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. 1996 Sep 17;93(19):10046-50.
doi: 10.1073/pnas.93.19.10046.

Lipid thioesters derived from acylated proteins accumulate in infantile neuronal ceroid lipofuscinosis: correction of the defect in lymphoblasts by recombinant palmitoyl-protein thioesterase

J Y Lu  1 , L A Verkruyse, S L Hofmann
Affiliations

Lipid thioesters derived from acylated proteins accumulate in infantile neuronal ceroid lipofuscinosis: correction of the defect in lymphoblasts by recombinant palmitoyl-protein thioesterase

J Y Lu et al. Proc Natl Acad Sci U S A. .

Abstract

Palmitoyl-protein thioesterase is a lysosomal long-chain fatty acyl hydrolase that removes fatty acyl groups from modified cysteine residues in proteins. Mutations in palmitoyl-protein thioesterase were recently found to cause the neurodegenerative disorder infantile neuronal ceroid lipofuscinosis, a disease characterized by accumulation of amorphous granular deposits in cortical neurons, leading to blindness, seizures, and brain death by the age of three. In the current study, we demonstrate that [35S]cysteine-labeled lipid thioesters accumulate in immortalized lymphoblasts of patients with infantile neuronal ceroid lipofuscinosis. The accumulation in cultured cells is reversed by the addition of recombinant palmitoyl-protein thioesterase that is competent for lysosomal uptake through the mannose-6-phosphate receptor. The [35S]cysteine-labeled lipids are substrates for palmitoyl-protein thioesterase in vitro, and their formation requires prior protein synthesis. These data support a role for palmitoyl-protein thioesterase in the lysosomal degradation of S-acylated proteins and define a major new pathway for the catabolism of acylated proteins in the lysosome.

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References

    1. J Biol Chem. 1996 Jun 28;271(26):15831-6 - PubMed
    1. J Biol Chem. 1996 Aug 9;271(32):19191-8 - PubMed
    1. J Biol Chem. 1984 Apr 25;259(8):4934-40 - PubMed
    1. Am J Med Genet Suppl. 1988;5:21-6 - PubMed
    1. J Biol Chem. 1989 May 15;264(14):8222-9 - PubMed

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