Biochemical properties of the monomeric mutant of human cathepsin E expressed in Chinese hamster ovary cells: Comparison with dimeric forms of the natural and recombinant cathepsin E

Journal of Biochemistry

Volumn 119, Issue 1, 1996, Pages 126-134

  Tsukuba, Takayuki ^a   Sakai, Hideaki ^b   Yamada, Masayuki ^c   Maeda, Hidefumi ^a   Hori, Hitoshi ^c   Azuma, Takeshi ^d   Akamine, Akifumi ^a   Yamamoto, Kenji ^a  

^a KYUSHU UNIVERSITY   (Japan)

^b NAGASAKI UNIVERSITY   (Japan)

^c TOSOH CORPORATION   (Japan)

^d UNIVERSITY OF FUKUI   (Japan)

Author keywords

Aspartic proteinase; Cathepsin D; Cathepsin E; Monomer mutant; Structural stabilization

Indexed keywords

ASPARTIC PROTEINASE; CATHEPSIN D; CYSTEINE; DIMER; MONOMER; RECOMBINANT PROTEIN;

ANIMAL CELL; ARTICLE; BIOCHEMISTRY; CHO CELL; COMPARATIVE STUDY; DISULFIDE BOND; ENDOPLASMIC RETICULUM; ENDOSOME; HUMAN; HUMAN CELL; NONHUMAN; PH; PROTEIN LOCALIZATION; SITE DIRECTED MUTAGENESIS; TEMPERATURE;

EID: 0030028617     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021197     Document Type: Article

References (35)

1. Takeda-Ezaki, M. and Yamamoto, K. (1993) Isolation and biochemical characterization of procathepsin E from human erythrocyte membranes. Arch. Biochem. Biophys. 304, 352-358
2. Yonezawa, S., Takahashi, T., Ichinise, M., Miki, K., Tanaka, J., and Gasa, S. (1990) Structural studies of rat cathepsin E: Amino-terminal structure and carbohydrate units of mature enzyme. Biochem. Biophys. Res. Commun. 166, 1032-1038
3. Okamoto, K., Yu, H., Misumi, Y., Ikehara, Y., and Yamamoto, K. (1995) Isolation and sequencing of two cDNA clones encoding rat spleen cathepsin E and analysis of the activation of purified procathepsin E. Arch. Biochem. Biophys. 322, 103-111
4. Saku, T., Sakai, H., Shibata, Y., Kato, Y., and Yamamoto, K. (1991) An immunocytochemical study on distinct intracellular localization of cathepsin E and cathepsin D in human gastric cells and various rat cells. J. Biochem. 110, 956-964
5. Muto, N., Yamamoto, M., Tani, S., and Yonezawa, S. (1988) Characteristic distribution of cathepsin E which immunologically cross-reacts with the 86-kDa acid proteinase from rat gastric mucosa. J. Biochem. 103, 629-632
6. Sakai, H., Saku, T., Kato, Y., and Yamamoto, K. (1989) Quantitation and immunohistochemical localization of cathepsins D and E in rat tissues and blood cells. Biochim. Biophys. Acta 991, 367-375
7. Kageyama, T., Ichinose, M., Tsukada, S., Miki, K., Kurosawa, K., Koiwa, O., Tanji, M., Yakabe, E., Athauda, S.B.P., and Takahashi, K. (1992) Gastric procathepsin E and progastricsin from guinea pig: Purification, molecular cloning of cDNAs, and characterization of enzymatic properties, with special reference to procathesin E. J. Biol. Chem. 267, 16450-16459
8. Yamamoto, K., Yamamoto, H., Takeda, M., and Kato, Y. (1988) An aspartic proteinase of erythrocyte membranes: Proposed mechanism for activation and further molecular properties. Biol. Chem. Hoppe-Seyler 396, 315-322
9. Barrett, A.J. (1977) Cathepsin D and other carboxyl proteinases in Proteinases in Mammalian Cells and Tissues, pp. 209-248, Elsevier-North-Holland, Amsterdam
10. Tsukuba, T., Yamada, M., Hori, H., Azuma, T., and Yamamoto, K. (1995) Comparative studies on dimeric and monomeric forms of human cathepsin E in Intracellular Protein Catabolism (Bond, J.S. and Suzuki, K., eds.) Proc. 10th ICOP Symp., Plenum Press, Tokyo, in press
11. Fowler, S.D., Kay, J., Dunn, B.M., and Tatnell, P.J. (1995) Monomeric human cathepsin E. FEBS Lett. 366, 72-74
12. Tsukuba, T., Hori, H., Azuma, T., Takahashi, T., Taggart, R.T., Akamine, A., Ezaki, M., Nakanishi, H., Sakai, H., and Yamamoto, K. (1993) Isolation and characterization of recombinant human cathepsin E expressed in Chinese hamster overy cells. J. Biol. Chem. 268, 7276-7282
13. Sakai, H., Kato, Y., and Yamamoto, K. (1992) Synthesis and intracellular distribution of cathepsin E in differentiating murine Friend erythroleukemiacells. Arch. Biochem. Biophys. 294, 412-417
14. Ichimaru, E., Sakai, H., Saku, T., Kunimatsu, K., Kato, Y., Kato, I., and Yamamoto, K. (1990) Characterization of hemoglobin-hydrolyzed acidic proteinases in human and rat neutrophils. J. Biochem. 108, 1009-1015
15. Finzi, G., Cornaggia, M., Capella, C., Fiocca, R., Bosi, F., Solcia, E., and Samloff, I.M. (1993) Cathepsin E in follicle associated epithelium of intestine and tonsils: Localization to M cells and possible role in antigen processing. Histochemistry 99, 201-211
16. Yoshimine, Y., Tsukuba, T., Isobe, R., Sumi, M., Akamine, A., Maeda, K., and Yamamoto, K. (1995) Specific immunocytochemical localization of cathepsin E at the ruffled border membrane of active osteoclasts. Cell Tissue Res. 281, 85-91
17. Finley, E.M. and Kornfeld, S. (1994) Subcellular localization and targeting of cathepsin E. J. Biol. Chem. 269, 31259 31266
18. Yamamoto, K. and Marchesi, V.T. (1984) Purification and characterization of acid proteinase from human erythrocyte membranes. Biochim. Biophys. Acta 790, 208-218
19. Yamamoto, K., Katsuda, N., Himeno, M., and Kato, K. (1979) Cathepsin D of rat spleen: Affinity purification and properties of two types of cathepsin D. Eur. J. Biochem. 95, 459-467
20. Yamamoto, K., Takeda, M., Yamamoto, H., Tatsumi, M., and Kato, Y. (1985) Human erythrocyte membrane acid proteinase (EMAP): Sidedness and relation to cathepsin D. J. Biochem. 97, 821-830
21. Takeda, M., Ueno, E., Kato, Y., and Yamamoto, K. (1986) Isolation and catalytic and immunochemical properties of cathepsin D-like acid proteinase from rat erythrocyte. J. Biochem. 100, 1269-1277
22. Kunkel, T. A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82, 488-492
23. Sanger, F., Nicklen, S., and Coulson, A.R. (1977) DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74, 5463-5467
24. Barrett, A.J. and Kirschke, H. (1981) Cathepsin B, cathepsin H, and cathepsin L in Methods in Enzymology (Lorand, L., ed.) Vol. 80, pp. 535-561, Academic Press, San Diego
25. Yamamoto, K., Kamata, O., and Kato, Y. (1984) Differential effects of anti-inflammatory agents on lysosomal cysteine proteinases cathepsins B and H from rat spleen. Jpn. J. Pharmacol. 35, 253-258
26. Robins, E., Hirsh, H.E., and Emmons, S.S. (1968) Glycosidase in neurous system I: Assay, some properties and distribution of β-galactosidase, β-glucuronidase and β-glucosidase. J. Biol. Chem. 243, 4246-4252
27. Lowry, O.H., Rosebrough, N.J., Farr, A.L., and Landall, R.J. (1951) Protein measurement with the folin phenol reagent. J. Biol. Chem. 193, 265-275
28. Goto, T., Tsukuba, T., Ayasaka, N., Yamamoto, K., and Tanaka, T. (1992) Immunocytochemical localization of cathepsin D in the rat osteoclast. Histochemistry 97, 13 18
29. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
30. Towbin, H., Steahelin, T., and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354
31. Hartmann, E., Gorlich, D., Kostka, S., Otto, A., Kraft, R., Knespel, S., Burger, E., Rapoport, T.A., and Prehn, S. (1993) A tetrameric complex of membrane proteins in the endoplasmic reticulum. Eur. J. Biochem. 214, 375-381
32. Thomas, D.J., Richards, A.D., Jupp, R.A., Ueno, E., Yamamoto, K., Samloff, I.M., Dunn, B.M., and Kay, J. (1989) Stabilization of cathepsin E by ATP. FEBS Lett. 243, 145-148
33. Yamamoto, K., Sakai, H., Ueno, E., and Kato, Y. (1991) Biological significance and activity control of cathepsin E in Structure and Functuion of the Aspartic Proteinases (Dunn, B.M., ed.) pp. 297-306, Plenum Press, New York
34. Athauda, S.B.P., Takahashi, T., Kageyama, T., and Takahashi, K. (1991) Autocatalytic processing of procathepsin E to cathepsin E and their structural differences. Biochem. Biophys. Res. Commun. 175, 152-158
35. Kageyama, T. (1993) Rabbit procathepsin E and cathepsin E: Nucleotide sequence of cDNA, hydrolytic specificity for biologically active peptides and gene expression during development. Eur. J. Biochem. 216, 717-728