Cloning and chromosomal mapping of the human gene of neuroglycan C (NGC), a neural transmembrane chondroitin sulfate proteoglycan with an EGF module

@article{Yasuda1998CloningAC,
  title={Cloning and chromosomal mapping of the human gene of neuroglycan C (NGC), a neural transmembrane chondroitin sulfate proteoglycan with an EGF module},
  author={Yoko Yasuda and Yoshihito Tokita and Sachiko Aono and Fumiko Matsui and Takao Ono and Shin‐ichi Sonta and Eiji Watanabe and Yasuo Nakanishi and Atsuhiko Oohira},
  journal={Neuroscience Research},
  year={1998},
  volume={32},
  pages={313-322}
}
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.
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.
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.
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.
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.
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.
Neuroglycan C, a brain-specific part-time proteoglycan, with a particular multidomain structure
TLDR
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.
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.
Neuroglycan C, a novel member of the neuregulin family.
Neuroglycan C Is a Novel Midkine Receptor Involved in Process Elongation of Oligodendroglial Precursor-like Cells*
TLDR
It is concluded that neuroglycan C is a novel component of midkine receptors involved in process elongation in undifferentiated bipolar CG-4 cells.
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References

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Neuroglycan C, a Novel Membrane-spanning Chondroitin Sulfate Proteoglycan That Is Restricted to the Brain (*)
TLDR
The sequence of the proteoglycan did not exhibit significant homology to any other known protein, indicating that the proteglycan, designated neuroglycan C, is a novel integral membrane proteogly can.
Multiple domains of the large fibroblast proteoglycan, versican.
TLDR
It is suggested that the large fibroblast proteoglycan, herein referred to as versican, may function in cell recognition, possibly by connecting extracellular matrix components and cell surface glycoproteins.
Chicken Acidic Leucine-rich EGF-like Domain Containing Brain Protein (CALEB), a Neural Member of the EGF Family of Differentiation Factors, Is Implicated in Neurite Formation
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.
Identification and synthesis of a recognition signal for the attachment of glycosaminoglycans to proteins.
TLDR
The results suggest that the proteoglycan recognition consensus sequence for the attachment of glycosaminoglycans to core proteins consists of acidic amino acids closely followed by the tetrapeptide Ser-Gly-Xaa-Gy, where Xaa is any amino acid.
Identification of Heregulin, a Specific Activator of p185erbB2
TLDR
Several complementary DNA clones encoding related HRGs were identified, all of which are similar to proteins in the epidermal growth factor family, and heregulin transcripts were identified in several normal tissues and cancer cell lines.
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