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The reports the crystal structure of the N-terminal domain of TIN2 in complex with TIN2-binding motifs from TPP1 and TRF2, revealing how TIN2 interacts cooperatively with TPP1 and TRF2.
TPP1 cleaves and destabilizes fibrillar amyloid-beta at multiple sites in a time- and pH-dependent manner.
To confirm clinical suspicion of CLN2 disease, the recommended gold standard for laboratory diagnosis is demonstration of deficient TPP1 enzyme activity (in leukocytes, fibroblasts, or dried blood spots) and the identification of causative mutations in each allele of the TPP1/CLN2 gene.
These studies indicate that optimal treatment outcomes for CLN2 disease may require delivery of TPP1 systemically as well as directly to the central nervous system.
TPP1 is overexpressed in hepatocellular carcinoma tissues and significantly correlated with poor prognosis of hepatocellular carcinoma patients.RFX5 acts as a direct positive transcriptional regulator of TPP1 in hepatocellular carcinoma.
TPP1(CLN2) mutation is associated with neuronal ceroid lipofuscinosis.
To our knowledge, our results bring the first evidence of a mechanism that links TPP-1 deficiency and oxidative stress-induced changes in mitochondrial morphology.
hypothesize that loss of function variants abolishing TPP1 enzyme activity lead to CLN2 disease, whereas variants that diminish TPP1 enzyme activity lead to SCAR7
This study demonistrated that the CLN2 gene 4 mutation in late infantile neuronal ceroid lipofuscinosis.
TPP1 mutants utilize the advantages of a zebrafish model for understanding the pathogenesis of late infantile (or classic late infantile neuronal ceroid lipofuscinosis) disease.
The variant juvenile phenotype comprises approximately 50% of CLN2 in South America. The five most frequent South American mutations comprise 66% of pathological alleles.
Gemfibrozil and fenofibrate, Food and Drug Administration-approved lipid-lowering drugs, up-regulate tripeptidyl-peptidase 1 in brain cells via peroxisome proliferator-activated receptor alpha and may have implications in late infantile Batten disease therapy
Studies indicate that TPP-I is the only member of the sedolisin family that has been shown to exhibit tripeptidyl peptidase activity and is related to the fatal hereditary disease, Batten disease.
Intrathecal human tripeptidyl-peptidase 1 administration reduces lysosomal storage in a canine model of late infantile neuronal ceroid lipofuscinosis.
the critical residues in the TPPI catalysis and its structure-function analysis
Data show that most TPPI variants displayed obstructed transport to the lysosomes.
The authors conducted a phase I study of late infantile neuronal ceroid lipofuscinosis using an adenoassociated virus serotype 2 (AAV2) vector containing the deficient CLN2 gene (AAV2(CU)hCLN2).
The clinical, biochemical, and molecular genetic aspects of lysosomal storage disorders are discussed in this review
Data show that three neuronal ceroid lipofuscinoses disease forms with similar tissue pathology are connected at the molecular level: CLN5 polypeptides directly interact with the CLN2 and CLN3 proteins
Missense mutations, R127Q, N286S, and T353P represent novel, previously not described alleles.
telomeres are protected from hyper-resection through the repression of the ATM and ATR kinases by TRF2 and TPP1-bound POT1a/b, respectively.
Rssults suggested that CLN2, CLN3 and CLN5 genes may play an important role in early embryonal neurogenesis.
demonstrated that cells expressing TIN2DeltaTPP1 instead of wild-type TIN2 phenocopy the POT1a,b knockout setting without showing additional phenotypes
TPPI activity becomes crucial for the neuronal functions later in development.
Telomere protection by TPP1/POT1 requires tethering to TIN2.
TPP1 protects telomere integrity and regulates telomerase recruitment to telomeres, thereby preventing early occurrence of degenerative skin pathologies.
TPP1 deletion resulted in the release of POT1a and POT1b from chromatin and loss of these proteins from telomeres, indicating that TPP1 is required for the telomere association of POT1a and POT1b but not for their stability.
Lysosomal degradation of cholecystokinin-(29-33)-amide in mouse brain is dependent on this enzyme: implications for the degradation and storage of peptides in classical late-infantile neuronal ceroid lipofuscinosis (tripeptidyl peptidase-I)
TPP-I is the predominant proteolytic enzyme responsible for the intracellular degradation of neuromedin B
The CLN2-targeted mouse recapitulates much of the pathology and clinical features of classical late-infantile neuronal ceroid lipofuscinosis
Tpp1 confers telomere end protection by recruiting Pot1a and Pot1b to telomeres. Knockdown of Tpp1 elicits an ataxia telangiectasia mutated protein (ATR)-dependent DNA damage response at telomeres.
Expression of 6% of normal TPPI activity increased lifespan to that of unaffected mice.
Results indicate that the loss of TPPI cannot be functionally compensated for by DPPI.
While all treatment groups show a marked increase in total TPP-I activity over wild-type mice, neonatally treated mice displayed high levels of TPP-I activity in the CNS 1 yr after administration which was spread throughout the brain.
This gene encodes a member of the sedolisin family of serine proteases. The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. It is synthesized as a catalytically-inactive enzyme which is activated and auto-proteolyzed upon acidification. Mutations in this gene result in late-infantile neuronal ceroid lipofuscinosis, which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome.
ceroid-lipofuscinosis, neuronal 2
, tripeptidyl-peptidase 1
, cell growth-inhibiting gene 1 protein
, growth-inhibiting protein 1
, lysosomal pepstatin insensitive protease
, tripeptidyl aminopeptidase
, lysosomal pepstatin-insensitive protease
, tripeptidyl peptidase 1
, tripeptidyl-peptidase I
, tripeptidyl peptidase-I