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J. Biol. Chem., Vol. 275, Issue 21, 15741-15748, May 26, 2000

This Article Full Text Full Text (PDF) All Versions of this Article: 275/21/15741    most recent M903271199v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Köhl, R. Articles by Kiefer, P. Search for Related Content PubMed PubMed Citation Articles by Köhl, R. Articles by Kiefer, P. Social Bookmarking                      What's this?

Cysteine-rich Fibroblast Growth Factor Receptor Alters Secretion and Intracellular Routing of Fibroblast Growth Factor 3^*

Roman Köhl, Marianne Antoine, Bradley B. Olwin, Clive Dickson^§, and Paul Kiefer^¶

From Ruhr-Universität Bochum, Medizinische Fakultät, Abteilung für Virologie, Universitätsstrasse 150, Gebäuole MA 6/130, D-44780 Bochum, Germany, the  Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, Colorado 80308, and ^§ Imperial Cancer Research Fund Laboratories, 44 Lincoln's Inn Fields, London WC2A 3PX, United Kingdom

Expression of the cysteine-rich fibroblast growth factor (FGF) receptor (CFR) in COS-1 cells strongly inhibits the secretion of co-expressed FGF3. By using a column retention assay and affinity chromatography, we demonstrate that at physiological salt concentrations FGF3 binds with strong affinity to CFR in vivo and in vitro. Furthermore, to show that FGF3 binds to CFR in vivo, truncation mutants of CFR with changed subcellular distributions were shown to cause a similar redistribution of FGF3. Although CFR is a 150-kDa integral membrane glycoprotein that is primarily located in the Golgi apparatus, we show here that in COS-1 cells a substantial proportion of CFR is secreted. This is due to a carboxyl-terminal proteolytic cleavage that releases the intraluminal portion of the protein for secretion. However, the apparent size of the integral membrane and secreted CFR appears similar, since the loss of protein mass is balanced by a gain of complex carbohydrates. The released CFR is associated with the extracellular matrix through its affinity for glycosaminoglycans. These findings show that CFR can modulate the secretion of FGF3 and may control its biological activity by regulating its secretion.

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