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J. Biol. Chem., Vol. 278, Issue 26, 24164-24173, June 27, 2003

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Phosphacan Short Isoform, a Novel Non-proteoglycan Variant of Phosphacan/Receptor Protein Tyrosine Phosphatase-, Interacts with Neuronal Receptors and Promotes Neurite Outgrowth^*

Jeremy Garwood  , Nicolas Heck , Frank Reichardt ¶ and Andreas Faissner ||

From the Laboratoire de Neurobiologie du Développement et de la Régénération, CNRS Centre de Neurochimie, 67084 Strasbourg, France, ^¶Max Planck Institute for Medical Research, 69120 Heidelberg, Germany, and ^||Department of Cell Morphology and Molecular Neurobiology, Ruhr-University, 44780 Bochum, Germany

Phosphacan, one of the principal proteoglycans in the extracellular matrix of the central nervous system, is implicated in neuron-glia interactions associated with neuronal differentiation and myelination. We report here the identification of a novel truncated form of phosphacan, phosphacan short isoform (PSI), that corresponds to the N-terminal carbonic anhydrase- and fibronectin type III-like domains and half of the spacer region. The novel cDNA transcript was isolated by screening of a neonatal brain cDNA expression library using a polyclonal antibody raised against phosphacan. Expression of this transcript in vivo was confirmed by Northern blot hybridization. Analysis of brain protein extracts reveals the presence of a 90-kDa glycosylated protein in the phosphate-buffered saline-insoluble 100,000 x g fraction that reacts with antisera against both phosphacan and a recombinant PSI protein and that has the predicted N-terminal sequence. This protein is post-translationally modified with oligosaccharides, including the HNK-1 epitope, but, unlike phosphacan, it is not a proteoglycan. The expression of the PSI protein varies during central nervous system development in a fashion similar to that observed for phosphacan, being first detected around embryonic day 16 and then showing a dramatic increase in expression to plateau around the second week post-natal. Both the native and recombinant PSI protein can interact with the Ig cell adhesion molecules, F3/contactin and L1, and in neurite outgrowth assays, the PSI protein can promote outgrowth of cortical neurons when used as a coated substrate. Hence, the identification of this novel isoform of phosphacan/receptor protein tyrosine phosphatase- provides a new component in cell-cell and cell-extracellular matrix signaling events in which these proteins have been implicated.

Received for publication, November 18, 2002 , and in revised form, March 27, 2003.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AJ428208.

^* This work was supported in part by the CNRS, the German Research Council (DFG, Fa 159/11-1,2,3), the International Spinal Research Trust, and the Association pour la Recherche contre le Cancer. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Awarded a Poste rouge from the CNRS during part of this work. To whom correspondence should be addressed. Tel.: 33-3-88-45-66-53; Fax: 33-3-88-41-17-80; E-mail: garwood{at}neurochem.u-strasbg.fr.

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