Molecular cloning, mRNA expression and enzymatic characterization of cathepsin F from olive flounder (Paralichthys olivaceus)

Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

Volumn 154, Issue 2, 2009, Pages 211-220

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

^a Pukyong National University   (South Korea)

^b GEOPHYSICAL LABORATORY   (United States)

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

Author keywords

Cathepsin F; cDNA cloning; Cysteine protease; Epidermal mucus; mRNA expression; Olive flounder; Paralichthys olivaceus

Indexed keywords

CATHEPSIN F; CYSTEINE PROTEINASE; INTERLEUKIN 1BETA; INTERLEUKIN 6; LIPOPOLYSACCHARIDE; MESSENGER RNA;

ANIMAL TISSUE; ARTICLE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; ENZYME ACTIVITY; ESCHERICHIA COLI; EXPRESSION VECTOR; FLOUNDER; GENE EXPRESSION; GILL; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PARALICHTHYS OLIVACEUS; PH; PRIORITY JOURNAL; PROTEIN LOCALIZATION; SEQUENCE ANALYSIS; TISSUE DISTRIBUTION;

ESCHERICHIA COLI; MAMMALIA; PARALICHTHYS OLIVACEUS; PLEURONECTOIDEI;

EID: 67651113435     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2009.06.005     Document Type: Article

References (53)

1. 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
2. Aranishi F., and Mano N. Antibacterial cathepsins in different types of ambicoloured Japanese flounder skin. Fish Shellfish Immunol. 10 (2000) 87-89
3. Barrett A.J., and Kirschke H. Cathepsin B, Cathepsin H, and cathepsin L. Methods Enzymol. 80 (1981) 535-561
4. Berti P.J., and Storer A.C. Alignment/phylogeny of the papain superfamily of cysteine proteases. J. Mol. Biol. 246 (1995) 273-283
5. Bond J.S., and Butler P.E. Intracellular proteases. Annu. Rev. Biochem. 56 (1987) 333-364
6. Chapman H.A., Riese R.J., and Shi G.P. Emerging roles for cysteine proteases in human biology. Annu. Rev. Physiol. 59 (1997) 63-88
7. Corripio-Miyar Y., Bird S., Tsamopoulos K., and Secombes C.J. Cloning and expression analysis of two pro-inflammatory cytokines, IL-1β and IL-8, in haddock (Melanogrammus aeglefinus). Mol. Immunol. 44 (2007) 1361-1373
8. Deussing J., Tisljar K., Papazoglou A., and Peters C. Mouse cathepsin F: cDNA cloning, genomic organization and chromosomal assignment of the gene. Gene 251 (2000) 165-173
9. Dong W.R., Xiang L.X., and Shao J.Z. Cloning and characterisation of two natural killer enhancing factor genes (NKEF-A and NKEF-B) in pufferfish, Tetraodon nigroviridis. Fish Shellfish Immunol. 22 (2007) 1-15
10. Emmadi D., Iwahori A., Hirono I., and Aoki T. cDNA microarray analysis of interleukin-1b-induced Japanese flounder Paralichthys olivaceus kidney cells. Fish. Sci. 71 (2005) 519-530
11. Fabra M., and Cerdà J. Ovarian cysteine proteinases in the teleost Fundulus heteroclitus: molecular cloning and gene expression during vitellogenesis and oocyte maturation. Mol. Reprod. Dev. 67 (2004) 282-294
12. Gildberg A. Aspartic proteinases in fishes and aquatic invertebrates. Comp. Biochem. Physiol. B 91 (1988) 425-435
13. 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
14. Hall T.A. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp. Ser. 41 (1999) 95-98
15. Kumar S., Tamura K., and Nei M. MEGA3: integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment. Brief. Bioinform. 5 (2004) 150-163
16. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
17. Laing K.J., Zou J.J., Wang T., Bols N., Hirono I., Aoki T., and Secombes C.J. Identification and analysis of an interleukin 8-like molecule in rainbow trout Oncorhynchus mykiss. Dev. Comp. Immunol. 26 (2002) 433-444
18. 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
19. Martoglio B., and Dobberstein B. Signal sequences: more than just greasy peptides. Trends Cell Biol. 8 (1998) 410-415
20. Mason R.W., Bergman C.A., Lu G., Frenck Holbrook J., and Sol-Church K. Expression and characterization of cathepsin P. Biochem. J. 378 (2004) 657-663
21. Mommsen T.P. Salmon spawning migration and muscle protein metabolism: the August Krogh principle at work. Comp. Biochem. Physiol. B 139 (2004) 383-400
22. Mommsen T.P., and Korsgaard B. Vitellogenesis. In: Rocha M.J., Arukwe A., and Kapoor B.G. (Eds). Fish reproduction (2008), Science Publishers, New Hampshire
23. Nägler D.K., Sulea T., and Menard R. Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen. Biochem. Biophys. Res. Commun. 257 (1999) 313-318
24. Nam B.H., Byon J.Y., Kim Y.O., Park E.M., Cho Y.C., and Cheong J. Molecular cloning and characterisation of the flounder (Paralichthys olivaceus) interleukin-6 gene. Fish Shellfish Immunol. 23 (2007) 231-236
25. Nielsen H., Engelbrecht J., Brunak S., and von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage site. Protein Eng. 10 (1997) 1-6
26. Petanceska S., and Devi L. Sequence analysis, tissue distribution, and expression of rat cathepsin S. J. Biol. Chem. 267 (1992) 26038-26043
27. Proudfoot N.J., and Brownlee G.G. 3′ non-coding region sequences in eukaryotic messenger RNA. Nature 263 (1976) 211-214
28. Rabkin E., Aikawa M., Stone J.R., Fukumoto Y., Libby P., and Schoen F.J. Activated interstitial myofibroblasts express catabolic enzymes and mediate matrix remodeling in myxomatous heart valves. Circulation 104 (2001) 2525-2532
29. Raldúa D., Fabra M., Bozzo M.G., Weber E., and Cerdà J. Cathepsin B-mediated yolk protein degradation during killifish oocyte maturation is blocked by an H + -ATPase inhibitor: effects on the hydration mechanism. Am. J. Physiol. Regul. Integr. Comp. Physiol. 290 (2006) 456-466
30. Rawlings N.D., and Barrett A.J. Families of cysteine peptidases. Methods Enzymol. 244 (1994) 461-486
31. Rawlings N.D., and Barrett A.J. MEROPS: the peptide database. Nucleic Acids Res. 27 (1999) 325-331
32. 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
33. Shahidi F., and Kamil J.Y. Enzymes from fish and aquatic invertebrates and their application in the food industry. Trends Food Sci. Technol. 12 (2001) 435-464
34. Shi G.P., Bryant R.A., Riese R., Verhelst S., Driessen C., Li Z., Bromme D., Ploegh H.L., and Chapman H.A. Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages. J. Exp. Med. 191 (2000) 1177-1186
35. Smith D.B., and Johnson K.S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67 (1988) 31-40
36. Somoza J.R., Palmer J.T., and Ho J.D. The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators. J. Mol. Biol. 322 (2002) 559-568
37. Subramanian S., MacKinnon S.L., and Ross N.W. A comparative study on innate immune parameters in the epidermal mucus of various fish species. Comp. Biochem. Physiol. B 148 (2007) 256-263
38. 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
39. Tingaud-Sequeira A., and Cerda 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
40. Tisljar K., Deussing J., and Peters C. Cathepsin J, a novel murine cysteine protease of the papain family with a placenta-restricted expression. FEBS Lett. 459 (1999) 299-304
41. Tsujinaka T., Ebisui C., Fujita J., Kishibuchi M., Morimoto T., Ogawa A., Katsume A., Ohsugi Y., Kominami E., and Monden M. Muscle undergoes atrophy in association with increase of lysosomal cathepsin activity in interleukin-6 transgenic mouse. Biochem. Biophys. Res. Commun. 207 (1995) 168-174
42. Tsujinaka T., Kishibuchi M., Yano M., Morimoto T., Ebisui C., Fujita J., Ogawa A., Shiozaki H., Kominami E., and Monden M. Involvement of interleukin-6 in activation of lysosomal cathepsin and atrophy of muscle fibers induced by intramuscular injection of turpentine oil in mice. J. Biochem. 122 (1997) 595-600
43. Turk B., Turk D., and Turk V. Lysosomal cysteine proteases: more than scavengers. Biochim. Biophys. Acta 1477 (2000) 98-111
44. Uinuk-ool T.S., Kuroda T.N., Figueroa F., Sato A., Samonte I.E., Mayer W.E., and Klein J. Phylogeny of antigen-processing enzyme: cathepsins of a cephalochordate, an agnathan and a bony fish. Scand. J. Immunol. 58 (2003) 436-448
45. Vazquez-Ortiz G., Pina-Sanchez P., Vazquez K., Duenas A., Taja L., Mendoza P., Garcia J.A., and Salcedo M. Overexpression of cathepsin F, matrix metalloproteinases 11 and 12 in cervical cancer. BMC Cancer 5 (2005) 68
46. Vernet T., Berti P.J., de Montigny C., Musil R., Tessier D.C., Ménard R., Magny M.C., Storer A.C., and Thomas D.Y. Processing of the papain precursor. The ionization state of a conserved amino acid motif within the Pro region participates in the regulation of intramolecular processing. J. Biol. Chem. 270 (1995) 10838-10846
47. Vihtelic T.S., Fadool J.M., Gao J., Thornton K.A., Hyde D.R., and Wistow G. Expressed sequence tag analysis of zebrafish eye tissues for NEIBank. Mol. Vis. 11 (2005) 1083-1100
48. Wang B., Shi G.P., Yao P.M., Li Z., Chapman H.A., and Brömme D. Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization. J. Biol. Chem. 273 (1998) 32000-32008
49. Wex T., Levy B., Wex H., and Brömme D. Human cathepsins F and W: a new subgroup of cathepsins. Biochem. Biophys. Res. Commun. 259 (1999) 401-407
50. Yasuda Y., Kaleta J., and Brömme D. The role of cathepsins in osteoporosis and arthritis: rationale for the design of new therapeutics. Adv. Drug Deliv. Rev. 57 (2005) 973-993
51. Zhang F.T., Zhang Y.B., Chen Y.D., Zhu R., Dong C.W., Li Y.Y., Zhang Q.Y., and Gui J.F. Expressional induction of Paralichthys olivaceus cathepsin B gene in response to virus, poly I:C and lipopolysaccharide. Fish Shellfish Immunol. 25 (2008) 542-549
52. Zou J., Clark M.S., and Secombes C.J. Characterisation, expression and promoter analysis of an interleukin-10 homologue in the puffer fish, Fugu rubripes. Immunogenetics 55 (2003) 325-335
53. Zou J., Bird S., Truckle J., Bols N., Horne M., and Secombes C. Identification and expression analysis of an IL-18 homologue and its alternatively spliced form in rainbow trout (Oncorhynchus mykiss). Eur. J. Biochem. 271 (2004) 1913-1923