TPP1

TPP1

A gene on chromosome 11p15 that encodes a sedolisin-type serine protease, which acts in lysosomes to cleave N-terminal tripeptides from substrates; it also has weak endopeptidase activity. Tripeptidyl peptidase I is activated and auto-proteolysed by acidification.

Molecular pathology
TPP1 mutations have been linked to late-infantile neuronal ceroid lipofuscinosis (CLN2, Jansky-Bielschowsky disease), which is due to the failure to degrade specific neuropeptides, and a subunit of ATP synthase in lysosomes.
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References in periodicals archive ?
Food and Drug Administration, Brineura, which is supposed to act as a replacement for TPP1, an essential enzyme that the four-year-old's body fails to produce because of his affliction.
Its active ingredient (cerliponase alfa) is a recombinant form of human TPP1, the enzyme deficient in patients with CLN2 disease.
The majority of the TINF2 mutations found in telomere syndrome patients lie in a cluster outside the binding regions of TINF2 to shelterin proteins TRF1, TRF2, and TPP1 and do not seem to influence the interaction of TINF2 with these proteins [20, 22].
The Ser245Tyr mutation lies outside of this mutation cluster and also outside of the binding regions of TINF2 to TRF1, TRF2, and TPP1.
Evaluation of the canine TPP1 gene as a candidate for neuronal ceroid lipofuscinosis in Tibetan terrier and Polish Owczarek Nizinny dogs.
Along with TRF1, RAP, TIN2 and TPP1, TRF2 comprises the shelterin complex, also known as the telosome.
To date, more than 30 mutations have been reported in the PPT1 and TPP1 genes, rendering molecular genetic analysis impractical as a primary means of diagnosis.
Brineura, an enzyme replacement therapy, is the first to be directly administered to the brain, treating the underlying cause of the condition by helping replace the deficient TPP1 enzyme.
The enzyme replacement therapy is designed to restore TPP1 enzyme activity and break down the storage materials that cause CLN2 disease.