Abstract

CGT is the key enzyme in the biosynthesis of cerebrosides and sulfatides. It is a glycoprotein residing in the endoplasmic reticulum which catalyzes the transfer of galactose from UDP-galactose to ceramide forming galactocerebroside (GalC). CGT mRNA expression coincides with the presence of GalC and sulfatide, being particularly abundant inoligodendrocytes and Schwann cells during active periods of myelination. Peak expression of the CGT gene occurs during the myelination period between p10 and p30. The CGT–/– mouse is a model for a new form of dysmyelinosis. The deficiency of galactocerebrosides and sulfatides leads to an increased fluidity, permeability, and impaired packing of the myelin lipid bilayer of the internodal membrane system. This may be the most important reason for the breakdown of saltatory conductance of myelinated axons in CGT–/– mice.

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