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Related Experiment Videos

Differential expression of MAG isoforms during development.

L Pedraza1, A B Frey, B L Hempstead

  • 1Department of Cell Biology, New York University Medical School 10016.

Journal of Neuroscience Research
|June 1, 1991
PubMed
Summary
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Myelin-associated glycoproteins (MAG) have two isoforms, L-MAG and S-MAG, with distinct developmental and tissue-specific expression. L-MAG plays a common role in early myelin formation in both CNS and PNS, while S-MAG predominates in adults.

Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Myelin-associated glycoproteins (MAG) are crucial for cell interactions between myelinating cells (oligodendrocytes and Schwann cells) and axons.
  • MAG exists in two main isoforms: large MAG (L-MAG) and small MAG (S-MAG), which are developmentally regulated.

Purpose of the Study:

  • To investigate the tissue-specific and developmental alternative splicing of MAG isoforms.
  • To clarify the expression patterns and potential roles of L-MAG and S-MAG in the central nervous system (CNS) and peripheral nervous system (PNS).

Main Methods:

  • Utilized monospecific antibodies to differentiate between MAG isoforms based on unique epitopes.
  • Analyzed MAG expression in both CNS and PNS tissues across different developmental stages.

Related Experiment Videos

  • Investigated the glycosylation patterns of MAG.

    • Main Results:

    • L-MAG is a major form in the early CNS and persists in adults, while its expression is limited in the adult PNS.
    • S-MAG is the predominant adult isoform in both CNS and PNS.
    • A developmentally regulated, higher-molecular-weight glycosylation variant of MAG was identified in the PNS.
    • MAG contains both N-linked and O-linked sugars, suggesting developmental modulation of function.

    Conclusions:

    • L-MAG expression is not exclusive to the CNS and likely plays a shared role in early myelination by both oligodendrocytes and Schwann cells.
    • Alternative splicing and glycosylation of MAG may regulate its function during myelinogenesis.