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פותח על ידי קלירמאש פתרונות בע"מ -
Novel interleukin-2 receptor subunit detected by cross-linking under high-affinity conditions
Year:
1986
Source of publication :
Science
Authors :
שרון, מיכל
;
.
Volume :
234
Co-Authors:
Sharon, M., Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, United States
Klausner, R.D., Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, United States
Cullen, B.R., Department of Molecular Genetics, Hoffinann-La Roche, Inc., Nutley, NJ 07110, United States
Chizzonite, R., Department of Molecular Genetics, Hoffinann-La Roche, Inc., Nutley, NJ 07110, United States
Leonard, W.J., Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, United States
Facilitators :
From page:
859
To page:
863
(
Total pages:
5
)
Abstract:
Interleukin-2 (IL-2) binds to both high- and low-affinity classes of IL-2 receptors on activated T lymphocytes. Only the high-affinity receptors are involved in receptor-mediated endocytosis and normally transduce the mitogenic signals of IL-2; however, the structural features distinguishing the high- and low-affinity receptors are unknown. When 125I-labeled IL-2 was chemically cross-linked to activated human T lymphocytes, two major bands were identified. Fust, as predicted, a 68- to 72-kilodalton band, consisting of IL-2 (15.5 kilodaltons) cross-linked to the IL-2 receptor (55 kilodaltons), was observed. Second, an unpredicted 85- to 92-kilodalton moiety was detected. This band was not present when IL-2 was cross-linked to transfected C127 cells, which exclusively express low-affinity receptors. The data presented are most consistent with the existence of a 70- to 77-kilodalton glycoprotein subunit (p70) which, upon associating with the 55-kilodalton low-affinity receptor (p55), transforms it into a high-affinity site. It is proposed that p55 and p70 be referred to as the α and β subunits, respectively, of the high-affinity IL-2 receptor.
Note:
Related Files :
Animals
cell line
Cross-Linking Reagents
human
human cell
Interleukin-2
mice
radioisotope
עוד תגיות
תוכן קשור
More details
DOI :
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
27797
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:34
Scientific Publication
Novel interleukin-2 receptor subunit detected by cross-linking under high-affinity conditions
234
Sharon, M., Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, United States
Klausner, R.D., Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, United States
Cullen, B.R., Department of Molecular Genetics, Hoffinann-La Roche, Inc., Nutley, NJ 07110, United States
Chizzonite, R., Department of Molecular Genetics, Hoffinann-La Roche, Inc., Nutley, NJ 07110, United States
Leonard, W.J., Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, United States
Novel interleukin-2 receptor subunit detected by cross-linking under high-affinity conditions
Interleukin-2 (IL-2) binds to both high- and low-affinity classes of IL-2 receptors on activated T lymphocytes. Only the high-affinity receptors are involved in receptor-mediated endocytosis and normally transduce the mitogenic signals of IL-2; however, the structural features distinguishing the high- and low-affinity receptors are unknown. When 125I-labeled IL-2 was chemically cross-linked to activated human T lymphocytes, two major bands were identified. Fust, as predicted, a 68- to 72-kilodalton band, consisting of IL-2 (15.5 kilodaltons) cross-linked to the IL-2 receptor (55 kilodaltons), was observed. Second, an unpredicted 85- to 92-kilodalton moiety was detected. This band was not present when IL-2 was cross-linked to transfected C127 cells, which exclusively express low-affinity receptors. The data presented are most consistent with the existence of a 70- to 77-kilodalton glycoprotein subunit (p70) which, upon associating with the 55-kilodalton low-affinity receptor (p55), transforms it into a high-affinity site. It is proposed that p55 and p70 be referred to as the α and β subunits, respectively, of the high-affinity IL-2 receptor.
Scientific Publication
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