Am J Physiol Cell Physiol Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol 264: C956-C960, 1993;
0363-6143/93 $5.00
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 Email this article to a friend
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 Harada, H.
Right arrow Articles by Suketa, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Harada, H.
Right arrow Articles by Suketa, Y.

AJP - Cell Physiology, Vol 264, Issue 4 C956-C960, Copyright © 1993 by American Physiological Society

ARTICLES

Extracellular ATP-induced regulation of epidermal growth factor signaling in cultured renal LLC-PK1 cells

H. Harada, H. Tai, A. Motomura, S. Suzuki and Y. Suketa
Department of Environmental Biochemistry and Toxicology, University of Shizuoka, School of Pharmaceutical Sciences, Japan.

We investigated the effect of extracellular ATP on the interaction of epidermal growth factor (EGF) with its receptor in cultured renal epithelial cells, LLC-PK1. Pretreatment with ATP, but not adenosine, inhibited the binding of 125I-labeled EGF. The inhibition demonstrated by ATP resulted from a decrease in the affinity of EGF receptors for its ligand, with no change in the number of EGF receptors. Incubation of phorbol 12-myristate 13-acetate (PMA) for 30 min mimicked the ATP-mediated inhibition. On the other hand, prolonged pretreatment with PMA, which leads to disappearance of protein kinase C activity, reversed the inhibition. In addition, pretreatment with the protein kinase C inhibitor 1-(5-isoquinoline sulfonyl)-2-methylpiperazine prevented the ATP-mediated inhibition. ATP triggered an increase in inositol 1,4,5-trisphosphate levels and translocation of protein kinase C from cytosol to membranes, consist with the stimulation of phospholipase C and the activation of protein kinase C. These results demonstrate that extracellular ATP attenuates the ligand binding affinity of EGF receptor via the stimulation of phospholipase C, leading to the activation of protein kinase C in the LLC-PK1 cells.


This article has been cited by other articles:


Home page
 Am. J. Physiol. Renal Physiol.Home page
D. M. Filipovic, O. A. Adebanjo, M. Zaidi, and W. B. Reeves
Functional and molecular evidence for P2X receptors in LLC-PK1 cells
Am J Physiol Renal Physiol, June 1, 1998; 274(6): F1070 - F1077.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. S. Grewal, L. M. Luttrell, and J. R. Raymond
G Protein-coupled Receptors Desensitize and Down-regulate Epidermal Growth Factor Receptors in Renal Mesangial Cells
J. Biol. Chem., July 13, 2001; 276(29): 27335 - 27344.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online