Mice deficient in the lysosomal enzyme palmitoyl-protein thioesterase 1 (PPT1) display a complex retinal phenotype

Sci Rep. 2019 Oct 2;9(1):14185. doi: 10.1038/s41598-019-50726-8.

Abstract

Neuronal ceroid lipofuscinosis (NCL) type 1 (CLN1) is a neurodegenerative storage disorder caused by mutations in the gene encoding the lysosomal enzyme palmitoyl-protein thioesterase 1 (PPT1). CLN1 patients suffer from brain atrophy, mental and motor retardation, seizures, and retinal degeneration ultimately resulting in blindness. Here, we performed an in-depth analysis of the retinal phenotype of a PPT1-deficient mouse, an animal model of this condition. Reactive astrogliosis and microgliosis were evident in mutant retinas prior to the onset of retinal cell loss. Progressive accumulation of storage material, a pronounced dysregulation of various lysosomal proteins, and accumulation of sequestosome/p62-positive aggregates in the inner nuclear layer also preceded retinal degeneration. At advanced stages of the disease, the mutant retina was characterized by a significant loss of ganglion cells, rod and cone photoreceptor cells, and rod and cone bipolar cells. Results demonstrate that PPT1 dysfunction results in early-onset pathological alterations in the mutant retina, followed by a progressive degeneration of various retinal cell types at relatively late stages of the disease. Data will serve as a reference for future work aimed at developing therapeutic strategies for the treatment of retinal degeneration in CLN1 disease.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Lysosomes / metabolism
  • Mice
  • Mice, Inbred C57BL
  • Phenotype*
  • Photoreceptor Cells / metabolism
  • Photoreceptor Cells / pathology
  • Retinal Bipolar Cells / metabolism
  • Retinal Bipolar Cells / pathology
  • Retinal Degeneration / genetics*
  • Retinal Degeneration / metabolism
  • Retinal Degeneration / pathology
  • Retinal Ganglion Cells / metabolism
  • Retinal Ganglion Cells / pathology
  • Thiolester Hydrolases / deficiency
  • Thiolester Hydrolases / genetics*
  • Thiolester Hydrolases / metabolism

Substances

  • Thiolester Hydrolases
  • palmitoyl-protein thioesterase