The JI
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 Pelech, S. L.
Right arrow Articles by Federsppiel, B. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pelech, S. L.
Right arrow Articles by Federsppiel, B. S.

The Journal of Immunology, Vol 144, Issue 5 1759-1766, Copyright © 1990 by American Association of Immunologists

ARTICLES

IL-3-induced activation of protein kinases in the mast cell/megakaryocyte R6-XE.4 line

SL Pelech, HB Paddon, DL Charest and BS Federsppiel
Biomedical Research Centre, University of British Columbia, Vancouver, Canada.

A role for second messenger-regulated protein kinases in the early post- IL-3 receptor signal transduction pathway was investigated in the mast cell/megakaryocyte line R6-XE.4. The activity of the calcium- and phospholipid-dependent protein kinase C (PKC) was assessed by the ability of the enzyme to phosphorylate histone H1 in the presence of calcium, diacylglycerol, and phosphatidylserine or after proteolytic activation of PKC with trypsin. In high serum-supplemented cells, but not in cells that were preincubated in serum-deficient media for 6 h, subsequent treatment for 15 min with synthetic IL-3 (10 micrograms/ml) caused up to a sixfold increase in the calcium- and lipid-stimulated histone H1 phosphorylating activity of particulate-associated PKC after fractionation on MonoQ. However, there was no corresponding reduction of cytosolic PKC activity. Therefore, IL-3 appeared to modify the activity of preexisting membrane-associated PKC rather than eliciting its recruitment from the cytoplasm in R6-XE.4 cells. This was in contrast to the situation with FDC-P1 cells, where IL-3 induced PKC translocation. IL-3 also stimulated a cytosolic protein kinase that phosphorylated a synthetic peptide patterned after a phosphorylation site in ribosomal protein S6, but this IL did not alter the activity of cAMP-dependent protein kinase.


This article has been cited by other articles:


Home page
 J. Pharmacol. Exp. Ther.Home page
M. Musashi, K. Sakurada, K.-I. Kawamura, H. Iwasaki, Y. Tsuda, M. Kobayashi, M. Sasaki, K. Kato, E. Tanaka, T. Sudo, et al.
Phorbol Ester Enhancement of IL-3-Dependent Proliferation of Primitive Hematopoietic Progenitors of Mice in Culture
J. Pharmacol. Exp. Ther., January 1, 1997; 280(1): 225 - 231.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
S. L. Ettinger, R. W. Lauener, and V. Duronio
Protein Kinase C delta Specifically Associates with Phosphatidylinositol 3-Kinase Following Cytokine Stimulation
J. Biol. Chem., June 14, 1996; 271(24): 14514 - 14518.
[Abstract] [Full Text] [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.