Cathepsin A is expressed in primary human antigen-presenting cells

Immunology Letters

Volumn 128, Issue 2, 2010, Pages 143-147

  Reich, Michael ^a   Spindler, Klaus Dieter ^b   Burret, Michael ^b   Kalbacher, Hubert ^c   Boehm, Bernhard O ^a   Burster, Timo ^a  

^a UNIVERSITY HOSPITAL ULM   (Germany)

^b Insitute of General Zoology and Endokrinology   (Germany)

^c UNIVERSITY OF TÜBINGEN   (Germany)

Author keywords

Antigen presentation processing; Cathepsin A

Indexed keywords

AMINO ACID; CARBOXYPEPTIDASE C; CD14 ANTIGEN; CD19 ANTIGEN; CD4 ANTIGEN; CD8 ANTIGEN; EPITOPE; LACTACYSTIN; LYSOSOMAL PROTEASE; PEPTIDE; PROLINE; PROTEINASE; SERINE PROTEINASE; UNCLASSIFIED DRUG;

AMINO ACID TRANSPORT; ANTIGEN PRESENTING CELL; ARTICLE; B LYMPHOCYTE; BONE MARROW CELL; CARBOXY TERMINAL SEQUENCE; CELL LYSATE; CONTROLLED STUDY; DAUDI CELL; DENDRITIC CELL; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME LOCALIZATION; ENZYME RELEASE; HUMAN; HUMAN CELL; LYMPHOBLASTOID CELL; LYSOSOME; MONOCYTE; NEUTROPHIL; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; T LYMPHOCYTE;

AMINO ACID SEQUENCE; ANTIGEN-PRESENTING CELLS; ANTIGENS; B-LYMPHOCYTES; CATHEPSIN A; DENDRITIC CELLS; HUMANS; IMMUNOHISTOCHEMISTRY; MOLECULAR SEQUENCE DATA; PEPTIDES;

EID: 77249134959     PISSN: 01652478     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.imlet.2009.11.010     Document Type: Article

References (31)

1. Wilson N.S., Villadangos J.A. Regulation of antigen presentation and cross-presentation in the dendritic cell network: facts, hypothesis, and immunological implications. Adv Immunol 2005, 86:241-305.
2. Burster T., Beck A., Tolosa E., Marin-Esteban V., Rotzschke O., Falk K., et al. Cathepsin G, and not the asparagine-specific endoprotease, controls the processing of myelin basic protein in lysosomes from human B lymphocytes. J Immunol 2004, 172:5495-5503.
3. Stoeckle C., Sommandas V., Adamopoulou E., Belisle K., Schiekofer S., Melms A., et al. Cathepsin G is differentially expressed in primary human antigen-presenting cells. Cell Immunol 2009, 255:41-45.
4. Reich M., Lesner A., Legowska A., Sienczyk M., Oleksyszyn J., Boehm B.O., et al. Application of specific cell permeable cathepsin G inhibitors resulted in reduced antigen processing in primary dendritic cells. Mol Immunol 2009, 46:2994-2999.
5. Zavasnik-Bergant T., Turk B. Cysteine cathepsins in the immune response. Tissue Antigens 2006, 67:349-355.
6. Rudensky A, Beers C. Lysosomal cysteine proteases and antigen presentation. Ernst Schering Res Found Workshop 2006:81-95.
7. Watts C., Matthews S.P., Mazzeo D., Manoury B., Moss C.X. Asparaginyl endopeptidase: case history of a class II MHC compartment protease. Immunol Rev 2005, 207:218-228.
8. Riese R.J., Wolf P.R., Bromme D., Natkin L.R., Villadangos J.A., Ploegh H.L., et al. Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity 1996, 4:357-366.
9. Yasuda Y., Li Z., Greenbaum D., Bogyo M., Weber E., Bromme D., et al. A novel and potent elastolytic activity expressed in activated macrophages. J Biol Chem 2004, 279:36761-36770.
10. Reich M., Wieczerzak E., Jankowska E., Palesch D., Boehm B.O., Burster T. Specific cathepsin B inhibitor is cell-permeable and activates presentation of TTC in primary human dendritic cells. Immunol Lett 2009, 123:155-159.
11. Villadangos J.A., Ploegh H.L. Proteolysis in MHC class II antigen presentation: who's in charge? Immunity 2000, 12:233-239.
12. Bennett K., Levine T., Ellis J.S., Peanasky R.J., Samloff I.M., Kay J., et al. Antigen processing for presentation by class II major histocompatibility complex requires cleavage by cathepsin E. Eur J Immunol 1992, 22:1519-1524.
13. Nishioku T., Hashimoto K., Yamashita K., Liou S.Y., Kagamiishi Y., Maegawa H., et al. Involvement of cathepsin E in exogenous antigen processing in primary cultured murine microglia. J Biol Chem 2002, 277:4816-4822.
14. Chain B.M., Free P., Medd P., Swetman C., Tabor A.B., Terrazzini N. The expression and function of cathepsin E in dendritic cells. J Immunol 2005, 174:1791-1800.
15. Burster T., Reich M., Zaidi N., Voelter W., Boehm B.O., Kalbacher H. Cathepsin E regulates the presentation of tetanus toxin C-fragment in PMA activated primary human B cells. Biochem Biophys Res Commun 2008, 377:1299-1303.
16. Shibko S., Pangborn J., Tappel A.L. Studies on the release of lysosomal enzymes from kidney lysosomes. J Cell Biol 1965, 25:479-483.
17. Galjart N.J., Gillemans N., Harris A., van der Horst G.T., Verheijen F.W., Galjaard H., et al. Expression of cDNA encoding the human " protective protein" associated with lysosomal beta-galactosidase and neuraminidase: homology to yeast proteases. Cell 1988, 54:755-764.
18. Matsuda K. Studies on cathepsins of rat liver lysosomes. III. Hydrolysis of peptides, and inactivation of angiotensin and bradykinin by cathepsin A. J Biochem 1976, 80:659-669.
19. Kawamura Y., Matoba T., Hata T., Doi E. Substrate specificities of cathepsin A,L and A, S from pig kidney. J Biochem 1977, 81:435-441.
20. Jackman H.L., Tan F.L., Tamei H., Beurling-Harbury C., Li X.Y., Skidgel R.A., et al. A peptidase in human platelets that deamidates tachykinins. Probable identity with the lysosomal " protective protein" J Biol Chem 1990, 265:11265-11272.
21. Seyrantepe V., Hinek A., Peng J., Fedjaev M., Ernest S., Kadota Y., et al. Enzymatic activity of lysosomal carboxypeptidase (cathepsin) A is required for proper elastic fiber formation and inactivation of endothelin-1. Circulation 2008, 117:1973-1981.
22. Cuervo A.M., Mann L., Bonten E.J., d'Azzo A., Dice J.F. Cathepsin A regulates chaperone-mediated autophagy through cleavage of the lysosomal receptor. Embo J 2003, 22:47-59.
23. D'Azzo A., Hoogeveen A., Reuser A.J., Robinson D., Galjaard H. Molecular defect in combined beta-galactosidase and neuraminidase deficiency in man. Proc Natl Acad Sci U S A 1982, 79:4535-4539.
24. Rudenko G., Bonten E., Hol W.G., d'Azzo A. The atomic model of the human protective protein/cathepsin A suggests a structural basis for galactosialidosis. Proc Natl Acad Sci U S A 1998, 95:621-625.
25. Hanna W.L., Turbov J.M., Jackman H.L., Tan F., Froelich C.J. Dominant chymotrypsin-like esterase activity in human lymphocyte granules is mediated by the serine carboxypeptidase called cathepsin A-like protective protein. J Immunol 1994, 153:4663-4672.
26. Satake A., Itoh K., Shimmoto M., Saido T.C., Sakuraba H., Suzuki Y. Distribution of lysosomal protective protein in human tissues. Biochem Biophys Res Commun 1994, 205:38-43.
27. Kozlowski L., Wojtukiewicz M.Z., Ostrowska H., Cathepsin A activity in primary and metastatic human melanocytic tumors. Arch Dermatol Res 2000, 292:68-71.
28. Birkus G., Wang R., Liu X., Kutty N., MacArthur H., Cihlar T., et al. Cathepsin A is the major hydrolase catalyzing the intracellular hydrolysis of the antiretroviral nucleotide phosphonoamidate prodrugs GS-7340 and GS-9131. Antimicrob Agents Chemother 2007, 51:543-550.
29. Jackman H.L., Tan F., Schraufnagel D., Dragovic T., Dezso B., Becker R.P., et al. Plasma membrane-bound and lysosomal peptidases in human alveolar macrophages. Am J Respir Cell Mol Biol 1995, 13:196-204.
30. Burster T., Marin-Esteban V., Boehm B.O., Dunn S., Rotzschke O., Falk K., et al. Design of protease-resistant myelin basic protein-derived peptides by cleavage site directed amino acid substitutions. Biochem Pharmacol 2007, 74:1514-1523.
31. Schroter C.J., Braun M., Englert J., Beck H., Schmid H., Kalbacher H. A rapid method to separate endosomes from lysosomal contents using differential centrifugation and hypotonic lysis of lysosomes. J Immunol Methods 1999, 227:161-168.