TPP1 Antibody

1. 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. PMID: 29160297
2. TPP1 cleaves and destabilizes fibrillar amyloid-beta at multiple sites in a time- and pH-dependent manner. PMID: 29378960
3. 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. PMID: 27553878
4. 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. PMID: 28079862
5. 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. PMID: 27840983
6. TPP1(CLN2) mutation is associated with neuronal ceroid lipofuscinosis. PMID: 24271013
7. 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. PMID: 23249249
8. hypothesize that loss of function variants abolishing TPP1 enzyme activity lead to CLN2 disease, whereas variants that diminish TPP1 enzyme activity lead to SCAR7 PMID: 23418007
9. This study demonistrated that the CLN2 gene 4 mutation in late infantile neuronal ceroid lipofuscinosis. PMID: 22832778
10. TPP1 mutants utilize the advantages of a zebrafish model for understanding the pathogenesis of late infantile (or classic late infantile neuronal ceroid lipofuscinosis) disease. PMID: 23587805
11. The variant juvenile phenotype comprises approximately 50% of CLN2 in South America. The five most frequent South American mutations comprise 66% of pathological alleles. PMID: 23266810
12. 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 PMID: 22989886
13. 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. PMID: 22016395
14. Intrathecal human tripeptidyl-peptidase 1 administration reduces lysosomal storage in a canine model of late infantile neuronal ceroid lipofuscinosis. PMID: 21784683
15. the critical residues in the TPPI catalysis and its structure-function analysis PMID: 20689811
16. Data show that most TPPI variants displayed obstructed transport to the lysosomes. PMID: 20340139
17. 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). PMID: 20672930
18. The clinical, biochemical, and molecular genetic aspects of lysosomal storage disorders are discussed in this review PMID: 12125808
19. 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 PMID: 12134079
20. Missense mutations, R127Q, N286S, and T353P represent novel, previously not described alleles. PMID: 12376936
21. human tripeptidyl-peptidase I is processed by a serine protease to the mature, active form in vivo PMID: 12488460
22. a novel mutation in neuronal ceroid lipofuscinosis PMID: 12698559
23. CLN2 gene mutations may result in low cerebrospinal fluid pterin production in classical neuronal ceroid lipofuscinoses of late infantile onset. PMID: 12950156
24. human tripeptidyl-peptidase I must be N-glycosylated for folding, trafficking, and stability PMID: 14702339
25. mutant Asn286Ser CLN2 lacks one oligosaccharide chain resulting in enzymatic inactivation PMID: 14736728
26. intramolecular (unimolecular) mechanism of TPP I activation and autoprocessing PMID: 15143070
27. TPP-I is the predominant proteolytic enzyme responsible for the intracellular degradation of neuromedin B PMID: 15158442
28. Functional analyses of CLN2 mutations reveal transport disruption of tripeptidyl-peptidase I to lysosomes. PMID: 15317752
29. tripeptidyl-peptidase I activation, activity, and stability are regulated by glycosaminoglycans PMID: 15582991
30. Ser475 and Asp360, also Glu272, Asp276, and Asp327 are important for catalytic activity of tripeptidyl peptidase I PMID: 15733845
31. Substrate-binding cleft of TPP-I composed of only 6 subsites; TPP-I prefers bulky and hydrophobic amino acid residues at P(1) position and Ala, Arg, or Asp at P(2) position; hydrophilic interactions at the S(2) subsite are necessary for TPP-I. PMID: 16091586
32. Mutational screening of CLCN2 gene, revealed a homozygous mutation G2003C (exon 17), leading to a Ser/Thr substitution at the codon 668, in two of the three in malignant migrating partial seizures patients. PMID: 16168594
33. there is a close correlation between CLN2 and CLN1 expression and colorectal carcinoma progression and metastasis and suggest that they may be potential molecular targets PMID: 16518810
34. Clinical features, histological findings, and genetic study reveal that CLN2 type is the most common form of neuronal ceroid lipofuscinosis. There is male predominance of 90.1% in this part of the Arab world. PMID: 17690061
35. CLN2/TPP1 deficiency: the novel mutation IVS7-10A>G causes intron retention and is associated with a mild disease phenotype. PMID: 17959406
36. the tripeptidyl peptidase I prosegment is a potent, slow-binding inhibitor of its cognate enzyme PMID: 18411270
37. Lysosome-related genes, such as CLN2, CLN3, and HEXB, may be involved in the pathogenesis of adipose tissue hypertrophy in TED. PMID: 18552385
38. Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis. PMID: 19038966
39. Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis PMID: 19038967
40. This novel deletion mutation in the CLN2 gene in a family of Arab origin from Israel sheds further light on the epidemiology of neuronal ceroid lipofuscinosis as a worldwide disease PMID: 19748052
41. functional analysis of variants expressed in CHO cells PMID: 11462245

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HGNC: 2073

OMIM: 204500

KEGG: hsa:1200

STRING: 9606.ENSP00000299427

UniGene: Hs.523454