Document Detail


Neurexin IV, caspr and paranodin--novel members of the neurexin family: encounters of axons and glia.
MedLine Citation:
PMID:  9786343     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Axonal insulation is of key importance for the proper propagation of action potentials. In Drosophila and other invertebrates, it has recently been demonstrated that septate junctions play an essential role in axonal insulation or blood-brain-barrier formation. Neurexin IV, a molecular component of Drosophila septate junctions, has been shown to be essential for axonal insulation in the PNS in embryos and larvae. Interestingly, a vertebrate homolog of Neurexin IV, caspr--also named paranodin--has been shown to localize to septate-like junctional structures. These vertebrate junctions are localized to the paranodal region of the nodes of Ranvier, between axons and Schwann cells. Caspr/paranodin might play an important role in barrier formation, and link neuronal membrane components with the axonal cytoskeletal network.
Authors:
H J Bellen; Y Lu; R Beckstead; M A Bhat
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.; Review    
Journal Detail:
Title:  Trends in neurosciences     Volume:  21     ISSN:  0166-2236     ISO Abbreviation:  Trends Neurosci.     Publication Date:  1998 Oct 
Date Detail:
Created Date:  1998-12-18     Completed Date:  1998-12-18     Revised Date:  2009-11-03    
Medline Journal Info:
Nlm Unique ID:  7808616     Medline TA:  Trends Neurosci     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  444-9     Citation Subset:  IM    
Affiliation:
Dept of Human and Molecular Genetics, Howard Hughes Medical Institute, Baylor College of Medicine, Houston, TX 77030, USA.
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MeSH Terms
Descriptor/Qualifier:
Action Potentials / physiology
Animals
Axons / metabolism*,  ultrastructure
Blood-Brain Barrier / physiology*
Cell Adhesion Molecules, Neuronal*
Drosophila / physiology
Drosophila Proteins*
Insect Proteins / physiology*
Membrane Glycoproteins / physiology*
Membrane Proteins / physiology*
Molecular Structure
Myelin Sheath / physiology
Nerve Tissue Proteins / physiology*
Neuroglia / metabolism*,  ultrastructure
Neuropeptides / physiology*
Neurotransmitter Agents / secretion
Ranvier's Nodes / ultrastructure
Receptors, Cell Surface / physiology*
Synaptic Membranes / ultrastructure
Chemical
Reg. No./Substance:
0/Cell Adhesion Molecules, Neuronal; 0/Drosophila Proteins; 0/Insect Proteins; 0/Membrane Glycoproteins; 0/Membrane Proteins; 0/Nerve Tissue Proteins; 0/Neuropeptides; 0/Neurotransmitter Agents; 0/Nrx protein, Drosophila; 0/Receptors, Cell Surface

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