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Gene Review

TPP2  -  tripeptidyl peptidase II

Homo sapiens

Synonyms: TPP-2, TPP-II, Tripeptidyl aminopeptidase, Tripeptidyl-peptidase 2, Tripeptidyl-peptidase II
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Disease relevance of TPP2


High impact information on TPP2


Biological context of TPP2


Anatomical context of TPP2


Associations of TPP2 with chemical compounds

  • When native TPP II was dissociated into smaller units through dialysis against a dilute Tris buffer, it could be digested by chymotrypsin into three stable fragments of 70 kDa, 42 kDa and 20 kDa [13].
  • Antibodies against a 65 kDa cell-binding fragment of fibronectin specifically reacted with TPP II, whereas antibodies against the collagen-binding domain, the main heparin-binding domain or the N-terminal fibrin-binding domain did not react [13].
  • There is an in-frame methionine at position 8, which probably represents the starting point of translation, indicating that the complete coding sequence for TPP II now has been determined [14].
  • Furthermore, we show that proteasomes are unlikely to generate MHC class I ligands with a C-terminal lysine residue, suggesting processing of these ligands by a different protease that may be tripeptidyl-peptidase II (TPPII) [15].
  • Use of a dehydroalanine-containing peptide as an efficient inhibitor of tripeptidyl peptidase II [16].

Physical interactions of TPP2

  • Moreover, the affinity-purified antibodies against TPP II reacted with a 105 kDa cell-binding fragment of fibronectin but not with the fibrin-binding domain or the collagen-binding domain [13].

Regulatory relationships of TPP2


Other interactions of TPP2


Analytical, diagnostic and therapeutic context of TPP2


  1. Mitotic infidelity and centrosome duplication errors in cells overexpressing tripeptidyl-peptidase II. Stavropoulou, V., Xie, J., Henriksson, M., Tomkinson, B., Imreh, S., Masucci, M.G. Cancer Res. (2005) [Pubmed]
  2. Tripeptidyl peptidase II in haemolysates and liver homogenates of various species. Bålöw, R.M., Eriksson, I. Biochem. J. (1987) [Pubmed]
  3. Down-regulation of proteolytic complexes following EBV activation in BL cells. Matusali, G., Leo, A.D., Gavioli, R., Bertelli, L., Renzo, L.D., Mattia, E. Biochem. Biophys. Res. Commun. (2007) [Pubmed]
  4. Human monocytes possess a serine protease activity capable of degrading HIV-1 reverse transcriptase in vitro. Château, M.T., Robert-Hebmann, V., Devaux, C., Lazaro, J.B., Canard, B., Coux, O. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  5. A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation. Reits, E., Neijssen, J., Herberts, C., Benckhuijsen, W., Janssen, L., Drijfhout, J.W., Neefjes, J. Immunity (2004) [Pubmed]
  6. Generation of major histocompatibility complex class I antigens: functional interplay between proteasomes and TPPII. Kloetzel, P.M. Nat. Immunol. (2004) [Pubmed]
  7. Active site of tripeptidyl peptidase II from human erythrocytes is of the subtilisin type. Tomkinson, B., Wernstedt, C., Hellman, U., Zetterqvist, O. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  8. Localization of the human tripeptidyl peptidase II gene (TPP2) to 13q32-q33 by nonradioactive in situ hybridization and somatic cell hybrids. Martinsson, T., Vujic, M., Tomkinson, B. Genomics (1993) [Pubmed]
  9. Identification and characterization of the promoter for the gene encoding human tripeptidyl-peptidase II. Lindås, A.C., Tomkinson, B. Gene (2005) [Pubmed]
  10. Characterization of trypanosome protein phosphatase 1 and 2A catalytic subunits. Erondu, N.E., Donelson, J.E. Mol. Biochem. Parasitol. (1991) [Pubmed]
  11. The final N-terminal trimming of a subaminoterminal proline-containing HLA class I-restricted antigenic peptide in the cytosol is mediated by two peptidases. Lévy, F., Burri, L., Morel, S., Peitrequin, A.L., Lévy, N., Bachi, A., Hellman, U., Van den Eynde, B.J., Servis, C. J. Immunol. (2002) [Pubmed]
  12. Axonal transports of tripeptidyl peptidase II in rat sciatic nerves. Chikuma, T., Shimizu, M., Tsuchiya, Y., Kato, T., Hojo, H. Neurochem. Int. (2007) [Pubmed]
  13. Immunological cross-reactivity between human tripeptidyl peptidase II and fibronectin. Tomkinson, B., Zetterqvist, O. Biochem. J. (1990) [Pubmed]
  14. Nucleotide sequence of cDNA covering the N-terminus of human tripeptidyl peptidase II. Tomkinson, B. Biomed. Biochim. Acta (1991) [Pubmed]
  15. Modeling the MHC class I pathway by combining predictions of proteasomal cleavage, TAP transport and MHC class I binding. Tenzer, S., Peters, B., Bulik, S., Schoor, O., Lemmel, C., Schatz, M.M., Kloetzel, P.M., Rammensee, H.G., Schild, H., Holzhütter, H.G. Cell. Mol. Life Sci. (2005) [Pubmed]
  16. Use of a dehydroalanine-containing peptide as an efficient inhibitor of tripeptidyl peptidase II. Tomkinson, B., Grehn, L., Fransson, B., Zetterqvist, O. Arch. Biochem. Biophys. (1994) [Pubmed]
  17. Overlapping regional distribution of CCK and TPPII mRNAs in Cynomolgus monkey brain and correlated levels in human cerebral cortex (BA 10). Radu, D., Tomkinson, B., Zachrisson, O., Weber, G., de Belleroche, J., Hirsch, S., Lindefors, N. Brain Res. (2006) [Pubmed]
  18. Degradation of glyceraldehyde-3-phosphate dehydrogenase triggered by 4-hydroxy-2-nonenal and 4-hydroxy-2-hexenal. Tsuchiya, Y., Yamaguchi, M., Chikuma, T., Hojo, H. Arch. Biochem. Biophys. (2005) [Pubmed]
  19. Recombinant interferon-gamma secreted by Chinese hamster ovary-320 cells cultivated in suspension in protein-free media is protected against extracellular proteolysis by the expression of natural protease inhibitors and by the addition of plant protein hydrolysates to the culture medium. Mols, J., Peeters-Joris, C., Wattiez, R., Agathos, S.N., Schneider, Y.J. In Vitro Cell. Dev. Biol. Anim. (2005) [Pubmed]
  20. Effects of an inhibitor of tripeptidyl peptidase II (Ala-Ala-Phe-chloromethylketone) and its combination with an inhibitor of the chymotrypsin-like activity of the proteasome (PSI) on apoptosis, cell cycle and proteasome activity in U937 cells. Bury, M., Młynarczuk, I., Pleban, E., Hoser, G., Kawiak, J., Wójcik, C. Folia Histochem. Cytobiol. (2001) [Pubmed]
  21. Identification of the catalytic triad in tripeptidyl-peptidase II through site-directed mutagenesis. Hilbi, H., Jozsa, E., Tomkinson, B. Biochim. Biophys. Acta (2002) [Pubmed]
  22. Supramolecular structure of tripeptidyl peptidase II from human erythrocytes as studied by electron microscopy, and its correlation to enzyme activity. Macpherson, E., Tomkinson, B., Bålöw, R.M., Höglund, S., Zetterqvist, O. Biochem. J. (1987) [Pubmed]
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