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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 (显示 CLN6 蛋白).
To our knowledge, our results bring the first evidence of a mechanism that links TPP-1 deficiency and oxidative stress-induced (显示 SQSTM1 蛋白) 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 (显示 CLN6 蛋白).
TPP1 mutants utilize the advantages of a zebrafish model for understanding the pathogenesis of late infantile (or classic late infantile neuronal ceroid lipofuscinosis (显示 CLN6 蛋白)) 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 (显示 PPARA 蛋白) and may have implications in late infantile Batten disease therapy
telomeres are protected from hyper-resection through the repression of the ATM (显示 ATM 蛋白) and ATR kinases by TRF2 (显示 TERF2 蛋白) and TPP1-bound POT1a (显示 POT1 蛋白)/b, respectively.
Rssults suggested that CLN2, CLN3 (显示 CLN3 蛋白) and CLN5 (显示 CLN5 蛋白) genes may play an important role in early embryonal neurogenesis.
demonstrated that cells expressing TIN2DeltaTPP1 instead of wild-type TIN2 (显示 TINF2 蛋白) phenocopy the POT1a (显示 POT1 蛋白),b knockout setting without showing additional phenotypes
TPPI activity becomes crucial for the neuronal functions later in development.
Telomere protection by TPP1/POT1 (显示 POT1 蛋白) requires tethering to TIN2 (显示 TINF2 蛋白).
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 (显示 POT1 蛋白) and POT1b from chromatin and loss of these proteins from telomeres, indicating that TPP1 is required for the telomere association of POT1a (显示 POT1 蛋白) and POT1b but not for their stability.
Lysosomal degradation of cholecystokinin (显示 CCK 蛋白)-(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 (显示 CLN6 蛋白) (tripeptidyl peptidase-I)
TPP-I is the predominant proteolytic enzyme responsible for the intracellular degradation of neuromedin B
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