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Tpp1  -  tripeptidyl peptidase I

Rattus norvegicus

Synonyms: Cln2, TPP-1, TPP-I, Tripeptidyl aminopeptidase, Tripeptidyl-peptidase 1, ...
 
 
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Disease relevance of Tpp1

  • The strategy of this clinical study is based on the concept that persistent expression in the CNS of the normal CLN2 cDNA with production of sufficient amounts of TPP-I should prevent further loss of neurons, and hence limit disease progression [1].
 

High impact information on Tpp1

  • Assessment at 5 and 13 weeks demonstrated widespread detection of TPP-I in neurons, but not glial cells, at all regions of injection [2].
  • In the central nervous system (CNS), the deficiency of TPP-I results in the accumulation of proteins in lysosomes leading to a loss of neurons causing progressive neurological decline, and death by ages 10-12 years [2].
  • At the longer time points following striatal administration, TPP-I-positive cell bodies were also observed in the substantia nigra, frontal cerebral cortex and thalamus of the injected hemisphere, and the frontal cerebral cortex of the noninjected hemisphere [2].
  • Cln2p/TPP-I is a unique enzyme with both tripeptidyl peptidase and endopeptidase activities for certain substrate specificity [3].
  • In particular, the TPP-I activity was low in the brains of both animals and high in the rat testis, although its protein levels were high in the former tissue and low in the latter [4].
 

Anatomical context of Tpp1

 

Associations of Tpp1 with chemical compounds

 

Other interactions of Tpp1

  • The present immunohistochemical study further examined the localization of lysosomal aminopeptidases, cathepsin C, and tripeptidyl peptidase I (TPP-I) in the rat lung [5].
  • These results showing that lysosomal aminopeptidases such as cathepsin H, cathepsin C and TPP-I are localized in lamellar bodies of type II alveolar epithelial cells strongly argue for the participation of lysosomal aminopeptidases in the formation process of surfactant containing specific proteins [5].
 

Analytical, diagnostic and therapeutic context of Tpp1

References

  1. Clinical protocol. Administration of a replication-deficient adeno-associated virus gene transfer vector expressing the human CLN2 cDNA to the brain of children with late infantile neuronal ceroid lipofuscinosis. Crystal, R.G., Sondhi, D., Hackett, N.R., Kaminsky, S.M., Worgall, S., Stieg, P., Souweidane, M., Hosain, S., Heier, L., Ballon, D., Dinner, M., Wisniewski, K., Kaplitt, M., Greenwald, B.M., Howell, J.D., Strybing, K., Dyke, J., Voss, H. Hum. Gene Ther. (2004) [Pubmed]
  2. AAV2-mediated CLN2 gene transfer to rodent and non-human primate brain results in long-term TPP-I expression compatible with therapy for LINCL. Sondhi, D., Peterson, D.A., Giannaris, E.L., Sanders, C.T., Mendez, B.S., De, B., Rostkowski, A.B., Blanchard, B., Bjugstad, K., Sladek, J.R., Redmond, D.E., Leopold, P.L., Kaminsky, S.M., Hackett, N.R., Crystal, R.G. Gene Ther. (2005) [Pubmed]
  3. Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis. Ezaki, J., Takeda-Ezaki, M., Oda, K., Kominami, E. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  4. The expression of tripeptidyl peptidase I in various tissues of rats and mice. Koike, M., Shibata, M., Ohsawa, Y., Kametaka, S., Waguri, S., Kominami, E., Uchiyama, Y. Arch. Histol. Cytol. (2002) [Pubmed]
  5. Specific localization of lysosomal aminopeptidases in type II alveolar epithelial cells of the rat lung. Yayoi, Y., Ohsawa, Y., Koike, M., Zhang, G., Kominami, E., Uchiyama, Y. Arch. Histol. Cytol. (2001) [Pubmed]
  6. Acute doxorubicin (adriamycin) dosage does not reduce cardiac protein synthesis in vivo, but decreases diaminopeptidase I and proline endopeptidase activities. Zima, T., Tesar, V., Mantle, D., Koll, M., Patel, V., Richardson, P.J., Preedy, V.R. Exp. Mol. Pathol. (2001) [Pubmed]
 
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