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MAL, a proteolipid in glycosphingolipid enriched domains: functional implications in myelin and beyond

M Frank1

  • 1Brain Research Institute, Department of Neuromorphology, University of Zurich, Switzerland. frankm03@doc.mssm.edu

Progress in Neurobiology
|March 30, 2000
PubMed

Insights

Myelin and lymphocyte protein MAL (VIP17/MVP17) is crucial for myelin formation and is found in T-cells and epithelial cells. MAL protein interacts with glycosphingolipids, influencing cell signaling and membrane properties.

Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Myelin and lymphocyte protein MAL (VIP17/MVP17) is a 17 kD proteolipid with four transmembrane domains.
  • MAL protein is expressed in myelinating cells (oligodendrocytes, Schwann cells) and T-cells, as well as kidney, stomach, and thyroid epithelial cells.

Purpose of the Study:

  • To investigate the localization and function of MAL protein in the nervous system and epithelial cells.
  • To explore the association of MAL with glycosphingolipids and its role in membrane microdomains.

Main Methods:

  • Cloning of MAL cDNA from human T-cells, rat oligodendrocytes, and MDCK cell line.
  • Analysis of MAL protein expression and localization in different cell types.
  • Copurification studies to assess the association of MAL with glycosphingolipids.

Main Results:

  • MAL expression in the nervous system parallels myelin formation, with predominant localization in compact myelin.
  • Outside the nervous system, MAL is found in the apical plasma membrane of epithelial cells, co-enriched with specific glycosphingolipids.
  • MAL copurifies with glycosphingolipids in detergent-insoluble domains, suggesting functional interactions.

Conclusions:

  • MAL plays a role in the formation, stabilization, and maintenance of glycosphingolipid-enriched membrane microdomains.
  • MAL contributes to specific membrane properties in both myelin and epithelial cells.
  • MAL-glycosphingolipid complexes may be involved in signaling, cell differentiation, and apical sorting.

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