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The chondroitin sulfate proteoglycans neurocan, brevican, phosphacan, and versican are differentially regulated following spinal cord injury
Neurocan Is Upregulated in Injured Brain and in Cytokine-Treated Astrocytes
It is shown that the CSPG neurocan, which is expressed in the CNS, exerts a repulsive effect on growing cerebellar axons and raises the possibility that neurocan interferes with axonal regeneration after CNS injury.
Fibrinogen Triggers Astrocyte Scar Formation by Promoting the Availability of Active TGF-β after Vascular Damage
Results identify fibrinogen as a primary astrocyte activation signal, provide evidence that deposition of inhibitory proteoglycans is induced by a blood protein that leaks in the CNS after vasculature rupture, and point to TGF-β as a molecular link between vascular permeability and scar formation.
The neuronal chondroitin sulfate proteoglycan neurocan binds to the neural cell adhesion molecules Ng-CAM/L1/NILE and N-CAM, and inhibits neuronal adhesion and neurite outgrowth
- D. Friedlander, P. Milev, L. Karthikeyan, R. Margolis, R. U. Margolis, M. Grumet
- Biology, ChemistryThe Journal of cell biology
- 1 May 1994
Experiments using anti-Ng-CAM antibodies as a substrate indicate that neurocan has a direct inhibitory effect on neuronal adhesion and neurite growth, and a role for chondroitin sulfate in this process is indicated, although the core glycoprotein also has binding activity.
Mice Deficient for Tenascin-R Display Alterations of the Extracellular Matrix and Decreased Axonal Conduction Velocities in the CNS
Observations indicate an essential role for TN-R in the formation of perineuronal nets and in normal conduction velocity of optic nerve in mutant mice generated by homologous recombination using embryonic stem cells.
Interactions of the chondroitin sulfate proteoglycan phosphacan, the extracellular domain of a receptor-type protein tyrosine phosphatase, with neurons, glia, and neural cell adhesion molecules
The studies suggest that by binding to neural cell adhesion molecules, and possibly also by competing for ligands of the transmembrane phosphatase, phosphacan may play a major role in modulating neuronal and glial adhesion, neurite growth, and signal transduction during the development of the central nervous system.
Demonstration of mammalian protein O-mannosyltransferase activity: coexpression of POMT1 and POMT2 required for enzymatic activity.
A method to detect protein O-mannosyltransferase activity in mammalian cells was developed and it was shown that coexpression of both PomT1 and POMT2 was necessary for the enzyme activity, but expression of either POM t1 or POMt2 alone was insufficient.
Postnatal development of perineuronal nets in wild‐type mice and in a mutant deficient in tenascin‐R
It is concluded that the lack of TN‐R initially and continuously disturbs the molecular scaffolding of extracellular matrix components in perineuronal nets and may interfere with the development of the specific micromilieu of the ensheathed neurons and adjacent glial cells and may also permanently change their functional properties.
Differential regulation of expression of hyaluronan-binding proteoglycans in developing brain: aggrecan, versican, neurocan, and brevican.
Striking and distinctive changes in the concentrations of the different members of this family of structurally related proteoglycans in developing brain, including changes in opposite directions for versican mRNA splice variants, indicate that the individual proteoglyCans and their isoforms probably serve unique functions during nervous tissue histogenesis.
Phosphacan, a chondroitin sulfate proteoglycan of brain that interacts with neurons and neural cell-adhesion molecules, is an extracellular variant of a receptor-type protein tyrosine phosphatase.
- P. Maurel, U. Rauch, M. Flad, R. Margolis, R. U. Margolis
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 29 March 1994
These proteoglycans may modulate cell interactions and other developmental processes in nervous tissue through heterophilic binding to cell-surface and extracellular matrix molecules, and by competition with ligands of the transmembrane phosphatase.