Neuroglycan C, a Novel Membrane-spanning Chondroitin Sulfate Proteoglycan That Is Restricted to the Brain (*)

@article{Watanabe1995NeuroglycanCA,
  title={Neuroglycan C, a Novel Membrane-spanning Chondroitin Sulfate Proteoglycan That Is Restricted to the Brain (*)},
  author={Eiji Watanabe and Nobuaki Maeda and Fumiko Matsui and Yoichi Kushima and Masaharu Noda and Atsuhiko Oohira},
  journal={The Journal of Biological Chemistry},
  year={1995},
  volume={270},
  pages={26876 - 26882}
}
Monoclonal antibodies were raised to membrane-bound proteoglycans derived from rat brain, and four monoclonal antibodies that recognized a 150-kDa chondroitin sulfate proteoglycan with a core glycoprotein of 120 kDa were obtained. Immunohistological study revealed that the proteoglycan was associated with developing neurons. We screened rat brain cDNA libraries using the four monoclonal antibodies and isolated overlapping cDNA clones that encoded the entire core protein of 514 amino acids plus… 

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Neuroglycan C, a brain-specific part-time proteoglycan, with a particular multidomain structure
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Results obtained from immunohistological, cell biological and biochemical experiments suggest that NGC is involved in neuronal circuit formation in the central nervous system and the proposed functions of NGC in the brain are verified.
Glycosylation Site for Chondroitin Sulfate on the Neural Part-time Proteoglycan, Neuroglycan C*
TLDR
The CS glycosylation was not necessary for intracellular trafficking of NGC to the cell surface at least in Neuro 2a cells, suggesting that the addition of CS chains to the NGC core protein is regulated in a manner different from that of other CS proteoglycans.
Phosphorylation of Neuroglycan C, a Brain-specific Transmembrane Chondroitin Sulfate Proteoglycan, and Its Localization in the Lipid Rafts*
TLDR
This is the first report to demonstrate that NGC can be phosphorylated both intracellularly and pericellularly, and the findings suggest that a kinase with a specificity similar to that of casein kinase II is responsible for the NGC ectodomain phosphorylation.
Neuroglycan C, A Brain-Specific Chondroitin Sulfate Proteoglycan, Interacts with Pleiotrophin, A Heparin-Binding Growth Factor
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Results suggest that NGC interacts with PTN, and pleiotrophin bound to both chondroitin sulfate-bearing NGC and chONDroitinase-treated NGC prepared from the neonatal rat brain.
A membrane‐bound heparan sulfate proteoglycan that is transiently expressed on growing axons in the rat brain
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The data suggest that H5‐PG is a glycoconjugate on axonal surface that is involved in axonal outgrowth and/or synaptogenesis in the central nervous system.
Developmental changes in the biochemical and immunological characters of the carbohydrate moiety of neuroglycan C, a brain-specific chondroitin sulfate proteoglycan
TLDR
Findings indicate that the structure of the carbohydrate moiety of NGC is developmentally regulated, and differs from those of neurocan and phosphacan, and may be partly implicated in the modulation of neuronal cell recognition during brain development.
Ectodomain shedding of neuroglycan C, a brain‐specific chondroitin sulfate proteoglycan, by TIMP‐2‐ and TIMP‐3‐sensitive proteolysis
TLDR
Both EGF‐like and neurite outgrowth‐promoting activity of the NGC ectodomain may be regulated by this proteolytic processing.
Expression and identification of a new splice variant of neuroglycan C, a transmembrane chondroitin sulfate proteoglycan, in the human brain
TLDR
The expression of NGC in the human brain, mainly in the hippocampus, was studied and some observations were confirmed by conducting experiments using rat brain, and NGC‐IV, which was first found in the present study, had the shortest cytoplasmic domain among the four variants.
Neuroglycan C, a neural tissue-specific transmembrane chondroitin sulfate proteoglycan, in retinal neural network formation.
TLDR
The results show spatiotemporal expression patterns of NGC, and suggest that it plays a role in the formation of neural networks in retinal development.
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