Tripeptidyl Peptidase 1 (TPP1) Deficiency in a 36-Year-Old Patient with Cerebellar-Extrapyramidal Syndrome and Dilated Cardiomyopathy [PDF]
Life, 2021 We report on a 36-year-old man with cerebellar-extrapyramidal syndrome and severe heart failure because of dilated cardiomyopathy of unknown origin. Dysarthria and cardiac arrhythmia began at early childhood (4 years of age).
Agnieszka Ługowska +11 more
doaj +5 more sources
A tripeptidyl peptidase 1 is a binding partner of the Golgi pH regulator (GPHR) in Dictyostelium [PDF]
Disease Models & Mechanisms, 2017 Mutations in tripeptidyl peptidase 1 (TPP1) have been associated with late infantile neuronal ceroid lipofuscinosis (NCL), a neurodegenerative disorder. TPP1 is a lysosomal serine protease, which removes tripeptides from the N-terminus of proteins and is
Maria Stumpf +8 more
doaj +5 more sources
Inducible transgenic expression of tripeptidyl peptidase 1 in a mouse model of late-infantile neuronal ceroid lipofuscinosis. [PDF]
PLoS ONE, 2018 Late-infantile neuronal ceroid lipofuscinosis is a fatal neurodegenerative disease of children caused by mutations resulting in loss of activity of the lysosomal protease, tripeptidyl peptidase 1 (TPP1).
Yuliya Nemtsova +4 more
doaj +5 more sources
Upregulation of tripeptidyl-peptidase 1 by 3-hydroxy-(2,2)-dimethyl butyrate, a brain endogenous ligand of PPARα: Implications for late-infantile Batten disease therapy [PDF]
Neurobiology of Disease, 2019 The late-infantile Batten disease or late-infantile neuronal ceroid lipofuscinosis (LINCL) is an autosomal recessive lysosomal storage disorder caused by mutations in the Cln2 gene leading to deficiency of lysosomal enzyme tripeptidyl peptidase 1 (TPP1).
Sudipta Chakrabarti +5 more
doaj +5 more sources
Lysosomal enzyme tripeptidyl peptidase 1 destabilizes fibrillar Aβ by multiple endoproteolytic cleavages within the β-sheet domain [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 2018 Significance Alzheimer’s disease is the leading cause of dementia. Accumulation of amyloid-beta (Aβ) plaques, which include β-sheet fibrils of Aβ, is a hallmark of the disease. Aβ aggregates can be endocytosed by microglia and delivered to lysosomes, but degradation of fibrillar Aβ in microglial lysosomes is slow.
Santiago Solé-Domènech +2 more
exaly +5 more sources
First in man study of intravitreal tripeptidyl peptidase 1 for CLN2 retinopathy. [PDF]
Eye (Lond), 2023 Abstract Background/Objectives CLN2 Batten Disease is a fatal neurodegenerative condition of childhood associated with retinal dystrophy and blindness. Intracerebroventricular infusion of rhTPP1 greatly slows the rate of neurodegenerative decline but not retinopathy.
Wawrzynski J +11 more
europepmc +4 more sources
Tripeptidyl Peptidase 1 Regulates Human Trophoblast Cell Proliferation Implying a Role in Placentation. [PDF]
Biomed Res Int, 2022 Proper placentation in the first trimester is essential for a healthy pregnancy in humans. A recent proteomics study of human placental tissue has identified that tripeptidyl peptidase 1 (TPP1) production is reduced in the placenta in early‐onset preeclampsia compared to uncomplicated pregnancy.
Zhou W, Dimitriadis E.
europepmc +4 more sources
Elevated levels of tripeptidyl peptidase 1 do not ameliorate pathogenesis in a mouse model of Alzheimer disease. [PDF]
Neurobiol Aging, 2022 One potential therapeutic strategy for Alzheimer disease (AD) is to promote degradation of amyloid beta (Aβ) and we previously demonstrated that the lysosomal protease tripeptidyl peptidase 1 (TPP1) can degrade Aβ fibrils in vitro. In this study, we tested the hypothesis that increasing levels of TPP1 might promote degradation of Aβ under physiological
Sleat DE +9 more
europepmc +3 more sources
Compound heterozygous mutations in tripeptidyl peptidase 1 cause rare autosomal recessive spinocerebellar ataxia type 7: A case report. [PDF]
World J Clin Cases, 2023 In recent years, metabolomics research has become a hot spot in the screening and treatment of cancer. It is a popular technique for the quantitative characterization of small molecular compounds in biological cells, tissues, organs or organisms. Further study of the tumor revealed that amino acid changes may occur early in the tumor.
Liu RH +7 more
europepmc +3 more sources
Lysosomal protein thermal stability does not correlate with cellular half-life: global observations and a case study of tripeptidyl-peptidase 1. [PDF]
Biochem J, 2020 Late-infantile neuronal ceroid lipofuscinosis (LINCL) is a neurodegenerative lysosomal storage disorder caused by mutations in the gene encoding the protease tripeptidyl-peptidase 1 (TPP1). Progression of LINCL can be slowed or halted by enzyme replacement therapy, where recombinant human TPP1 is administered to patients.
Collier AM +7 more
europepmc +4 more sources