Molecular cloning and mRNA expression of cathepsin C gene in black tiger shrimp (Penaeus monodon)

Comparative Biochemistry and Physiology - A Molecular and Integrative Physiology

Volumn 150, Issue 3, 2008, Pages 320-325

  Qiu, Lihua ^a   Jiang, Shigui ^a   Huang, Jianhua ^a   Wang, Weifang ^a   Zhang, Dianchang ^a   Wu, Qiaer ^a   Yang, Keng ^a  

^a SOUTH CHINA SEA FISHERIES RESEARCH INSTITUTE   (China)

Author keywords

Cathepsin C; Molecular cloning; mRNA expression; Penaeus monodon

Indexed keywords

ACUTE PHASE PROTEIN; COMPLEMENTARY DNA; CYSTEINE PROTEINASE; DIPEPTIDE; DIPEPTIDYL PEPTIDASE I; LIPOPOLYSACCHARIDE; MESSENGER RNA; PAPAIN; POLYADENYLIC ACID; POLYPEPTIDE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; FLUORESCENCE; GENE AMPLIFICATION; GENE EXPRESSION; HEPATOPANCREAS; IMMUNITY; ISOELECTRIC POINT; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; POLYADENYLATION; PROTEIN FAMILY; QUANTITATIVE ANALYSIS; REAL TIME POLYMERASE CHAIN REACTION; RNA TRANSCRIPTION; SHRIMP; UPREGULATION;

PENAEUS MONODON;

EID: 44749086356     PISSN: 10956433     EISSN: 15314332     Source Type: Journal    
DOI: 10.1016/j.cbpa.2008.04.001     Document Type: Article

References (38)

1. Bachere E., Gueguen Y., Gonzalez M., de Lorgeril J., Garnier J., and Romestand B. Insights into the anti-microbial defense of marine invertebrates: the penaeid shrimps and the oyster Crassostrea gigas. Immunol. Rev. 198 (2004) 149-168
2. Biswas C., and Mandal C. The role of amoebocytes in endotoxin-mediated coagulation in the innate immunity of Achatina fulica snails. Scand. J. Immunol. 49 (1999) 131-138
3. Brindley P.J., Kalinna B.H., Dalton J.P., Day S.R., Wong J.Y., Smythe M.L., and cManus D.P. Proteolytic degradation of host hemoglobin by schistosomes. Mol. Biochem. Parasitol. 89 (1997) 1-9
4. Cigic ́ B., Kriz ̌aj I., Kralj B., Turk V., and Pain R.H. Stoichiometry and eterogeneity of the pro-region chain in tetrameric human cathepsin C. Biochim. Biophys. Acta 1382 (1998) 143-150
5. Cigic ́ B., Dahl S.W., and Pain R.H. The residual pro-part of cathepsin C fulfills the criteria required for an intramolecular chaperone in folding and stabilizing the human proenzyme. Biochemistry 39 (2000) 12382-12390
6. Coffey J.W., and de Duve C. Digestive activity of lysosomes. I. The digestion of proteins by extracts of rat hepatopancreas lysosomes. J. Biol. Chem. 243 (1968) 3255-3263
7. D'Agrosa R.M., and Callahan J.W. In vitro activation of neuraminidase in the beta-galactosidase-neuraminidase-protective protein complex by cathepsin C. Biochem. Biophys. Res. Commun. 157 (1988) 770-775
8. Dahl S.W., Halkier T., Lauritzen C., Dolenc I., Pedersen J., Turk V., and Turk B. Human recombinant pro-dipeptidyl peptidase I (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic processing. Biochemistry 40 (2001) 1671-1678
9. Dolenc I., Turk B., Pungercic G., Ritonja A., and Turk V. Oligomeric structure and substrate induced inhibition of human cathepsin C. J. Biol. Chem. 270 (1995) 21626-21631
10. Doughty M.J., and Gruenstein E.I. Cell growth and substrate effects on characteristics of a lysosomal enzyme (cathepsin C) in Duchenne muscular dystrophy fibroblasts. Biochem. Cell. Biol. 65 (1987) 617-625
11. Gross P.S., Bartlett T.C., Browdy C.L., Chapman R.W., and Warr G.W. Immune gene discovery by expressed sequence tag analysis of hemocytes and hepatopancreas in the Pacific white shrimp, Litopenaeus vannamei, and the Atlantic white shrimp, L. setiferus. Dev. Comp. Immunol. 25 (2001) 565-577
12. Hu K.J., and Leung P.C. Shrimp cathepsin L encoded by an intronless gene has predominant expression in hepatopancreas, and occurs in the nucleus of oocyte. Comp. Biochem. Physiol., B 137 (2004) 21-33
13. Hu K.J., and Leung P.C. Food digestion by cathepsin L and digestion-related rapid cell differentiation in shrimp hepatopancreas. Comp. Biochem. Physiol., B 146 (2007) 69-80
14. Ishidoh K., Muno D., Sato N., and Kominami E. Molecular cloning of cDNA for rat cathepsin C. Cathepsin C, a cysteine proteinase with an extremely long propeptide. J. Biol. Chem. 266 (1991) 1632-16317
15. Iwanaga S. The molecular basis of innate immunity in the horseshoe crab. Curr. Opin. Immunol. 14 (2002) 87-95
16. In: Katunuma N., and Kominami E. (Eds). Intracellular Proteolysis: Mechanisms and Regulations (1989), Japan Scientific Press, Tokyo, Japan 3-23
17. Kominami E., Ishidoh K., Muno D., and Sato N. The primary structure and tissue distribution of cathepsin C. Biol. Chem. Hoppe-Seyler 373 (1992) 367-373
18. Knop M., Schiffer H.H., Rupp S., and Wolf D.H. Vacuolar/lysosomal proteolysis: proteases, substrates mechanisms. Curr. Opin. Cell Biol. 5 (1993) 990-996
19. Kumar S., Tamura K., and Nei M. MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief. Bioinform. 5 (2004) 150-163
20. Lee S.Y., and Soderhall K. Early events in crustacean innate immunity. Fish Shellfish Immunol. 12 (2002) 421-437
21. Lemaitre B., Nicolas E., Michaut L., Reichhart J.M., and Hoffmann J.A. The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell 86 (1996) 973-983
22. Lynch G.W., and Pfueller S.L. Thrombin-independent activation of platelet factor XIII by endogenous platelet acid protease. Thromb. Haemost. 59 (1988) 372-377
23. McDonald J.K., Callahan P.X., Zeitman B.B., and Ellis S. Inactivation and degradation of glucagon by dipeptidyl aminopeptidase I (cathepsin C) of rat hepatopancreas. J. Biol. Chem. 244 (1969) 6199-6208
24. McGuire M.J., Lipsky P.E., and Thiele D.L. Generation of active myeloid and lymphoid granule serine proteases requires processing by the granule thiol protease dipeptidyl peptidase I.J. Biol. Chem. 268 (1993) 2458-2467
25. Metrione R.M., and MacGeorge N.L. The mechanism of action of dipeptidyl aminopeptidase. Inhibition by amino acid derivatives and amines; activation by aromatic compounds. Biochemistry 14 (1975) 5249-5252
26. Nauland U., and Rijken D.C. Activation of thrombin-inactivated singlechain urokinase-type plasminogen activator by dipeptidyl peptidase I (cathepsin C). Eur. J. Biochem. 223 (1994) 497-501
27. Pham C.T.N., and Ley T.J. Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 8627-8632
28. Pham C.T.N., Armstrong R.J., Zimonjic D.B., Popescu N.C., Payan D.G., and Ley T.J. Molecular cloning, chromosomal localization, and expression of murine dipeptidyl peptidase I. J. Biol. Chem. 272 (1997) 10695-10703
29. Qiu G.F., Yamanoa K., and Unuma T. Cathepsin C transcripts are differentially expressed in the final stages of oocyte maturation in kuruma prawn Marsupenaeus japonicus. Comp. Biochem. Physiol., B 140 (2005) 171-181
30. Rao N.V., Rao G.V., and Hoidal J.R. Human dipeptidyl-peptidase I. Gene characterization, localization, and expression. J. Biol. Chem. 72 (1997) 10260-10265
31. Robalino J., Almeida J.S., McKillen D., Colglazier J., Trent H.F., Chen Y.A., Peck M.E.T., Browdy C.L., Chapman R.W., Warr G.W., and Gross P.S. Insights into the immune transcriptome of the shrimp Litopenaeus vannamei: tissue-specific expression profiles and transcriptomic responses to immune challenge. Physiol. Genomics 29 (2007) 44-56
32. Smyth M.J., McGuire M.J., and Thia K.Y. Expression of recombinant human granzyme B. A processing and activation role for dipeptidyl peptidase I. J. Immunol. 154 (1995) 6299-62305
33. Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTALX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25 (1997) 4876-4882
34. Turk B., Turk V., and Turk D. Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol. Chem. 378 (1997) 141-150
35. Turk V., Turk B., and Turk D. Lysosomal cysteine protease: facts and opportunities. EMBO J. 20 (2001) 4629-4633
36. Ulevitch R.J., and Tobias P.S. Receptor-dependent mechanisms of cell stimulation by bacterial endotoxin. Annu. Rev. Immunol. 13 (1995) 437-457
37. Wolters P.J., Pham C.T., Muilenburg D.J., Ley T.J., and Caughey G.H. Dipeptidyl peptidase I is essential for activation of mast cell chymases, but not tryptases, in mice. J. Biol. Chem. 276 (2001) 18551-18556
38. Zhao Z.-Y., Yin Z.-X., Weng S.-P., Guan H.-J., Li S.-D., Xing K., Chan S.-M., and He J.-G. Profiling of differentially expressed genes in hepatopancreas of white spot syndrome virus-resistant shrimp (Litopenaeus vannamei) by suppression subtractive hybridization. Fish Shellfish Immunol. 22 (2007) 520-534