AJP - Renal Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Am J Physiol Renal Physiol 267: F428-F436, 1994;
0363-6127/94 $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 Cybulsky, A. V.
Right arrow Articles by McTavish, A. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cybulsky, A. V.
Right arrow Articles by McTavish, A. J.

AJP - Renal Physiology, Vol 267, Issue 3 428-F436, Copyright © 1994 by American Physiological Society


ARTICLES

Epidermal growth factor receptor activation in developing rat kidney

A. V. Cybulsky, P. R. Goodyer and A. J. McTavish
Department of Medicine, Royal Victoria Hospital, Montreal, Quebec, Canada.

Epidermal growth factor (EGF) binding increases in late-gestational rat kidney and then falls toward basal adult levels postnatally during the 1st wk. We report that the increase in EGF binding is accompanied by an increase in EGF receptor (EGFR) protein and activation of EGFR tyrosine kinase. Multiple proteins were endogenously tyrosine phosphorylated in kidney membranes from fetal rats, and the phosphorylation pattern was similar in rats ranging from 16 to 21 days of gestation. Tyrosine phosphorylation was, however, almost undetectable in 12-wk adult rat kidneys (controls). Among the phosphoproteins in fetal kidney, a prominent 170-kDa protein was identified as EGFR. Endogenous tyrosine phosphorylation of EGFR (reflecting receptor activation) was 30-fold higher in fetal kidney membranes than in adult (3- to 7-fold higher when adjusted for differences in EGF binding or EGFR protein content). The EGFR substrate, phospholipase C-gamma 1, was tyrosine phosphorylated in fetal kidneys but not adult, and a greater proportion was membrane-associated in fetal kidneys, consistent with activation of phospholipase C-gamma 1. Thus EGFR tyrosine kinase activity is increased in late-gestational rat kidney. Induction and activation of EGFR may mediate perinatal renal cell growth and development.


This article has been cited by other articles:


Home page
Am. J. Physiol. Renal Physiol.Home page
A. V. Cybulsky, T. Takano, J. Papillon, A. Khadir, K. Bijian, C.-C. Chien, C. E. Alpers, and H. Rabb
Renal expression and activity of the germinal center kinase SK2
Am J Physiol Renal Physiol, January 1, 2004; 286(1): F16 - F25.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
K. Qing, J. Hansen, K. A. Weigel-Kelley, M. Tan, S. Zhou, and A. Srivastava
Adeno-Associated Virus Type 2-Mediated Gene Transfer: Role of Cellular FKBP52 Protein in Transgene Expression
J. Virol., October 1, 2001; 75(19): 8968 - 8976.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
K. Amsler and S. K. Kuwada
Membrane receptor location defines receptor interaction with signaling proteins in a polarized epithelium
Am J Physiol Cell Physiol, January 1, 1999; 276(1): C91 - C101.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Renal Physiol.Home page
M. Arar, H. K. Zajicek, I. Elshihabi, and M. Levi
Epidermal growth factor inhibits Na-Pi cotransport in weaned and suckling rats
Am J Physiol Renal Physiol, January 1, 1999; 276(1): F72 - F78.
[Abstract] [Full Text] [PDF]




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