2001
DOI: 10.1053/ejpn.2000.0439
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Tripeptidyl-peptidase 1 in neuronal ceroid lipofuscinoses and other lysosomal storage disorders

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Cited by 9 publications
(5 citation statements)
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“…Under standard conditions, CHO cells expressing this mutant protein demonstrated $1.8% of the wtTPPI activity, similar to what we have observed previously in the frozen brain tissue of a compound heterozygote toward p.Arg447His and g.3556G4C ($2.2% of the control values) [Wisniewski et al, 2001]. Given that individuals carrying this mutation demonstrate a milder, protracted course of the disease in comparison with the classic phenotype [Wisniewski et al, 1999], our data suggest that even a very low level of TPPI activity is able to slow down the disease process.…”
Section: Discussionsupporting
confidence: 86%
See 1 more Smart Citation
“…Under standard conditions, CHO cells expressing this mutant protein demonstrated $1.8% of the wtTPPI activity, similar to what we have observed previously in the frozen brain tissue of a compound heterozygote toward p.Arg447His and g.3556G4C ($2.2% of the control values) [Wisniewski et al, 2001]. Given that individuals carrying this mutation demonstrate a milder, protracted course of the disease in comparison with the classic phenotype [Wisniewski et al, 1999], our data suggest that even a very low level of TPPI activity is able to slow down the disease process.…”
Section: Discussionsupporting
confidence: 86%
“…Thus, our study indicates that both folding difficulties and impaired specific activity may underlie the disease process in subjects carrying the p.Gly77Arg mutation. The total cellular activity of this variant we found in expressing cells ($1% of wtTPPI value) is similar to the TPPI activity reported in brain tissue from a compound heterozygote (p.Gly77Arg/g.3556G4C), that demonstrated a classic CLN2 phenotype [Wisniewski et al, 2001].…”
Section: Discussionsupporting
confidence: 85%
“…Neuronal ceroid lipofuscinoses can occur by inherited defects in lysosomal proteases, e.g. by an impaired palmitoyl protein thioesterase, that removes fatty acid from lipoproteins or by a defect in tripeptidyl peptidase (182184). …”
Section: Posttranslational Modifications Of Proteins In Neurodegeneramentioning
confidence: 99%
“…These pigments are usually located in lysosomes, as lysosomes normally engulf cytoplasmic components in a process called autophagy and degrade them. In neuronal ceroid lipofuscinoses, however, engulfment continues but degradation of the material is impaired and, therefore, the material accumulates in lysosomes (184). …”
Section: Posttranslational Modifications Of Proteins In Neurodegeneramentioning
confidence: 99%
“…Late-infantile NCL (LINCL) is caused by mutations in tripeptidyl peptidase-1 (TPP1; CLN2) [7375] (reviewed in [76]). TPP1 is a lysosomal serine protease with N-terminal exopeptidase activity, weak endoproteolytic activity, [77, 78] and known structure [79, 80] (reviewed in [76]) (Fig.…”
Section: Ncl-associated Soluble Proteins In the Lysosomementioning
confidence: 99%