Conformational and biochemical characterization of a biologically active rat recombinant Protease Nexin-1 expressed in E. coli

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 4, 2009, Pages 602-614

  Arcone, Rosaria ^a   Chinali, Alberto ^b   Pozzi, Nicola ^c   Parafati, Maddalena ^a   Maset, Fabio ^c   Pietropaolo, Concetta ^b   De Filippis, Vincenzo ^c  

^a UNIVERSITY MAGNA GRAECIA OF CATANZARO   (Italy)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^c UNIVERSITY OF PADOVA   (Italy)

Author keywords

Conformational characterization; Neuroblastoma NB2A cell line; Protease Nexin 1; Recombinant protein; Thrombin

Indexed keywords

HEPARIN; PROTEASE NEXIN I; THROMBIN; TRYPTOPHAN;

ANIMAL CELL; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; MASS SPECTROMETRY; MOUSE; NERVE FIBER GROWTH; NEUROBLASTOMA CELL; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; TWO DIMENSIONAL GEL ELECTROPHORESIS;

AMINO ACID SEQUENCE; ANIMALS; BLOTTING, WESTERN; CELL LINE, TUMOR; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CIRCULAR DICHROISM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; HELA CELLS; HEPARIN; HUMANS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NEURITES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RATS; RECOMBINANT PROTEINS; SERPINS; THROMBIN;

ESCHERICHIA COLI; RATTUS;

EID: 61849100991     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.12.006     Document Type: Article

References (61)

1. Eaton D.L., and Baker J.B. Phorbol ester and mitogens stimulate human fibroblast secretions of plasmin-activatable plasminogen activator and protease nexin, an antiactivator/antiplasmin. J. Cell Biol. 97 (1983) 323-328
2. Guttridge D.C., Lau A., Tran L., and Cunningham D.D. Thrombin causes a marked delay in skeletal myogenesis that correlates with the delayed expression of myogenin and p21CIP1/WAF1. J. Biol. Chem. 272 (1997) 24117-24120
3. Bouton M.C., Richard B., Rossignol P., Philippe M., Guillin M.C., Michel J.B., and Jandrot-Perrus M. The serpin protease-nexin 1 is present in rat aortic smooth muscle cells and is upregulated in L-NAME hypertensive rats. Arterioscler. Thromb. Vasc. Biol. 23 (2003) 142-147
4. Hoffmann M.C., Nitsch C., Scotti A.L., Reinhard E., and Monard D. The prolonged presence of glia-derived nexin, an endogenous protease inhibitor, in the hippocampus after ischemia-induced delayed neuronal death. Neuroscience 49 (1992) 397-408
5. Reinhard E., Suidan H.S., Pavlik A., and Monard D. Glia-derived nexin/protease nexin-1 is expressed by a subset of neurons in the rat brain. J. Neurosci. Res. 37 (1994) 256-270
6. Silverman G.A., Bird P.I., Carrell R.W., Church F.C., Coughlin P.B., Gettins P.G., Irving J.A., Lomas D.A., Luke C.J., Moyer R.W., Pemberton P.A., Remold-O'Donnell E., Salvesen G.S., Travis J., and Whisstock J.C. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. J. Biol. Chem. 276 (2001) 33293-33296
7. Baker J.B., Low D.A., Simmer R.L., and Cunningham D.D. Protease-nexin: a cellular component that links thrombin and plasminogen activator and mediates their binding to cells. Cell 21 (1980) 37-45
8. Crisp R.J., Knauer D.J., and Knauer M.F. Roles of the heparin and low density lipid receptor-related protein-binding sites of protease nexin 1 (PN1) in urokinase-PN1 complex catabolism. The PN1 heparin-binding site mediates complex retention and degradation but not cell surface binding or internalization. J. Biol. Chem. 275 (2000) 19628-19637
9. Le Bonniec B.F., Guinto E.R., and Stone S.R. Identification of thrombin residues that modulate its interactions with antithrombin III and alpha 1-antitrypsin. Biochemistry 34 (1995) 12241-12248
10. Lawrence D.A., Olson S.T., Muhammad S., Day D.E., Kvassman J.O., Ginsburg D., and Shore J.D. Partitioning of serpin-proteinase reactions between stable inhibition and substrate cleavage is regulated by the rate of serpin reactive center loop insertion into beta-sheet A. J. Biol. Chem. 275 (2000) 5839-5844
11. Mansuy I.M., van der Putten H., Schmid P., Meins M., Botteri F.M., and Monard D. Variable and multiple expression of Protease Nexin-1 during mouse organogenesis and nervous system development. Development 119 (1993) 1119-1134
12. Giau R., Carrette J., Bockaert J., and Homburger V. Constitutive secretion of protease nexin-1 by glial cells and its regulation by G-protein-coupled receptors. J. Neurosci. 25 (2005) 8995-9004
13. Beilin O., Karussis D.M., Korczyn A.D., Gurwitz D., Aronovich R., Hantai D., Grigoriadis N., Mizrachi-Kol R., and Chapman J. Increased thrombin inhibition in experimental autoimmune encephalomyelitis. J. Neurosci. Res. 79 (2005) 351-359
14. Cavanaugh K.P., Gurwitz D., Cunningham D.D., and Bradshaw R.A. Reciprocal modulation of astrocyte stellation by thrombin and protease nexin-1. J. Neurochem. 54 (1990) 1735-1743
15. Nitsch C., Scotti A.L., Monard D., Heim C., and Sontag K.H. The glia-derived protease nexin 1 persists for over 1 year in rat brain areas selectively lesioned by transient global ischaemia. Eur. J. Neurosci. 5 (1993) 292-297
16. Cunningham D.D., Pulliam L., and Vaughan P.J. Protease nexin-1 and thrombin: injury-related processes in the brain. Thromb. Haemost. 70 (1993) 168-171
17. Onuma Y., Asashima M., and Whitman M. A Serpin family gene, protease nexin-1 has an activity distinct from protease inhibition in early Xenopus embryos. Mech. Dev. 123 (2006) 463-471
18. Grimaldi M., Arcone R., Ciliberto G., and Schettini G. Synergistic stimulation of interleukin 6 release and gene expression by phorbol esters and interleukin 1 beta in rat cortical astrocytes: role of protein kinase C activation and blockade. J. Neurochem. 64 (1995) 1945-1953
19. Sommer J., Gloor S.M., Rovelli G.F., Hofsteenge J., Nick H., Meier R., and Monard D. cDNA sequence coding for a rat glia-derived nexin and its homology to members of the serpin superfamily. Biochemistry 26 (1987) 6407-6410
20. Sanger F., Nicklen S., and Coulson A.R. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. U. S. A. 74 (1977) 5463-5467
21. Blasi F., Ciarrocchi A., Luddi A., Strazza M., Riccio M., Santi S., Arcone R., Pietropaolo C., D'Angelo R., Costantino-Ceccarini E., and Melli M. Stage-specific gene expression in early differentiating oligodendrocytes. Glia 39 (2002) 114-123
22. Studier F.W., Rosenberg A.H., Dunn J.J., and Dubendorff J.W. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185 (1990) 60-89
23. Kozak M. At least six nucleotides preceding the AUG initiator codon enhance translation in mammalian cells. J. Mol. Biol. 196 (1987) 947-950
24. Arcone R., Pucci P., Zappacosta F., Fontaine V., Malorni A., Marino G., and Ciliberto G. Single-step purification and structural characterization of human interleukin-6 produced in Escherichia coli from a T7 RNA polymerase expression vector. Eur. J. Biochem. 198 (1991) 541-547
25. 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
26. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
27. Jungblut P.R., and Seifert R. Analysis by high-resolution two-dimensional electrophoresis of differentiation-dependent alterations in cytosolic protein pattern of HL-60 leukemic cells. J. Biochem. Biophys. Methods 21 (1990) 47-58
28. Heukeshoven J., and Dernick R. Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining. Electrophoresis 6 (1985) 103-112
29. Gill S.C., and von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182 (1989) 319-326
30. Fenton II J.W., Fasco M., and Stackrow A.B. Human thrombins: production, evaluation, and properties of α-thrombin. J. Biol. Chem. 252 (1977) 3587-3598
31. Dang Q.D., and Di Cera E. A simple activity assay for thrombin and hirudin. J. Protein. Chem. 13 (1994) 367-373
32. Olson S.T., Björk I., and Shore J.D. Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin. Methods Enzymol. 222 (1993) 525-559
33. Stout T.J., Graham H., Buckley D.I., and Matthews D.J. Structures of active and latent PAI-1: a possible stabilizing role for chloride ions. Biochemistry 39 (2000) 8460-8469
34. Kopp J., and Schwede T. The SWISS-MODEL repository of annotated three-dimensional protein structure homology models. Nucleic Acids Res. 32 (2004) D230-234
35. Gerstein M. A resolution-sensitive procedure for comparing protein surface and its application to the comparison of antigen-combining sites. Acta Cryst. A48 (1992) 271-276
36. Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: 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
37. Lottenberg R., and Jackson C.M. Solution composition dependent variation in extinction coefficients for p-nitroaniline. Biochim. Biophys. Acta 742 (1983) 558-564
38. Stone S.R., Nick H., Hofsteenge J., and Monard D. Glial-derived neurite-promoting factor is a slow-binding inhibitor of trypsin, thrombin, and urokinase. Arch. Biochem. Biophys. 252 (1987) 237-244
39. Wallace A., Rovelli G., Hofsteenge J., and Stone S.R. Effect of heparin on the glia-derived-nexin-thrombin interaction. Biochem. J. 257 (1989) 191-196
40. Rovelli G., Stone S.R., Guidolin A., Sommer J., and Monard D. Characterization of the heparin-binding site of glia-derived nexin/protease nexin-1. Biochemistry 31 (1992) 3542-3549
41. Wells C.M., and Di Cera E. Thrombin is a Na(+)-activated enzyme. Biochemistry 31 (1992) 11721-11730
42. Tarnowski B.I., Spinale F.G., and Nicholson J.H. DAPI as a useful stain for nuclear quantitation. Biotech. Histochem. 66 (1991) 297-302
43. Evans D.L., McGrogan M., Scott R.W., and Carrell R.W. Protease specificity and heparin binding and activation of recombinant protease nexin I. J. Biol. Chem. 266 (1991) 22307-22312
44. Stone S.R., Brown-Luedi M.L., Rovelli G., Guidolin A., McGlynn E., and Monard D. Localization of the heparin-binding site of glia-derived nexin/protease nexin-1 by site-directed mutagenesis. Biochemistry 33 (1994) 7731-7735
45. Brahms S., and Brahms J. Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism. J. Mol. Biol. 138 (1980) 149-178
46. Bruch M., Weiss V., and Engel J. Plasma serine proteinase inhibitors (serpins) exhibit major conformational changes and a large increase in conformational stability upon cleavage at their reactive sites. J. Biol. Chem. 263 (1988) 16626-16630
47. Dwivedi A.M., Woodeshick R.W., Walton H.L., and Reilly T.M. A spectroscopic study of the conformations of active and latent forms of recombinant plasminogen activator inhibitor-1. Biochem. Biophys. Res. Commun. 175 (1991) 437-443
48. Strickland E.H. Aromatic contributions to circular dichroism spectra of proteins. CRC Crit. Rev. Biochem. 2 (1974) 113-175
49. Lakowicz J.R. Fluorescence studies of structural fluctuations in macromolecules as observed by fluorescence spectroscopy in the time, lifetime, and frequency domains. Methods Enzymol. 131 (1986) 518-567
50. Zhou A., Carrell R.W., and Huntington J.A. The serpin inhibitory mechanism is critically dependent on the length of the reactive center loop. J. Biol. Chem. 276 (2001) 27541-27547
51. Huntington J.A., Read R.J., and Carrell R.W. Structure of a serpin-protease complex shows inhibition by deformation. Nature 407 (2000) 923-926
52. Stavridi E.S., O'Malley K., Lukacs C.M., Moore W.T., Lambris J.D., Christianson D.W., Rubin H., and Cooperman B.S. Structural change in alpha-chymotrypsin induced by complexation with alpha 1-antichymotrypsin as seen by enhanced sensitivity to proteolysis. Biochemistry 35 (1996) 10608-10615
53. Arcone R., Pagliuca M.G., Chinali A., Grimaldi M., Schettini G., Gast A., and Pietropaolo C. Thrombin mutants with altered enzymatic activity have an impaired mitogenic effect on mouse fibroblasts and are inefficient modulators of stellation of rat cortical astrocytes. Biochim. Biophys. Acta 1451 (1999) 173-186
54. Lawrence D.A., Ginsburg D., Day D.E., Berkenpas M.B., Verhamme I.M., Kvassman J.O., and Shore J.D. Serpin-protease complexes are trapped as stable acyl-enzyme intermediates. J. Biol. Chem. 270 (1995) 25309-25312
55. Olson S.T. Transient kinetics of heparin-catalyzed protease inactivation by antithrombin III. Linkage of protease-inhibitor-heparin interactions in the reaction with thrombin. J. Biol. Chem. 263 (1988) 1698-1708
56. Turgeon V.L., and Houenou L.J. The role of thrombin-like (serine) proteases in the development, plasticity and pathology of the nervous system. Brain Res. Brain Res. Rev. 25 (1997) 85-95
57. Cunningham D.D. Regulation of neuronal cells and astrocytes by protease nexin-1 and thrombin. Ann. N.Y. Acad. Sci. 674 (1992) 228-236
58. Klann E., and Shelton K.R. A lead-associated nuclear protein which increases in maturing brain and in differentiating neuroblastoma 2A cells exposed to cyclic AMP-elevating agents. Brain Res. Dev. Brain Res. 57 (1990) 71-75
59. Gossen M., and Bujard H. Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 5547-5551
60. Guenther J., Nick H., and Monard D. A glia-derived neurite-promoting factor with protease inhibitory activity. EMBO J. 4 (1985) 1963-1966
61. Chen L.M., Zhang X., and Chai K.X. Regulation of prostasin expression and function in the prostate. Prostate 59 (2004) 1-12