Expression and identification of a new splice variant of neuroglycan C, a transmembrane chondroitin sulfate proteoglycan, in the human brain

@article{Aono2006ExpressionAI,
  title={Expression and identification of a new splice variant of neuroglycan C, a transmembrane chondroitin sulfate proteoglycan, in the human brain},
  author={Sachiko Aono and Yoshihito Tokita and Yoko Yasuda and Kanako Hirano and Shinobu Yamauchi and Takuya Shuo and Fumiko Matsui and Hiroomi Keino and Akiko Kashiwai and Noriko Kawamura and Atsuyoshi Shimada and Masao Kishikawa and Mitsuoki Asai and Atsuhiko Oohira},
  journal={Journal of Neuroscience Research},
  year={2006},
  volume={83}
}
Neuroglycan C (NGC) is a transmembrane chondroitin sulfate proteoglycan with an EGF module. We studied the expression of NGC in the human brain, mainly in the hippocampus, and confirmed some observations by conducting experiments using rat brain. In humans, NGC mRNA was expressed exclusively in the brain, especially in the immature brain. The telencephalon, including the hippocampus and neocortex, showed strong mRNA expression. NGC was immunolocalized to neuropils in the hippocampus and… 
Ectodomain shedding of neuroglycan C, a brain‐specific chondroitin sulfate proteoglycan, by TIMP‐2‐ and TIMP‐3‐sensitive proteolysis
TLDR
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TLDR
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References

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Genomic Organization and Expression Pattern of Mouse Neuroglycan C in the Cerebellar Development*
TLDR
Western blot analysis demonstrated that, although N GC in the immature cerebellum existed in a proteoglycan form, most NGC in the mature Cerebellum did not bear chondroitin sulfate chain(s), indicating that NGC is a typical part-time proteoglyca.
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.
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.
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TLDR
This review mainly summarizes recent studies on the involvement of these three classes of proteoglycan in cell-cell and cell-substratum interactions during the brain development.
Brain development and multiple molecular species of proteoglycan
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TLDR
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TLDR
CDNA cloning indicates that CALEB is a multidomain protein that consists of an NH2-terminal glycosylation region, a leucine-proline–rich segment, an acidic box, a single EGF-like domain, a transmembrane, and a short cytoplasmic stretch.
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TLDR
It is demonstrated that CALEB mRNA is dynamically regulated after optic nerve lesion and that this mRNA is expressed in most developing and in one-third of the few regenerating retinal ganglion cells.
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TLDR
This enzyme has now been shown to restore synaptic plasticity in the visual cortex of adult rats by disrupting perineuronal nets, which contain high levels of chondroitin sulphate proteoglycans (CS‐PGs) and are expressed postnatally around groups of certain neurons in the normal CNS.
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