The expression of protein disulfide isomerase from Litopenaeus vannamei hemocytes is regulated by bacterial inoculation

Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics

Volumn 4, Issue 3, 2009, Pages 141-146

  Vargas Albores, Francisco ^a   Martínez Martínez, Alejandro ^b   Aguilar Campos, Jorge ^b   Jiménez Vega, Florinda ^b  

^a CENTRO DE INVESTIGACIÓN EN ALIMENTACIÓN Y DESARROLLO   (Mexico)

^b UNIVERSIDAD AUTÓNOMA DE CIUDAD JUÁREZ   (Mexico)

Author keywords

Disulphide bridge; Folding protein; Hemocytes; Immune response; Thioredoxin

Indexed keywords

COMPLEMENTARY DNA; MESSENGER RNA; PROTEIN DISULFIDE ISOMERASE; THIOREDOXIN;

5' UNTRANSLATED REGION; AMINO ACID SEQUENCE; ARTICLE; BLOOD CELL; CONTROLLED STUDY; CRUSTACEA; DNA LIBRARY; ENDOPLASMIC RETICULUM; GENE EXPRESSION REGULATION; IMMUNITY; INVERTEBRATE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN MOTIF; SEQUENCE HOMOLOGY; SHRIMP; VERTEBRATE; VIBRIO ALGINOLYTICUS;

BACTERIA (MICROORGANISMS); CRUSTACEA; DECAPODA (CRUSTACEA); INVERTEBRATA; LITOPENAEUS VANNAMEI; VERTEBRATA; VIBRIO ALGINOLYTICUS;

EID: 67650165713     PISSN: 1744117X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbd.2009.01.001     Document Type: Article

References (60)

1. Ado K., Takeda N., Kikichu M., and Taniguchi Y. The pressure effect on the structure and functions of protein disulfide isomerase. Biochim. Biophys. Acta 1764 (2006) 586-592
2. Akagi S., Yamamoto T., Yoshimori R., Masaki R., Ogawa Y., and Tsashiro. Localization of protein disulfide isomerase on plasma membranes of rat exocrine pancreatic cells. Cytochemistry 36 (1988) 1069-1074
3. Alanen H.I., Williamson R.A., Howard M.J., Lappi A.K., Jantti H.P., Rautio S.M., Kellokumpu S., and Ruddock L.W. Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member. J. Biol. Chem. 278 (2003) 28912-28920
4. Anelli T., Alessio M., Mezghrani A., Simmen T., Talamo F., Bachi A., and Sitia R. ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J. 21 (2002) 835-844
5. Bachère E., Destoumieux D., and Bulet P. Penaeidins, antimicrobial peptides of shrimp: a comparison with other effectors of innate immunity. Aquaculture 191 (2000) 71-88
6. Bartlett T.C., Cuthbertson B.J., Shepard E.F., Chapman R.W., Gross P.S., and Warr G.W. Crustins, homologues of an 11.5-kDa antibacterial peptide, from two species of penaeid shrimp, Litopenaeus vannamei and Litopenaeus setiferus. Mar. Biotechnol. 4 (2002) 278-293
7. Chivers P.T., Laboissiere M.C., and Raines R.T. The CXXC motif: imperatives for the formation of native disulfide bonds in the cell. EMBO J. 15 (1996) 2659-2667
8. Chivers P.T., Prehoda K.E., and Raines R.T. The CXXC motif: a rheostat in the active site. Biochemistry 36 (1997) 4061-4066
9. Cho J., Furie B., Coughlin S., and Furie B. A critical role for extracellular protein disulfide isomerase during thrombus formation in mice. J. Clin. Invest. 118 (2008) 1123-1131
10. Darby N.J., Kemmink J., and Creighton T.E. Identifying and characterizing a structural domain of protein disulfide isomerase. Biochemistry 35 (1996) 10517-10528
11. Desilva M.G., Lu J., Donadel G., Modi W.S., Xie H., Notkins A.L., and Lan M.S. Characterization and chromosomal localization of a new protein disulfide isomerase, PDIp, highly expressed in human pancreas. DNA Cell Biol. 15 (1996) 9-16
12. Destoumieux D., Munoz M., and Bachère E. Penaeidins, a family of antimicrobial peptides from penaeid shrimp (Crustacea, Decapoda). Cell. Mol. Life Sci. 57 (2000) 1260-1271
13. Dyrlov-Bendtsen J., Nielsen H., von-Heijne G., and Brunak S. Improved prediction of signal peptides: SignalP 3.0. J. Mol. Biol. 340 (2004) 783-795
14. Edman J.C. Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature 317 (1985) 267-270
15. Ellgaard L., and Ruddock L.W. The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO J. 6 (2005) 28-32
16. Frand A.R., and Kaiser C.A. Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum. Mol. Biol. Cell 11 (2000) 2833-2843
17. Goo T.W., Yun Y.E., Hwang J., Kang S.-W., Park S., You K.-H., and Kwon O.-Y. Molecular characterization of a Bombyx mori protein disulfide isomerase (bPDI). Cell Stress Chaper. 7 (2002) 118-125
18. Hall T.A. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98NT. Nucleic Acids Symp. Ser. 41 (1999) 95-98
19. Hikima S., Hikima J.-i., Rojtinnakorn J., Hirono I., and Aoki T. Characterization and function of kuruma shrimp lysozyme possessing lytic activity against Vibrio species. Gene 316 (2003) 187-195
20. Horibe T., Gomi M., Iguchi D., Ito H., Kitamura Y., Masuoka T., Tsujimoto I., Kimura T., and Kikuchi M. Different contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding. J. Biol. Chem. 279 (2004) 4604-4611
21. Houston N.L., Fan C.F., Xiang J.Q., Schulze J.M., Jung R., and Boston R.S. Phylogenetic analyses identify 10 classes of the protein disulfide isomerase family in plants, including single-domain protein disulfide isomerase-related proteins. Plant Physiol. 137 (2005) 762-778
22. Huang C.-C., Sritunyalucksana K., Söderhäll K., and Song Y.-L. Molecular cloning and characterization of tiger shrimp (Penaeus monodon) transglutaminase. Dev. Comp. Immunol. 28 (2004) 279-294
23. Jiménez-Vega F., and Vargas-Albores F. A four-kazal domain protein in Litopenaeus vannamei hemocytes. Dev. Comp. Immunol. 29 (2005) 385-391
24. Jiménez-Vega F., and Vargas-Albores F. Isoforms of Litopenaeus vannamei anti-Lipopolysaccharide and its expression by bacterial challenge. J. Shellfish Res. 24 (2007) 1-7
25. Jiménez-Vega F., and Vargas-Albores F. A secretory leukocyte proteinase inhibitor (SLPI)-like protein from Litopenaeus vannamei haemocytes. Fish Shellfish Immunol. 23 (2007) 1119-1126
26. Jiménez-Vega F., Yepiz Plascencia G., Vargas-Albores F., and Söderhäll K. An immunity related single WAP domain-containing protein from Litopenaeus vannamei hemocytes. Biochem. Biophys. Res. Commun. 314 (2004) 681-687
27. Kemmink J., Darby N.J., Dijkstra K., Scheek R.M., and Creighton T.E. Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase. Protein Sci. 4 (1995) 2587-2593
28. Kemmink J., Darby N.J., Dijkstra K., Nilges M., and Creighton T.E. The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules. Curr. Biol. 7 (1997) 239-245
29. Laboissiere M.C., Sturley S.L., and Raines R.T. The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J. Biol. Chem. 270 (1995) 28006-28009
30. LaMantia M., and Lennarz W.J. The essential function of yeast protein isomerase does not reside in its isomerase activity. Cell 74 (1993) 899-908
31. Masip L., Pan J.L., Haldar S., Penner-Hahn J.E., DeLisa M.P., Georgiou G., Bardwell J.C., and Collet J.F. An engineered pathway for the formation of protein disulfide bonds. Science 303 (2004) 1185-1189
32. McKay R., Zhu L., and Shortridge R.D. A Drosophila gene that encodes a member of the protein disulfide isomerase/phospholipase C-alpha family. Insect Biochem. Mol. Biol. 25 (1995) 647-654
33. Montaño-Pérez K., Yepiz-Plascencia G., Higuera-Ciapara I., and Vargas-Albores F. Purification and characterization of the clotting protein from the white shrimp (Penaeus vannamei). Comp. Biochem. Physiol. B 122 (1999) 381-387
34. Murshid A., and Presley J.F. ER-to-Golgi transport and cytoskeletal interactions in animal cells. Cell. Mol. Life Sci. 61 (2004) 133-145
35. Narindrasorasak S., Yao P., and Sarkar B. Protein disulfide isomerase, a multifunctional protein chaperone, shows copper-binding activity. Biochem. Biophys. Res. Commun. 311 (2003) 405-414
36. Natsuka S., Takubo R., Seki R., and Ikura K. Molecular cloning and expression of Caenorhabditis elegans ERp57-homologue with transglutaminase activity. J. Biochem. 130 (2001) 731-735
37. Pirneskoski A., Ruddock L.W., Klappa P., Freedman R.B., Kivirikko K.I., and Koivunen P. Domains b′ and a′ of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. The N-terminal domains a and b enhances this function and can be substituted in part by those of ERp57. J. Biol. Chem. 276 (2001) 11287-11293
38. Pirneskoski A., Klappa P., Lobell M., Williamson R.A., Byrne L., Alanen H.I., Salo K.E., Kivirikko K.I., Freedman R.B., and Ruddock L.W. Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase. J. Biol. Chem. 279 (2004) 10374-10381
39. Puig A., and Gilbert H.F. Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme. J. Biol. Chem. 269 (1994) 7764-7771
40. Reinhardt C., von Bruhl M.L., Manukyan D., Grahl L., Lorenz M., Altmann B., Dlugai S., Hess S., Konrad I., Orschiedt L., Mackmann N., Ruddock L., Massberg S., and Engelmann B. Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation. J. Clin. Invest. 118 (2008) 1110-1122
41. Roux M.M., Pain A., Klimpel K.R., and Dhar A.K. The lipopolysaccharide and β-1,3-glucan binding protein gene is upregulated in white spot virus-infected shrimp (Penaeus stylirostris). J. Virol. 76 (2002) 7140-7149
42. Sambrook J., and Rusell D. Molecular Cloning: A Laboratory Manual. 3rd ed. (2001), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
43. Sevier C.S., and Kaiser C.A. Formation and transfer of disulphide bonds in living cells. Nat. Rev. Mol. Cell Biol. 3 (2002) 836-847
44. Smith J.D., Tang B.C., and Robinson A.S. Protein disulfide isomerase, but not binding protein, overexpression enhances secretion of a non-disulfide-bonded protein in yeast. Biotechnol. Bioeng. 85 (2004) 340-350
45. Söderhäll K., and Cerenius L. Crustacean immunity. Ann. Rev. Fish Dis. (1992) 3-23
46. Söderhäll K., and Cerenius L. Role of the prophenoloxidase-activating system in invertebrate immunity. Curr. Opin. Immunol. 10 (1998) 23-28
47. Sotelo-Mundo R.R., Islas-Osuna M.A., de-la-Re-Vega E., Hernandez-Lopez J., Vargas-Albores F., and Yepiz-Plascencia G. cDNA cloning of the lysozyme of the white shrimp Penaeus vannamei. Fish Shellfish Immunol. 15 (2003) 325-331
48. Sritunyalucksana K.S., Sithisarn P., Withayachumnarnkul B., and Flegel T.W. Activation of prophenoloxidase, agglutinin and antibacterial activity in haemolymph of the black tiger prawn, Penaeus monodon, by immunostimulants. Fish Shellfish Immunol. 9 (1999) 21-30
49. Sritunyalucksana K., Wongsuebsantati K., Johansson M.W., and Söderhäll K. Peroxinectin, a cell adhesive protein associated with the proPO system from the black tiger shrimp, Penaeus monodon. Dev. Comp. Immunol. 25 (2001) 353-363
50. Sritunyalucksana K., Lee S.Y., and Söderhäll K. A β-1,3-glucan binding protein from the black tiger shrimp, Penaeus monodon. Dev. Comp. Immunol. 26 (2002) 237-245
51. Sullivan D.C., Huminiecki L., Moore J.W., Boyle J.J., Poulsom R., Creamer D., Barker J., and Bicknell R. EndoPDI, a novel protein-disulfide isomerase-like protein that is preferentially expressed in endothelial cells acts as a stress survival factor. J. Biol. Chem. 278 (2003) 47079-47088
52. Tamura K., Dudley J., Nei M., and Kumar S. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24 (2007) 1596-1599
53. Tu B.P., and Weissman J.S. Oxidative protein folding in eukaryotes: mechanisms and consequences. J. Cell Biol. 164 (2004) 341-346
54. Turano C., Coppari S., Altieri F., and Ferraro A. Proteins of the PDI family: unpredicted non-ER locations and functions. J. Cell Physiol. 193 (2002) 154-163
55. Vargas-Albores F., and Yepiz-Plascencia G. Beta glucan binding protein and its role in shrimp immune response. Aquaculture 191 (2000) 13-21
56. Vargas-Albores F., Guzmán-Murillo A., and Ochoa J.L. A Lipopolysaccharide-binding agglutinin isolated from brown shrimp (Penaeus californiensis HOLMES) haemolymph. Comp. Biochem. Physiol. A 104 (1993) 407-413
57. Vargas-Albores F., Guzman-Murillo M.A., and Ochoa J.L. An anticoagulant solution for haemolymph collection and prophenoloxidase studies of penaeid shrimp (Penaeus californiensis). Comp. Biochem. Physiol. A 106 (1993) 299-303
58. Vargas-Albores F., Jiménez-Vega F., and Söderhäll K. A plasma protein isolated from brown shrimp (Penaeus californiensis) which enhances the activation of prophenoloxidase system by β-1,3-glucan. Dev. Comp. Immunol. 20 (1996) 299-306
59. Vargas-Albores F., Yepiz Plascencia G., Jiménez-Vega F., and Avila-Villa A. Structural and functional differences of Litopenaeus vannamei crustins. Comp. Biochem. Physiol. B 138 (2004) 415
60. Wilkinson B., and Gilbert H.F. Protein disulfide isomerase. Biochem. Biophys. Acta 1699 (2004) 35-44