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…
15 Citations
Ectodomain shedding of neuroglycan C, a brain‐specific chondroitin sulfate proteoglycan, by TIMP‐2‐ and TIMP‐3‐sensitive proteolysis
- BiologyJournal of neurochemistry
- 2007
Both EGF‐like and neurite outgrowth‐promoting activity of the NGC ectodomain may be regulated by this proteolytic processing.
Neuroglycan C, A Brain-Specific Chondroitin Sulfate Proteoglycan, Interacts with Pleiotrophin, A Heparin-Binding Growth Factor
- Biology, ChemistryNeurochemical Research
- 2010
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.
Neuroglycan C Is a Novel Midkine Receptor Involved in Process Elongation of Oligodendroglial Precursor-like Cells*
- BiologyJournal of Biological Chemistry
- 2006
It is concluded that neuroglycan C is a novel component of midkine receptors involved in process elongation in undifferentiated bipolar CG-4 cells.
Differential neuroglycan C expression during retinal degeneration in Rpe65−/− mice
- BiologyMolecular vision
- 2008
During retinal degeneration in Rpe65−/− mice, NGC expression is induced in the neural retina, but not in the RPE, where NGC is expressed at highest levels.
Identification and Functions of Chondroitin Sulfate in the Milieu of Neural Stem Cells*
- BiologyJournal of Biological Chemistry
- 2006
Results suggest that brain-specific chondroitin sulfate proteoglycans are involved in the proliferation of neural stem cells as a group of cell microenvironmental factors.
Opposing functions of chondroitin sulfate and heparan sulfate during early neuronal polarization
- BiologyNeuroscience
- 2010
On the Modulatory Roles of Neuregulins/ErbB Signaling on Synaptic Plasticity
- BiologyInternational journal of molecular sciences
- 2019
Current evidence points to a central role of NRGs/ErbB receptors in controlling glutamatergic LTP/LTD and GABAergic LTD at hippocampal CA3–CA1 synapses, thus supporting that NRGs or ErbB signaling is essential for proper brain functions, cognitive processes, and complex behaviors.
Demystifying the extracellular matrix and its proteolytic remodeling in the brain: structural and functional insights
- Biology, ChemistryCellular and Molecular Life Sciences
- 2019
This review has compiled the current knowledge about the structure and function of important ECM molecules in the brain and their proteolytic remodeling by matrix metalloproteinases and other enzymes, highlighting the special structures they form.
References
SHOWING 1-10 OF 23 REFERENCES
Genomic Organization and Expression Pattern of Mouse Neuroglycan C in the Cerebellar Development*
- BiologyThe Journal of Biological Chemistry
- 2000
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.
Cloning and chromosomal mapping of the human gene of neuroglycan C (NGC), a neural transmembrane chondroitin sulfate proteoglycan with an EGF module
- BiologyNeuroscience Research
- 1998
Phosphorylation of Neuroglycan C, a Brain-specific Transmembrane Chondroitin Sulfate Proteoglycan, and Its Localization in the Lipid Rafts*
- Biology, ChemistryThe Journal of Biological Chemistry
- 2002
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*
- BiologyJournal of Biological Chemistry
- 2004
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.
Molecular interactions of neural chondroitin sulfate proteoglycans in the brain development.
- Biology, ChemistryArchives of biochemistry and biophysics
- 2000
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.
Proteoglycans in the developing brain: new conceptual insights for old proteins.
- Biology, ChemistryPhysiological reviews
- 2000
This review summarizes the most recent data on structures and functions of brain proteoglycans and focuses on new physiological concepts for their potential roles in the developing central nervous system.
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
- BiologyThe Journal of cell biology
- 1997
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.
CALEB Binds via Its Acidic Stretch to the Fibrinogen-like Domain of Tenascin-C or Tenascin-R and Its Expression Is Dynamically Regulated after Optic Nerve Lesion*
- BiologyThe Journal of Biological Chemistry
- 2001
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.
Chondroitin sulphate proteoglycans: preventing plasticity or protecting the CNS?
- BiologyJournal of anatomy
- 2004
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.