Heparin cofactor II (RbHCII) from rock bream (Oplegnathus fasciatus): Molecular characterization, cloning and expression analysis

Fish and Shellfish Immunology

Volumn 30, Issue 1, 2011, Pages 194-208

  Umasuthan, Navaneethaiyer ^a   Whang, Ilson ^a   Lee, Youngdeuk ^a   Lee, Sukkyoung ^a   Kim, Yucheol ^a   Kim, Hyowon ^a   Jung, Sung Ju ^b   Oh, Myung Joo ^b   Choi, Cheol Young ^c   Yeo, Sang Yeob ^d   Lee, Sang Jun ^e   Lee, Jehee ^a  

^a Jeju National University   (South Korea)

^b Chonnam National University   (South Korea)

^c Hanbat National University   (South Korea)

^d Korea Maritime University   (South Korea)

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

Author keywords

Anti coagulation; Heparin cofactor II; Inhibitory activity; Rock bream; Serpin

Indexed keywords

EDWARDSIELLA TARDA; GASTEROSTEUS ACULEATUS; HYPEROGLYPHE POROSA; IRIDOVIRUS; OPLEGNATHUS FASCIATUS; ROCK BREAM IRIDOVIRUS; VERTEBRATA;

EID: 78650684871     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2010.10.004     Document Type: Article

References (60)

1. Cera E., Cantwell A. Determinants of thrombin specificity. Ann N Y Acad Sci 2001, 936:133-146.
2. Sim R., Laich A. Serine proteases of the complement system. Biochem Soc Trans 2000, 28:545-550.
3. Mark D.E., Lazzari K.G., Simson E.R. Are serine proteases involved in immune complex activation of neutrophils?. J Leukoc Biol 1988, 44:441-447.
4. Chasan R., Anderson K.V. The role of easter, an apparent serine protease, in organizing the dorsal-ventral pattern of the Drosophila embryo. Cell 1989, 56:391-400.
5. Law R.H., Zhang Q., McGowan S., Buckle A.M., Silverman G.A., Wong W., et al. An overview of the serpin superfamily. Genome Biol 2006, 7:216.
6. Silverman G.A., Bird P.I., Carrell R.W., Church F.C., Coughlin P.B., Gettins P.G., et al. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. J Biol Chem 2001, 276:33293-33296.
7. van Gent D., Sharp P., Morgan K., Kalsheker N. Serpins: structure, function and molecular evolution. Int J Biochem Cell Biol 2003, 35:1536-1547.
8. Huntington J.A., Read R.J., Carrell R.W. Structure of a serpin-protease complex shows inhibition by deformation. Nature 2000, 407:923-926.
9. Gettins P.G. Keeping the serpin machine running smoothly. Genome Res 2000, 10:1833-1835.
10. Irving J.A., Pike R.N., Lesk A.M., Whisstock J.C. Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function. Genome Res 2000, 10:1845-1864.
11. Ragg H., Lokot T., Kamp P.B., Atchley W.R., Dress A. Vertebrate serpins: construction of a conflict-free phylogeny by combining exon-intron and diagnostic site analyses. Mol Biol Evol 2001, 18:577-584.
12. Rawlings N.D., Barrett A.J., Bateman A. MEROPS: the peptidase database. Nucleic Acids Res 2010, 38:D227-D233.
13. Tollefsen D.M., Pestka C.A., Monafo W.J. Activation of heparin cofactor II by dermatan sulfate. J Biol Chem 1983, 258:6713-6716.
14. Parker K.A., Tollefsen D.M. The protease specificity of heparin cofactor II. Inhibition of thrombin generated during coagulation. J Biol Chem 1985, 260:3501-3505.
15. Church F.C., Noyes C.M., Griffith M.J. Inhibition of chymotrypsin by heparin cofactor II. Proc Natl Acad Sci U S A 1985, 82:6431-6434.
16. He L., Vicente C.P., Westrick R.J., Eitzman D.T., Tollefsen D.M. Heparin cofactor II inhibits arterial thrombosis after endothelial injury. J Clin Invest 2002, 109:213-219.
17. Tollefsen D.M. The interaction of glycosaminoglycans with heparin cofactor II. Ann N Y Acad Sci 1994, 714:21-31.
18. Ragg H., Ulshöfer T., Gerewitz J. On the activation of human leuserpin-2, a thrombin inhibitor, by glycosaminoglycans. J Biol Chem 1990, 265:5211-5218.
19. Blinder M.A., Marasa J.C., Reynolds C.H., Deaven L.L., Tollefsen D.M. Heparin cofactor II: cDNA sequence, chromosome localization, restriction fragment length polymorphism, and expression in Escherichia coli. Biochemistry 1988, 26(27):752-759.
20. Sheffield W.P., Schuyler P.D., Blajchman M.A. Molecular cloning and expression of rabbit heparin cofactor II: a plasma thrombin inhibitor highly conserved between species. Thromb Haemost 1994, 71:778-782.
21. Colwell N.S., Tollefsen D.M. Isolation of frog and chicken cDNAs encoding heparin cofactor II. Thromb Haemost 1998, 80:784-790.
22. Droegea M., Hill B. The genome sequencer FLXTM System-Longer reads, more applications, straight forward bioinformatics and more complete data sets. J Biotechnol 2008, 136:3-10.
23. Bairoch A., Bucher P., Hofmann K. The PROSITE data base, its status in 1997. Nucleic Acids Res 1997, 25:217-221.
24. Letunic I., Doerks T., Bork P. SMART 6: recent updates and new developments. Nucleic Acids Res 2009, 37:D229-D232.
25. Bendtsen J.D., Nielsen H., von Heijne G., Brunak S. Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 2004, 340:783-795.
26. Chang W.C., Lee T.Y., Shien D.M., Hsu J.B., Horng J.T., Hsu P.C., et al. Incorporating support vector machine for identifying protein tyrosine sulfation sites. J Comput Chem 2009, 30:2526-2537.
27. Thompson J.D., Higgins D.G., 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 1994, 22:4673-4680.
28. Kumar S., Tamura K., Nei M. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief Bioinformatics 2004, 5:150-163.
29. Arnold K., Bordoli L., Kopp J., Schwede T. The SWISS-MODEL Workspace: a web-based environment for protein structure homology modelling. Bioinformatics 2006, 22:195-201.
30. Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using real time quantitative PCR and the 2ΔΔCT method. Methods 2001, 25:402-408.
31. Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
32. Baglin T.P., Carrell R.W., Church F.C., Esmon C.T., Huntington J.A. Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism. Proc Natl Acad Sci U S A 2002, 99:11079-11084.
33. Colwell N.S., Grupe M.J., Tollefsen D.M. Amino acid residues of heparin cofactor II required for stimulation of thrombin inhibition by sulphated polyanions. Biochim Biophys Acta 1999, 1431:148-156.
34. Bourin M.C., Lindahl U. Glycosaminoglycans and the regulation of blood coagulation. Biochem J 1993, 289:313-330.
35. Hayakawa Y., Hirashima Y., Kurimoto M., Hayashi N., Hamada H., Kuwayama N., et al. Contribution of basic residues of the A helix of heparin cofactor II to heparin- or dermatan sulfate-mediated thrombin inhibition. FEBS Lett 2002, 522:147-150.
36. Jagadeeswaran P., Sheehan J.P. Analysis of blood coagulation in the zebrafish. Blood Cells Mol Dis 1999, 25:239-249.
37. Sheehan J., Templer M., Gregory M., Hanumanthaiah R., Troyer D., Phan T., et al. Demonstration of the extrinsic coagulation pathway in teleostei: identification of zebrafish coagulation factor VII. Proc Natl Acad Sci U S A 2001, 98:8768-8773.
38. Dias M.T., Olivira S.R. A review of blood coagulation system of fish. Braz J Biosci 2009, 7:205-224.
39. Park K.C., Osborne J.A., Tsoi S.C., Brown L.L., Johnson S.C. Expressed sequence tags analysis of Atlantic halibut (Hippoglossus hippoglossus) liver, kidney and spleen tissues following vaccination against Vibrio anguillarum and Aeromonas salmonicida. Fish Shellfish Immunol 2005, 18:393-415.
40. Arma N.R., Hirono I., Aok T. Identification of genes expressed in the liver of Japanese flounder Paralichthys olivaceus by expressed sequence tags. Fish Sci 2005, 71:504-518.
41. Hanumanthaiah R., Day K., Jagadeeswaran P. Comprehensive analysis of blood coagulation pathways in teleostei: evolution of coagulation factor genes and identification of zebrafish factor VIIi. Blood Cells Mol Dis 2002, 29:57-68.
42. Huang C.J., Lee M.S., Huang F.L., Chang G.D. A protease inhibitor of the serpin family is a major protein in carp perimeningeal fluid: II. cDNA cloning, sequence analysis, and Escherichia coli expression. J Neurochem 1995, 64:1721-1727.
43. Andersen O., Flengsrud R., Norberg K., Salte R. Salmon antithrombin has only three carbohydrate side chains, and shows functional similarities to human beta-antithrombin. Eur J Biochem 2000, 267:1651-1657.
44. Pratt C.W., Whinna H.C., Meade J.B., Treanor R.E., Church F.C. Physicochemical aspects of heparin cofactor II. Ann N Y Acad Sci 1989, 556:104-115.
45. Church F.C., Meade J.B., Pratt C.W. Structure-function relationships in heparin cofactor II: spectral analysis of aromatic residues and absence of a role for sulfhydryl groups in thrombin inhibition. Arch Biochem Biophys 1987, 259:331-340.
46. Pike R.N., Buckle A.M., le Bonniec B.F., Church F.C. Control of the coagulation system by serpins. Getting by with a little help from glycosaminoglycans. FEBS J 2005, 272:4842-4851.
47. Tollefsen D.M. Heparin cofactor II modulates the response to vascular injury. Arterioscler Thromb Vasc Biol 2007, 27:454-460.
48. Kumar A. Delving into vertebrate serpins for understanding their evolution. Nat Precedings 2009, http://dx.doi.org/10.1038/npre.2009.3050.1.
49. Church F.C., Pratt C.W., Hoffman M. Leukocyte chemoattractant peptides from the serpin heparin cofactor II. J Biol Chem 1999, 266:704-709.
50. Kamp P., Strathmann A., Ragg H. Heparin cofactor II, antithrombin-beta and their complexes with thrombin in human tissues. Thromb Res 2001, 101:483-491.
51. Hoffman M., Loh K.L., Bond V.K., Palmieri D., Ryan J.L., Church F.C. Localization of heparin cofactor II in injured human skin: a potential role in wound healing. Exp Mol Pathol 2003, 2003(75):109-118.
52. Dawes K.E., Gray A.J., Laurent G.J. Thrombin stimulates fibroblast chemotaxis and replication. Eur J Cell Biol 1993, 61:126-130.
53. Cohen W.M., Wu H.F., Featherstone G.L., Jenzano J.W., Lundblad R.L. Linkage between blood coagulation and inflammation: stimulation of neutrophil tissue kallikrein by thrombin. Biochem Biophys Res Commun 1991, 176:315-320.
54. Bar-Shavit R., Kahn A., Fenton J.W., Wilner G.D. Chemotactic response of monocytes to thrombin. J Cell Biol 1983, 96:282-285.
55. Shrivastava S., McVey J.H., Dorling A. The interface between coagulation and immunity. Am J Transplant 2007, 7:499-506.
56. Hewett J.A., Roth R.A. The coagulation system, but not circulating fibrinogen, contributes to liver injury in rats exposed to lipopolysaccharide from gram-negative bacteria. J Pharmacol Exp Ther 1995, 272:53-62.
57. Yee S.B., Harkema J.R., Ganey P.E., Roth R.A. The coagulation system contributes to synergistic liver injury from exposure to monocrotaline and bacterial lipopolysaccharide. Toxicol Sci 2003, 74:457-469.
58. Michie H.R., Manogue K.R., Spriggs D.R., Revhaug A., O'Dwyer S., Dinarello C.A., et al. Detection of circulating tumor necrosis factor after endotoxin administration. N Engl J Med 1988, 318:1481-1486.
59. Copple B.L., Moulin F., Hanumegowda U.M., Ganey P.E., Roth R.A. Thrombin and protease-activated receptor-1 agonists promote lipopolysaccharide-induced hepatocellular injury in perfused livers. J Pharmacol Exp Ther 2003, 305:417-425.
60. Vasseur S., Hoffmeister A., Garcia-Montero A., Barthet M., Saint-Michel L., Berthézène P., et al. Mice with targeted disruption of p8 gene show increased sensitivity to lipopolysaccharide and DNA microarray analysis of livers reveals an aberrant gene expression response. BMC Gastroenterol 2003, 3:25.