נגישות
menu      
חיפוש מתקדם
תחביר
חפש...
הספר "אוצר וולקני"
אודות
תנאי שימוש
ניהול
קהילה:
אסיף מאגר המחקר החקלאי
פותח על ידי קלירמאש פתרונות בע"מ -
The β-chain of the IL-2 receptor (p70) is tyrosine-phosphorylated on YT and HUT-102B2 cells
Year:
1989
Source of publication :
Journal of Immunology
Authors :
שרון, מיכל
;
.
Volume :
143
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
Gnarra, J.R., Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, 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:
2530
To page:
2533
(
Total pages:
4
)
Abstract:
IL-2 has previously been shown to rapidly induce activity of a tyrosine kinase. High-affinity IL-2 receptors that mediate the major mitogenic signals of IL-2 contain both p70 and p55 chains. p55 has no potential tyrosine phosphorylation sites and lacks consensus sequences found in protein tyrosine kinases. Inasmuch as the phosphorylation of hormone receptors is generally an important mechanism for regulating receptor function, we have now investigated the phosphorylation status of p70. By using anti-phosphotyrosine antibodies to immuno-precipitate affinity-labeled IL-2 receptors and to probe Western blots, we provide data suggesting that p70, but not p55, is constitutively tyrosine-phosphorylated on the leukemic cell lines studied.
Note:
Related Files :
Cell Line, Transformed
Cross-Linking Reagents
genetic engineering
histochemistry
human cell
phosphotyrosine
tyrosine
עוד תגיות
תוכן קשור
More details
DOI :
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
25656
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:16
You may also be interested in
Scientific Publication
The β-chain of the IL-2 receptor (p70) is tyrosine-phosphorylated on YT and HUT-102B2 cells
143
Sharon, M., Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, United States
Gnarra, J.R., Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, 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
The β-chain of the IL-2 receptor (p70) is tyrosine-phosphorylated on YT and HUT-102B2 cells
IL-2 has previously been shown to rapidly induce activity of a tyrosine kinase. High-affinity IL-2 receptors that mediate the major mitogenic signals of IL-2 contain both p70 and p55 chains. p55 has no potential tyrosine phosphorylation sites and lacks consensus sequences found in protein tyrosine kinases. Inasmuch as the phosphorylation of hormone receptors is generally an important mechanism for regulating receptor function, we have now investigated the phosphorylation status of p70. By using anti-phosphotyrosine antibodies to immuno-precipitate affinity-labeled IL-2 receptors and to probe Western blots, we provide data suggesting that p70, but not p55, is constitutively tyrosine-phosphorylated on the leukemic cell lines studied.
Scientific Publication
You may also be interested in