CLN2 disease do not have any enzyme called TPP1
or they have too little of it and this causes a build-up of substances called sosomal storage materials.
The company said that RGX-181 is a one-time treatment candidate for late-infantile neuronal ceroid lipofuscinosis type 2 (CLN2) disease, one of the most common forms of Batten disease caused by mutations in the tripeptidyl peptidase 1 (TPP1
Pharmacology studies conducted in an animal model of CLN2 disease demonstrated that a single administration of RGX-181 resulted in widespread distribution and sustained expression of the TPP1
enzyme in the CNS with significant improvements in neurobehavioral function and survival of the animals.
For instance, a study reported that a missense variant rs149418249 in the TPP1
gene confers colorectal cancer risk by interrupting TPP1-TIN2 interaction and influencing telomere length .
Tian et al., "A rare variant P507L in TPP1
-TIN2 interaction, influences telomere length, and confers colorectal cancer risk in Chinese population," Cancer Epidemiology Biomarkers & Prevention, vol.
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.
Brineura is the first FDA-approved treatment to slow loss of walking ability in symptomatic pediatric patients 3 years of age and older with late infantile neuronal ceroid lipofuscinosis type 2 (CLN2), also known as tripeptidyl peptidase-1 (TPP1
Here, we report results expanding the diagnostic portfolio to a 7-plex format including new assays for lysosomal enzymes tripeptidyl peptidase 1 (TPP1
), [alpha]-N- acetylglucosaminidase (NAGLU), and lysosomal [beta]-glucuronidase (GUSB).
They are telomere repeat-binding factor 1 (TRF1), telomere repeat-binding factor 2 (TRF2), repressor-activator protein 1 (RAP1), TRF1- and TRF2-interacting nuclear protein 2 (TIN2), tripeptidyl-peptidase 1 (TPP1
), and protection of telomere 1 (POT1) .
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].
Proteins comprising the Shelterin complex are TRF1, TRF2, TIN2, RAP1, TPP1
, and POT1.
Telosomyl stimulates the telosomic protein expression (POT1 and TPP1
), thus limiting the shortening of telomeres.