Proteolipid protein 1
- OMIM: 300401
- UniProt: P60201
The proteolipid protein 1 - called because of its strong hydrophobic properties as lipophilin - is based on the mass most abundant protein of the myelin sheath of nerve cells. It is a transmembrane protein with four transmembrane domains.
In the context of phylogenetic differentiation, it was exceptionally well " preserved " so that this type of protein in mice and humans is identical to 100 percent.
It has a molecular mass of 30,000 daltons as a membrane protein, and causes a stabilization of the myelin sheath. The proteolipid protein is characterized by a high content of apolar amino acids. This structural feature and the covalent binding of fatty acids explains his unusually good solubility in organic solvents, which corresponds to the part of lipids.
Point mutations in the PLP gene can give rise to pronounced myelination in mice as in humans. In humans, these manifest as Pelizaeus -Merzbacher disease ( PMK ), a condition that is referred to as a pup in dogs shaking. Another possible consequence is a spastic paraplegia.
But not only mutations or lacking in the PLP gene, but also duplications of the gene lead to a lighter form of this X-linked inherited disease. Triplicates or Verfünffachungen of the gene cause a rare, severe form of PMK.
PLP knockout mouse mutants develop initially noticeable, and are significantly older than one year, which has been shown that PLP is not absolutely necessary for myelin formation, but initially only promotes the stability of the myelin membrane. At the age of over a year, it comes as a sign of progressive axonal dysfunction to neurodegenerative symptoms such as ataxia and paralysis.