Evidence for additional subunits associated to the mouse interleukin 2 receptor p55/p75 complex

Horacio Saragovi, Thomas Malek

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

Previous studies have indicated that high-affinity interleukin 2 receptors (IL-2R) are comprised of at least two distinct noncovalently associated subunits of Mr 55,000 (p55) and Mr 75,000 (p75). To biochemically characterize p75, we have directly isolated IL-2R using affinity precipitations with immobilized IL-2. We now report that at least some mouse p75 appears to exist as a disulfide-linked heterodimer with a subunit of Mr 22,000 (p22). These findings suggest that functional high-affinity mouse IL-2R may be comprised of at least three distinct subunits. The possibility of an even more complex structure is suggested by the coprecipitation of a protein of Mr 40,000-45,000 (p40) that may represent an additional IL-2R-associated protein.

Original languageEnglish
Pages (from-to)11-15
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume87
Issue number1
StatePublished - Dec 1 1990

Fingerprint

Interleukin-2 Receptors
Disulfides
Interleukin-2
Proteins

Keywords

  • Receptor affinity
  • T lymphocytes

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

@article{2e9f7f304afc461fb5a7eaf7371ac7de,
title = "Evidence for additional subunits associated to the mouse interleukin 2 receptor p55/p75 complex",
abstract = "Previous studies have indicated that high-affinity interleukin 2 receptors (IL-2R) are comprised of at least two distinct noncovalently associated subunits of Mr 55,000 (p55) and Mr 75,000 (p75). To biochemically characterize p75, we have directly isolated IL-2R using affinity precipitations with immobilized IL-2. We now report that at least some mouse p75 appears to exist as a disulfide-linked heterodimer with a subunit of Mr 22,000 (p22). These findings suggest that functional high-affinity mouse IL-2R may be comprised of at least three distinct subunits. The possibility of an even more complex structure is suggested by the coprecipitation of a protein of Mr 40,000-45,000 (p40) that may represent an additional IL-2R-associated protein.",
keywords = "Receptor affinity, T lymphocytes",
author = "Horacio Saragovi and Thomas Malek",
year = "1990",
month = "12",
day = "1",
language = "English",
volume = "87",
pages = "11--15",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "1",

}

TY - JOUR

T1 - Evidence for additional subunits associated to the mouse interleukin 2 receptor p55/p75 complex

AU - Saragovi, Horacio

AU - Malek, Thomas

PY - 1990/12/1

Y1 - 1990/12/1

N2 - Previous studies have indicated that high-affinity interleukin 2 receptors (IL-2R) are comprised of at least two distinct noncovalently associated subunits of Mr 55,000 (p55) and Mr 75,000 (p75). To biochemically characterize p75, we have directly isolated IL-2R using affinity precipitations with immobilized IL-2. We now report that at least some mouse p75 appears to exist as a disulfide-linked heterodimer with a subunit of Mr 22,000 (p22). These findings suggest that functional high-affinity mouse IL-2R may be comprised of at least three distinct subunits. The possibility of an even more complex structure is suggested by the coprecipitation of a protein of Mr 40,000-45,000 (p40) that may represent an additional IL-2R-associated protein.

AB - Previous studies have indicated that high-affinity interleukin 2 receptors (IL-2R) are comprised of at least two distinct noncovalently associated subunits of Mr 55,000 (p55) and Mr 75,000 (p75). To biochemically characterize p75, we have directly isolated IL-2R using affinity precipitations with immobilized IL-2. We now report that at least some mouse p75 appears to exist as a disulfide-linked heterodimer with a subunit of Mr 22,000 (p22). These findings suggest that functional high-affinity mouse IL-2R may be comprised of at least three distinct subunits. The possibility of an even more complex structure is suggested by the coprecipitation of a protein of Mr 40,000-45,000 (p40) that may represent an additional IL-2R-associated protein.

KW - Receptor affinity

KW - T lymphocytes

UR - http://www.scopus.com/inward/record.url?scp=0025012981&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025012981&partnerID=8YFLogxK

M3 - Article

VL - 87

SP - 11

EP - 15

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 1

ER -