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Lierheimer, R; Kunz, B; Vogt, L; Savoca, R; Brodbeck, U; Sonderegger, P (1997). The neuronal cell-adhesion molecule axonin-1 is specifically released by an endogenous glycosylphosphatidylinositol-specific phospholipase. FEBS Journal, 243(1-2):502-510.

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Abstract

Axonin-1, a member of the immunoglobulin/fibronectin type-III family of cell-adhesion molecules, occurs both as a glycosylphosphatidylinositol-(glycosylPtdIns)-anchored membrane-bound and a soluble form. In vivo observations show that the major part of axonin-1 is found in the soluble fraction and that soluble axonin-1 perturbs neurite fasciculation and pathfinding in the developing chicken embryo. This has prompted further investigations into the mechanism of the axonin-1 release. We demonstrate here that axonin-1 released from dorsal root ganglion neurons contains ethanolamine and inositol, components of the glycosylPtdIns anchor. Secreted axonin-1 does not exhibit the cross-reacting determinant epitope, an indication that the cleavage of the anchor is not mediated by a phosphatidylinositol-specific phospholipase C. Treatment of dorsal root ganglion neurons with 1,10-phenanthroline, an inhibitor of glycosylPtdIns-specific phospholipase D, reduces the release of axonin-1 by 56%. Moreover, glycosylPtdIns-specific phospholipase D activity was detected in dorsal root ganglion neurons and brain. These results suggest that axonin-1 is released from the membrane by an endogenously expressed glycosylPtdIns-specific phospholipase D in vivo. With domain-swaping experiments between axonin-1 and its non-released relative F11, deletion mutants and monoclonal antibodies, we demonstrate that the fourth fibronectin type-III-like domain of axonin-1 is required for the generation of the soluble form of axonin-1.

Item Type:Journal Article, refereed
Communities & Collections:04 Faculty of Medicine > Institute of Biochemistry
07 Faculty of Science > Institute of Biochemistry
DDC:570 Life sciences; biology
Language:English
Date:15 January 1997
Deposited On:11 Feb 2008 13:20
Last Modified:27 Nov 2013 18:08
Publisher:Wiley-Blackwell
ISSN:0014-2956
Funders:Swiss National Science Foundation Grant Nrs. 3100-039209.93 and 3100-033815.92/2, Sandoz-Stiftung, Julius-Klaus-Stiftung, Fonds für medizinische Forschung der Universität Zürich
Publisher DOI:10.1111/j.1432-1033.1997.0502a.x
Related URLs:http://content.febsjournal.org/cgi/content/abstract/243/1/502
PubMed ID:9030778
Citations:Web of Science®. Times Cited: 24
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