Molecular cloning, tissue distribution and enzymatic characterization of cathepsin X from olive flounder (Paralichthys olivaceus)

Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

Volumn 151, Issue 2, 2008, Pages 203-212

  Ahn, Sang Jung ^a   Kim, Na Young ^a   Jeon, Soo Jin ^b   Sung, Ji Hea ^a   Je, Ju Eun ^a   Seo, Jung Soo ^c   Kim, Moo Sang ^a   Kim, Joong Kyun ^a   Chung, Joon Ki ^a   Lee, Hyung Ho ^a  

^a Pukyong National University   (South Korea)

^b STONY BROOK UNIVERSITY   (United States)

^c National Fisheries Research and Development Institute (NFRDI)   (South Korea)

Author keywords

Cathepsin X; cDNA cloning; Cysteine protease; Olive flounder; Paralichthys olivaceus; Polyclonal antibody

Indexed keywords

ANTIPAIN; CATHEPSIN; CATHEPSIN X; COMPLEMENTARY DNA; ENZYME PRECURSOR; GLUTATHIONE TRANSFERASE; LEUPEPTIN; LIPOPOLYSACCHARIDE; POLYCLONAL ANTIBODY; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME LINKED IMMUNOSORBENT ASSAY; ENZYME LOCALIZATION; FLOUNDER; GENE EXPRESSION; GENE OVEREXPRESSION; GENETIC CONSERVATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PARALICHTHYS OLIVACEUS; PH; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN MOTIF; PROTEIN PURIFICATION; REAL TIME POLYMERASE CHAIN REACTION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SEQUENCE ANALYSIS; TISSUE DISTRIBUTION; WESTERN BLOTTING;

ESCHERICHIA COLI; PARALICHTHYS OLIVACEUS;

EID: 50049093472     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2008.07.001     Document Type: Article

References (55)

1. Adachi W., Kawamoto S., Ohno I., Nishida K., Kinoshita S., Matsubara K., and Okubo K. Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium. Invest. Ophthalmol. Vis. Sci. 39 (1998) 1789-1796
2. Ahn S.J., Seo J.S., Kim M.S., Jeon S.J., Kim N.Y., Jang J.H., Kim K.H., Hong Y.K., Chung J.K., and Lee H.H. Cloning, site-directed mutagenesis and expression of cathepsin L-like cysteine protease from Uronema marinum (Ciliophora: Scuticociliatida). Mol. Biochem. Parasitol. 156 (2007) 191-198
3. Alves M.F., Araújo M.C., Juliano M.A., Oliveira E.M., Krieger J.E., Casarini D.E., Juliano L., and Carmona A.K. A continuous fluorescent assay for the determination of plasma and tissue angiotensin I-converting enzyme activity. Braz. J. Med. Biol. Res. 38 (2005) 861-868
4. Araújo M.C., Melo R.L., Cesari M.H., Juliano M.A., Juliano L., and Carmona A.K. Peptidase specificity characterization of C- and N-terminal catalytic sites of angiotensin I-converting enzyme. Biochemistry 39 (2000) 8519-8525
5. Barrett A.J., and Kirschke H. Cathepsin B, cathepsin H, and cathepsin L. Meths. Enzymol. 80 (1981) 535-561
6. Barrett A.J., Rawlings N.D., and Woessner F.J. Handbook of Proteolytic Enzymes (1998), Academic Press, London 1-1666
7. Berdowska I. Cysteine proteases as disease markers. Clin Chim. Acta. 342 (2004) 41-69
8. Bird S., Zou J., Wang T., Munday B., Cunningham C., and Secombes C.J. Evolution of interleukin-1beta. Cytokine Growth Factor Rev. 13 (2002) 483-502
9. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
10. Brömme D., Nallaseth F.S., and Turk B. Production and activation of recombinant papain-like cysteine proteases. Methods 32 (2004) 199-206
11. Dacks J.B., Kuru T., Liapounova N.A., and Gedamu L. Phylogenetic and primary sequence characterization of cathepsin B cysteine proteases from the oxymonad flagellate monocercomonoides. J. Eukaryot. Microbiol. 55 (2008) 9-17
12. Dickinson D.P. Cysteine peptidases of mammals: their biological roles and potential effects in the oral cavity and other tissues in health and disease. Crit. Rev. Oral. Biol. Med. 13 (2002) 238-275
13. Engelsma M.Y., Stet R.J., Schipper H., and Verburg-van Kemenade B.M. Regulation of interleukin 1 beta RNA expression in the common carp, Cyprinus carpio L. Dev. Comp. Immunol. 25 (2001) 195-203
14. Giulietti A., Overbergh L., Valckx D., Decallonne B., Bouillon R., and Mathieu C. An overview of real-time quantitative PCR: applications to quantify cytokine gene expression. Methods 25 (2001) 386-401
15. Hall T.A. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp. 41 (1999) 95-98
16. Kao C.M., and Huang F.L. Cloning and expression of carp cathepsin Z: possible involvement in yolk metabolism. Comp. Biochem. Physiol. B 149 (2008) 541-551
17. Karrer K.M., Peiffer S.L., and DiTomas M.E. Two distinct gene subfamilies within the family of cysteine protease genes. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 3063-3067
18. Kirschke H., and Barrett A.J. Chemistry of lysosomal proteinases. In: Glaumann, and Ballard (Eds). Lysosomes: Their Role in Protein Breakdown (1987), Academic Press, New York 193-238
19. Krueger S., Kalinski T., Hundertmark T., Wex T., Küster D., Peitz U., Ebert M., Nägler D.K., Kellner U., Malfertheiner P., Naumann M., Röcken C., and Roessner A. Up-regulation of cathepsin X in Helicobacter pylori gastritis and gastric cancer. J. Pathol. 207 (2005) 32-42
20. Kumar S., Tamura K., and Nei M. MEGA3: integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment. Brief Bioinform. 5 (2004) 150-163
21. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
22. Lanio M.E., Alvarez C., Pazos F., Martinez D., Martínez Y., Casallanovo F., Abuin E., Schreier S., and Lissi E. Effects of sodium dodecyl sulfate on the conformation and hemolytic activity of St I and St II, two isotoxins purified from Stichodactyla helianthus. Toxicon 41 (2003) 65-70
23. Lecaille F., Kaleta J., and Brömme D. Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design. Chem. Rev. 102 (2002) 4459-4488
24. Lim S.U., Seo J.S., Kim M.S., Ahn S.J., Jeong H.D., Kim K.H., Park N.G., Kim J.K., Chung J.K., and Lee H.H. Molecular cloning and characterization of cathepsin B from a scuticociliate, Uronema marinum. Comp. Biochem. Physiol. B 142 (2005) 283-292
25. Linnevers C.J., Smeekens S.P., and Bromme D. Human cathepsin W, a putative cysteine protease predominantly expressed in CD8+ T-lymphocytes. FEBS Lett. 405 (1997) 253-259
26. Liu W., and Spero D.M. Cysteine protease cathepsin S as a key step in antigen presentation. Drug News Perspect. 17 (2004) 357-363
27. Lusson J., Benjannet S., Hamelin J., Savaria D., Chrétien M., and Seidah N.G. The integrity of the RRGDL sequence of the proprotein convertase PC1 is critical for its zymogen and C-terminal processing and for its cellular trafficking. J. Biol. Chem. 326 (1997) 737-744
28. Martoglio B., and Dobberstein B. Signal sequences: more than just greasy peptides. Trends Cell Biol. 8 (1998) 410-415
29. McGrath M.E. The lysosomal cysteine proteases. Annu. Rev. Biophys. Biomol. Struct. 28 (1999) 181-204
30. McKerrow J.H., Engel J.C., and Caffrey C.R. Cysteine protease inhibitors as chemotherapy for parasitic infections. Bioorg. Med. Chem. 7 (1999) 639-644
31. Nägler D.K., and Ménard R. Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions. FEBS Lett. 434 (1998) 135-139
32. Nägler D.K., Zhang R., Tam W., Sulea T., Purisima E., and Menard R. Human cathepsin X a cysteine protease with unique carboxypeptidase activity. Biochemistry 38 (1999) 12648-12654
33. Nägler D.K., Lechner A.M., Oettl A., Kozaczynska K., Scheuber H.P., Gippner-Steppert C., Bogner V., Biberthaler P., and Jochum M. An enzyme-linked immunosorbent assay for human cathepsin X, a potential new inflammatory marker. J. Immunol. Methods 308 (2006) 241-250
34. Nielsen H., Engelbrecht J., Brunak S., and Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage site. Protein Eng. 10 (1997) 1-6
35. Otto H.H., and Schirmeister T. Cysteine proteases and their inhibitors. Chem. Rev. 97 (1997) 133-172
36. Proudfoot N.J., and Brownlee G.G. 3′ non-coding region sequences in eukaryotic messenger RNA. Nature 263 (1976) 211-214
37. Rawlings N.D., and Barret A.J. Families of cysteine peptidases. Methods Enzymol. 244 (1994) 461-486
38. Rawlings N.D., Morton F.R., and Barrett A.J. MEROPS: the peptidase database. Nucleic Acids Res. 34 (2006) D270-D272
39. Rosenthal P.J., Sijwali P.S., Singh A., and Shenai B.R. Cysteine proteases of malaria parasites: targets for chemotherapy. Curr. Pharm. Des. 8 (2002) 1659-1672
40. Sabatini R.A., Bersanetti P.A., Farias S.L., Juliano L., Juliano M.A., Casarini D.E., Carmona A.K., Paiva A.C., and Pesquero J.B. Determination of angiotensin I-converting enzyme activity in cell culture using fluorescence resonance energy transfer peptides. Anal. Biochem. 363 (2007) 255-262
41. Saitou N., and Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4 (1987) 406-425
42. Sakamoto E., Sakao Y., Taniguchi Y., and Yamafuji K. Cathepsin Y (a novel thiol enzyme) produces kinin potentiating peptide from the component protein of rat plasma. Immunopharmacology 45 (1999) 207-214
43. Santamaría I., Velasco G., Pendás A.M., Fueyo A., and López-Otín C. Cathepsin Z, a novel human cysteine proteinase with at short propeptide domain and a unique chromosomal location. J. Biol. Chem. 273 (1998) 16816-16823
44. Santamaría I., Velasco G., Pendás A.M., Paz A., and López-Otín C. Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain. J. Biol. Chem. 274 (1999) 13800-13809
45. Seppola M., Larsen A.N., Steiro K., Robertsen B., and Jensen I. Characterisation and expression analysis of the interleukin genes, IL-1beta, IL-8 and IL-10, in Atlantic cod (Gadus morhua L.). Mol. Immunol. 45 (2008) 887-897
46. Sol-Church K., Frenck J., Troeber D., and Mason R.W. Cathepsin P, a novel protease in mouse placenta. Biochem. J. 343 (1999) 307-309
47. Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
48. Tingaud-Sequeira A., and Cerdà J. Phylogenetic relationships and gene expression pattern of three different cathepsin L (Ctsl) isoforms in zebrafish: Ctsla is the putative yolk processing enzyme. Gene 386 (2007) 98-106
49. Towbin H., and Gordon J. Immunoblotting and dot immunoblotting: current status and outlook,. J. Immunol. Meths. 72 (1984) 313-340
50. Turk B., Turk D., and Turk V. Lysosomal cysteine proteases: more than scavengers. Biochim. Biophys. Acta. 1477 (2000) 98-111
51. Velasco G., Ferrando A.A., Puente X.S., Sánchez L.M., and López-Otín C. Human cathepsin O. Molecular cloning from a breast carcinoma, production of the active enzyme in Escherichia coli, and expression analysis in human tissues. J. Biol. Chem. 269 (1994) 27136-27142
52. Vernet T., Berti P.J., Montigny C., Musil R., Tessier D.C., Ménard R., Magny M.C., Storre A.C., and Thomas D.Y. Processing of the papain precursor. J. Biol. Chem. 270 (1995) 10838-10846
53. Wang B., Shi G.P., Yao P.M., Li Z., Chapman H.A., and Bromme D. Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization. J. Biol. Chem. 273 (1998) 32000-32008
54. Xu Z.J., Nakajima M., Suzuki Y., and Yamaguchi I. Cloning and characterization of the abscisic acid-specific glucosyltransferase gene from adzuki bean seedlings. Plant Physiol. 129 (2002) 1285-1295
55. Zou J., Holland J., Pleguezuelos O., Cunningham C., and Secombes C.J. Factors influencing the expression of interleukin-1 beta in cultured rainbow trout (Oncorhynchus mykiss) leucocytes. Dev. Comp. Immunol. 24 (2000) 575-582