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Papers In Press, published online ahead of print April 16, 2003
LNDR, Centre de Neurochimie, Strasbourg 67084
Corresponding Author: garwood{at}neurochem.u-strasbg.fr
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 typeIII-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 hybridisation. Analysis of brain protein extracts reveals the presence of a 90 kD glycosylated protein in the PBS-insoluble 100,000g fraction which 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 CNS development in a fashion similar to that observed for phosphacan, being first detected around E16 and then showing a dramatic increase in expression to plateau around the second week postnatal. Both the native and recombinant PSI protein can interact with the IgCAMs, 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/RPTP-b provides a new component in cell-cell and cell-ECM signaling events in which these proteins have been implicated.
J. Biol. Chem, 10.1074/jbc.M211721200
Submitted on November 18, 2002
Revised on April 16, 2003
Accepted on April 16, 2003
Phosphacan short isoform, a novel non-proteoglycan variant of phosphacan/RPTP-
, interacts with neuronal receptors and promotes neurite outgrowth
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