Internalization of IL-2 by an IL-2-dependent murine T cell lymphoma expressing no detectable cell surface receptors for IL-2

H C O'Neill, A Jaworowski

Research output: Contribution to journalArticleResearchpeer-review

1 Citation (Scopus)

Abstract

A murine Radiation leukemia virus-induced T cell lymphoma, 5C2, which is dependent on interleukin-2 (IL-2) for proliferation has been analyzed for interleukin-2 receptor (IL-2R) expression. Using fluorescence-activated cell sorter and electron microscopic analysis together with antibody specific for the known p55 chain of the murine IL-2R, no evidence has been obtained to suggest that these cells express detectable numbers of receptors with high affinity for IL-2. However, two different antibodies with specificity for the p55 chain of the IL-2R have been shown to inhibit 5C2 proliferation. An analysis of 125I-IL-2 binding has precluded a cell surface receptor density of greater than 80 molecules per cell. A temperature-dependent, nonspecific uptake of 125I-IL-2 has been described for 5C2. Uptake is saturated at 8.5 nM 125I-IL-2 with equilibrium being established within 60 min. When incubated at 37 degrees C in the presence of 400 pM 125I-IL-2, a maximum of approximately 2,000 molecules are internalized within 40 min. Uptake of other iodinated proteins by 5C2 was not observed. This property is unique to 5C2 and not to the control C6VL/1 cell line. Intracellular vesicles have also been found in 5C2 cells by electron microscopy which stain positively with gold-conjugated antibody specific for the p55 chain of the IL-2R. 5C2 appears to exhibit unique IL-2 regulatory characteristics.

Original languageEnglish
Pages (from-to)388-393
Number of pages6
JournalLeukemia
Volume2
Issue number6
Publication statusPublished - Jun 1988
Externally publishedYes

Fingerprint

T-Cell Lymphoma
Cell Surface Receptors
Interleukin-2
Interleukin-2 Receptors
Radiation Leukemia Virus
Murine Leukemia Viruses
Antibody Specificity
Antibodies
Gold
Electron Microscopy
Coloring Agents
Fluorescence
Electrons
Cell Line
Temperature
Proteins

Cite this

@article{5e95e0692e2e477aad8b4b5dc45ea99f,
title = "Internalization of IL-2 by an IL-2-dependent murine T cell lymphoma expressing no detectable cell surface receptors for IL-2",
abstract = "A murine Radiation leukemia virus-induced T cell lymphoma, 5C2, which is dependent on interleukin-2 (IL-2) for proliferation has been analyzed for interleukin-2 receptor (IL-2R) expression. Using fluorescence-activated cell sorter and electron microscopic analysis together with antibody specific for the known p55 chain of the murine IL-2R, no evidence has been obtained to suggest that these cells express detectable numbers of receptors with high affinity for IL-2. However, two different antibodies with specificity for the p55 chain of the IL-2R have been shown to inhibit 5C2 proliferation. An analysis of 125I-IL-2 binding has precluded a cell surface receptor density of greater than 80 molecules per cell. A temperature-dependent, nonspecific uptake of 125I-IL-2 has been described for 5C2. Uptake is saturated at 8.5 nM 125I-IL-2 with equilibrium being established within 60 min. When incubated at 37 degrees C in the presence of 400 pM 125I-IL-2, a maximum of approximately 2,000 molecules are internalized within 40 min. Uptake of other iodinated proteins by 5C2 was not observed. This property is unique to 5C2 and not to the control C6VL/1 cell line. Intracellular vesicles have also been found in 5C2 cells by electron microscopy which stain positively with gold-conjugated antibody specific for the p55 chain of the IL-2R. 5C2 appears to exhibit unique IL-2 regulatory characteristics.",
author = "O'Neill, {H C} and A Jaworowski",
year = "1988",
month = "6",
language = "English",
volume = "2",
pages = "388--393",
journal = "Leukemia",
issn = "0887-6924",
publisher = "Nature Publishing Group",
number = "6",

}

Internalization of IL-2 by an IL-2-dependent murine T cell lymphoma expressing no detectable cell surface receptors for IL-2. / O'Neill, H C; Jaworowski, A.

In: Leukemia, Vol. 2, No. 6, 06.1988, p. 388-393.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Internalization of IL-2 by an IL-2-dependent murine T cell lymphoma expressing no detectable cell surface receptors for IL-2

AU - O'Neill, H C

AU - Jaworowski, A

PY - 1988/6

Y1 - 1988/6

N2 - A murine Radiation leukemia virus-induced T cell lymphoma, 5C2, which is dependent on interleukin-2 (IL-2) for proliferation has been analyzed for interleukin-2 receptor (IL-2R) expression. Using fluorescence-activated cell sorter and electron microscopic analysis together with antibody specific for the known p55 chain of the murine IL-2R, no evidence has been obtained to suggest that these cells express detectable numbers of receptors with high affinity for IL-2. However, two different antibodies with specificity for the p55 chain of the IL-2R have been shown to inhibit 5C2 proliferation. An analysis of 125I-IL-2 binding has precluded a cell surface receptor density of greater than 80 molecules per cell. A temperature-dependent, nonspecific uptake of 125I-IL-2 has been described for 5C2. Uptake is saturated at 8.5 nM 125I-IL-2 with equilibrium being established within 60 min. When incubated at 37 degrees C in the presence of 400 pM 125I-IL-2, a maximum of approximately 2,000 molecules are internalized within 40 min. Uptake of other iodinated proteins by 5C2 was not observed. This property is unique to 5C2 and not to the control C6VL/1 cell line. Intracellular vesicles have also been found in 5C2 cells by electron microscopy which stain positively with gold-conjugated antibody specific for the p55 chain of the IL-2R. 5C2 appears to exhibit unique IL-2 regulatory characteristics.

AB - A murine Radiation leukemia virus-induced T cell lymphoma, 5C2, which is dependent on interleukin-2 (IL-2) for proliferation has been analyzed for interleukin-2 receptor (IL-2R) expression. Using fluorescence-activated cell sorter and electron microscopic analysis together with antibody specific for the known p55 chain of the murine IL-2R, no evidence has been obtained to suggest that these cells express detectable numbers of receptors with high affinity for IL-2. However, two different antibodies with specificity for the p55 chain of the IL-2R have been shown to inhibit 5C2 proliferation. An analysis of 125I-IL-2 binding has precluded a cell surface receptor density of greater than 80 molecules per cell. A temperature-dependent, nonspecific uptake of 125I-IL-2 has been described for 5C2. Uptake is saturated at 8.5 nM 125I-IL-2 with equilibrium being established within 60 min. When incubated at 37 degrees C in the presence of 400 pM 125I-IL-2, a maximum of approximately 2,000 molecules are internalized within 40 min. Uptake of other iodinated proteins by 5C2 was not observed. This property is unique to 5C2 and not to the control C6VL/1 cell line. Intracellular vesicles have also been found in 5C2 cells by electron microscopy which stain positively with gold-conjugated antibody specific for the p55 chain of the IL-2R. 5C2 appears to exhibit unique IL-2 regulatory characteristics.

M3 - Article

VL - 2

SP - 388

EP - 393

JO - Leukemia

JF - Leukemia

SN - 0887-6924

IS - 6

ER -