation.

• OSTI ID: 6870261
• Journal Information: Cellular Immunology; (USA), Journal Name: Cellular Immunology; (USA) Vol. 129:1; ISSN 0008-8749; ISSN CLIMB
• Country of Publication: United States
• Language: English

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59 BASIC BIOLOGICAL SCIENCES
AFFINITY
ANIMAL CELLS
ANIMALS
BETA DECAY RADIOISOTOPES
BIOCHEMICAL REACTION KINETICS
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
CELL FLOW SYSTEMS
CELL PROLIFERATION
CHEMICAL COMPOSITION
CHEMICAL REACTIONS
CONNECTIVE TISSUE CELLS
CROSS-LINKING
DAYS LIVING RADIOISOTOPES
DISEASES
ELECTRON CAPTURE RADIOISOTOPES
GROWTH FACTORS
IMMUNE SYSTEM DISEASES
INTERMEDIATE MASS NUCLEI
IODINE 125
IODINE ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
KINETICS
LEUKOCYTES
LYMPHOCYTES
LYMPHOKINES
LYMPHOMAS
MAMMALS
MAN
MATERIALS
MEMBRANE PROTEINS
MITOGENS
NEOPLASMS
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
POLYMERIZATION
PRIMATES
PROTEINS
RADIOISOTOPES
RADIORECEPTOR ASSAY
REACTION KINETICS
REAGENTS
RECEPTORS
SOMATIC CELLS
TRACER TECHNIQUES
TUMOR CELLS
VERTEBRATES