NDLI: Myelin P$_{0}$: New Knowledge and New Roles

Content Provider	Springer Nature Link
Author	Eichberg, Joseph
Copyright Year	2002
Abstract	Protein zero (P$_{0}$) is an integral transmembrane glycoprotein that serves as the major protein component of peripheral nerve myelin and is a member of the immunoglobulin (IgG) gene superfamily. As a cell adhesion molecule, P$_{0}$ mediates homophilic adhesive interactions between Schwann cell plasma membranes and is a key structural constituent of both the major dense line and intraperiod line of compact myelin. Both the extracellular and cytoplasmic domains contribute to these interactions and evidence indicates that the post-translational modifications of the molecule, including glycosylation, acylation and phosphorylation, play an important modulatory role in adhesion and likely in the proper trafficking of P$_{0}$ from the endoplasmic reticulum to the plasma membrane as well. Structural and genetic studies indicate that mutations in P$_{0}$ producing human demyelinating diseases probably do so by perturbing or preventing homophilic interactions during myelination, or by producing cellular toxicity or an unstable myelin sheath. A variety of transcription factors, growth factors and neurosteroids both directly and indirectly influence P$_{0}$ gene expression during maturation of the myelinating Schwann cell. Besides its structural function in myelin, P$_{0}$ may have roles in the delivery of other Schwann cell proteins to their proper location, especially at or near nodes of Ranvier, and in neuronal-glial interactions.
Starting Page	1331
Ending Page	1340
Page Count	10
File Format	PDF
ISSN	03643190
Journal	Neurochemical Research
Volume Number	27
Issue Number	11
e-ISSN	15736903
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	2002-01-01
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Neurosciences Neurology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Biochemistry Cellular and Molecular Neuroscience

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