The JI PBL Intereron Source
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     
 

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Pessa-Morikawa, T.
Right arrow Articles by Andersson, L. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pessa-Morikawa, T.
Right arrow Articles by Andersson, L. C.

The Journal of Immunology, Vol 144, Issue 7 2690-2695, Copyright © 1990 by American Association of Immunologists

ARTICLES

Functional maturation of human T lymphocytes is accompanied by changes in the G-protein pattern

T Pessa-Morikawa, T Mustelin and LC Andersson
Department of Pathology, University of Helsinki, Finland.

The putative guanine nucleotide binding (G)-protein involved in transduction of signals from the TCR/CD3 complex has not been identified. We have used a UV-photoaffinity labeling technique to covalently attach [alpha-32P]GTP to human lymphocyte and thymocyte membrane proteins. Ten bands specifically labeled with [32P]GTP were detected by SDS-PAGE and autoradiography in T lymphocyte membranes. Among these, a 40-kDa protein was identified by immunoblotting as the alpha-subunit of the adenylate cyclase-inhibiting G-protein, Gi, and two proteins of 44 and 46 kDa were identified as the alpha-subunits of adenylate cyclase stimulating G-protein (Gs). These proteins also served as substrates for ADP-ribosylation by pertussis toxin and cholera toxin, respectively. Comparison of GTP-labeled membrane proteins from immature and more mature thymocytes and blood T lymphocytes, revealed that bands of 26, 30, 34, 40, 44 and 46 kDa were absent or weakly labeled in immature thymocytes, intermediate in mature thymocytes, and strongest in blood T cells. Similar increases were seen in ADP ribosylation of the substrates for pertussis, cholera, and botulinum C3 toxin. However, corresponding quantitative changes in Gi and Gs were not detected by immunoblotting, which suggests that the increased labeling is caused by enhanced affinity of the proteins for GTP rather than by increased amount of protein during thymic maturation. A concomitant maturation of GTP-induced cAMP production was seen in the cell populations, but no such change occurred in direct activation of adenylate cyclase by forskolin. The changes in some (but not all) GTP-binding proteins during acquisition of immunocompetence indicates their importance in T lymphocyte physiology.


This article has been cited by other articles:


Home page
 Arterioscler. Thromb. Vasc. Bio.Home page
H. van der Vuurst, G. van Willigen, A. van Spronsen, M. Hendriks, J. Donath, and J.-W. N. Akkerman
Signal Transduction Through Trimeric G Proteins in Megakaryoblastic Cell Lines
Arterioscler. Thromb. Vasc. Biol., September 1, 1997; 17(9): 1830 - 1836.
[Abstract] [Full Text]

Home page
 ScienceHome page
J. Telfer and C. Rudd
A 32-kD GTP-binding protein associated with the CD4-p56lck and CD8-p56lck T cell receptor complexes
Science, October 18, 1991; 254(5030): 439 - 441.
[Abstract] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 1990 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 1990 by The American Association of Immunologists, Inc. All rights reserved.