JBC

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
Right arrow Citation Map
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
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Friesel, R.
Right arrow Articles by Maciag, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Friesel, R.
Right arrow Articles by Maciag, T.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 261, Issue 17, 7581-7584, 06, 1986

The characterization of the receptor for endothelial cell growth factor by covalent ligand attachment

R Friesel, WH Burgess, T Mehlman and T Maciag

Cellular receptors for endothelial cell growth factor (ECGF) have been demonstrated on several cell types by binding of 125I-ECGF in a specific and saturable manner (Schreiber, A. B., Kennedy, J., Kowalski, J., Friesel, R., Mehlman, T., and Maciag, T. (1985) Proc. Natl. Acad. Sci. U. S. A. 82, 6138-6142). Here we report the covalent cross-linking of 125I-ECGF to a polypeptide present on the surface of the plasma membrane of murine lung capillary endothelial cells by the homobifunctional reagent, disuccinimidyl suberate. Cross-linking of cell surface associated 125I-ECGF yields a major polypeptide with an apparent molecular weight of 150,000. Experiments demonstrated that the cross-linked polypeptide complex represents 125I-ECGF covalently bound specifically to a cell surface receptor because: covalent modification of the polypeptide was inhibited by excess, unlabeled ECGF; preincubation of cells with unlabeled ECGF at 37 degrees C significantly reduced cross-linking while incubation at 4 degrees C did not; other polypeptide growth factors do not compete with 125I-ECGF for cross-linking to the ECGF receptor; labeling of the polypeptide did not take place in the absence of DSS; and cells previously shown to have a paucity of ECGF receptors did not yield a cross-linked labeled receptor. These data suggest that the mitogenic events mediated by ECGF occur after occupancy of the specific cell surface polypeptide and suggest that these events are relevant to ECGF-induced signal transduction across the endothelial cell plasma membrane.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Eur Heart JHome page
R Tabibiazar and S.G Rockson
Angiogenesis and the ischaemic heart
Eur. Heart J., June 1, 2001; 22(11): 903 - 918.
[PDF]


Home page
Ann. Thorac. Surg.Home page
P. Pecher and B. A. Schumacher
Angiogenesis in ischemic human myocardium: clinical results after 3 years
Ann. Thorac. Surg., May 1, 2000; 69(5): 1414 - 1419.
[Abstract] [Full Text] [PDF]


Home page
CirculationHome page
B. Schumacher, P. Pecher, B. U. von Specht, and Th. Stegmann
Induction of Neoangiogenesis in Ischemic Myocardium by Human Growth Factors : First Clinical Results of a New Treatment of Coronary Heart Disease
Circulation, February 24, 1998; 97(7): 645 - 650.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. M. Neilson and R. Friesel
Ligand-independent Activation of Fibroblast Growth Factor Receptors by Point Mutations in the Extracellular, Transmembrane, and Kinase Domains
J. Biol. Chem., October 4, 1996; 271(40): 25049 - 25057.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. Tanahashi, M. Suzuki, T. Imamura, and Y. Mitsui
Identification of a 79-kDa Heparin-binding Fibroblast Growth Factor (FGF) Receptor in Rat Hepatocytes and Its Correlation with the Different Growth Responses to FGF-1 between Hepatocyte Subpopulations
J. Biol. Chem., April 5, 1996; 271(14): 8221 - 8227.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. M. Neilson and R. E. Friesel
Constitutive Activation of Fibroblast Growth Factor Receptor-2 by a Point Mutation Associated with Crouzon Syndrome
J. Biol. Chem., November 3, 1995; 270(44): 26037 - 26040.
[Abstract] [Full Text] [PDF]


Home page
J. Thorac. Cardiovasc. Surg.Home page
R. Fasol, B. Schumacher, K. Schlaudraff, K.-H. Hauenstein, and R. Seitelberger
Experimental use of a modified fibrin glue to induce site-directed angiogenesis from the aorta to the heart
J. Thorac. Cardiovasc. Surg., June 1, 1994; 107(6): 1432 - 1439.
[Abstract] [Full Text]


Home page
ScienceHome page
J. Thompson, K. Anderson, J. DiPietro, J. Zwiebel, M Zametta, W. Anderson, and T Maciag
Site-directed neovessel formation in vivo
Science, September 9, 1988; 241(4871): 1349 - 1352.
[Abstract] [PDF]


Home page
ScienceHome page
J Folkman and M Klagsbrun
Angiogenic factors
Science, January 23, 1987; 235(4787): 442 - 447.
[Abstract] [PDF]


Home page
ScienceHome page
M Jaye, R Howk, W Burgess, G. Ricca, I. Chiu, M. Ravera, S. O'Brien, W. Modi, T Maciag, and W. Drohan
Human endothelial cell growth factor: cloning, nucleotide sequence, and chromosome localization
Science, August 1, 1986; 233(4763): 541 - 545.
[Abstract] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1986 by the American Society for Biochemistry and Molecular Biology.