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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.
Binding of POT1 (show POT1 Proteins)-TPP1 unfolds telomere secondary structure to assist loading of additional heterodimers.
Together, these functional data combined with biophysical analyses and homology modeling provide a molecular understanding of the diverse contributions of TPP1 in telomere maintenance.
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.
We found that NEK6 (show NEK6 Proteins)-mediated phosphorylation of TPP1 Ser255 in G2/M phase regulates the association between telomerase activity and TPP1. Furthermore, we found evidence that POT1 (show POT1 Proteins) negatively regulates TPP1 phosphorylation because the level of Ser255 phosphorylation was elevated when telomeres were elongated by a POT1 (show POT1 Proteins) mutant lacking its OB-fold domains
The conservation between fission yeast Tpz1-Pot1 (show POT1 Proteins) and human TPP1-POT1 (show POT1 Proteins) interactions resulted in mapping a human melanoma-associated (show ZNF654 Proteins) POT1 (show POT1 Proteins) mutation (A532P) to the TPP1-POT1 (show POT1 Proteins) interface.
that the insertion in fingers domain can mediate enzyme processivity and telomerase recruitment to telomeres in a TPP1-dependent manner
these data provide a molecular basis by which POT1 (show POT1 Proteins)-TPP1 increases the processivity of telomerase15. Further, we show that this increased processivity may arise from the dynamic sliding of POT1 (show POT1 Proteins)-TPP1 that induces fast translocation of telomerase.
Mutations have been identified in the TEN-domain of TERT (show TERT Proteins) that disrupt the interaction of telomerase with TPP1 in vivo and in vitro but have very little effect on the catalytic activity of telomerase.
telomeres are protected from hyper-resection through the repression of the ATM (show ATM Proteins) and ATR kinases by TRF2 (show TERF2 Proteins) and TPP1-bound POT1a (show POT1 Proteins)/b, respectively.
Rssults suggested that CLN2, CLN3 (show CLN3 Proteins) and CLN5 (show CLN5 Proteins) genes may play an important role in early embryonal neurogenesis.
demonstrated that cells expressing TIN2DeltaTPP1 instead of wild-type TIN2 (show TINF2 Proteins) phenocopy the POT1a (show POT1 Proteins),b knockout setting without showing additional phenotypes
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 (show PPARA Proteins) and may have implications in late infantile Batten disease therapy
TPPI activity becomes crucial for the neuronal functions later in development.
Telomere protection by TPP1/POT1 (show POT1 Proteins) requires tethering to TIN2 (show TINF2 Proteins).
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 (show POT1 Proteins) and POT1b from chromatin and loss of these proteins from telomeres, indicating that TPP1 is required for the telomere association of POT1a (show POT1 Proteins) and POT1b but not for their stability.
Lysosomal degradation of cholecystokinin (show CCK Proteins)-(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 (show CLN6 Proteins) (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