Isolation and characterization of α1-proteinase inhibitor from common carp (Cyprinus carpio) seminal plasma

Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

Volumn 148, Issue 3, 2007, Pages 264-276

  Wojtczak, M ^a   Calka J ^b   Glogowski, J ^a   Ciereszko, A ^a  

^a INSTITUTE OF ANIMAL REPRODUCTION AND FOOD RESEARCH   (Poland)

^b UNIVERSITY OF WARMIA AND MAZURY IN OLSZTYN   (Poland)

Author keywords

Carp; Fish; Semen; Serpin; 1 proteinase inhibitor

Indexed keywords

ALPHA 1 ANTITRYPSIN; AMINO ACID; CARBOHYDRATE; CHYMOTRYPSIN; ELASTASE; GLYCOPROTEIN; ISOENZYME; POLYCLONAL ANTIBODY; TRYPSIN; ANTIBODY;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CARBOHYDRATE ANALYSIS; CARP; CONNECTIVE TISSUE; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME ISOLATION; ENZYME LOCALIZATION; ENZYME PURIFICATION; ENZYME STABILITY; MALE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; RAINBOW TROUT; SEMINAL PLASMA; SEQUENCE HOMOLOGY; SPERM; SPERMATOGENESIS; SPERMATOZOON; TESTIS; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; CROSS REACTION; GLYCOSYLATION; IMMUNOHISTOCHEMISTRY; IMMUNOLOGY; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; MOLECULAR WEIGHT; POLYACRYLAMIDE GEL ELECTROPHORESIS;

BOVINAE; CYPRINIDAE; CYPRINUS CARPIO; ONCORHYNCHUS MYKISS; SALMONIDAE;

ALPHA 1-ANTITRYPSIN; AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES; CARPS; CROSS REACTIONS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLYCOSYLATION; IMMUNOHISTOCHEMISTRY; MALE; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; SEQUENCE HOMOLOGY, AMINO ACID; TESTIS;

EID: 35548988833     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2007.06.004     Document Type: Article

References (55)

1. Andersen Ø., Flengsrud R., Norberg K., and Salte R. Salmon antithrombin has only three carbohydrate side chains, and shows functional similarities to human β-antithrombin. Eur. J. Biochem. 267 (2000) 1651-1657
2. 1-proteinase inhibitor from carp (Cyprinus carpio) serum. Mar. Biotechnol. 1 (1999) 33-43
3. Barbour K.W., Wei S., Brannan C., Flotte T.R., Baumann H., Berger M., and Franklin G. The murine a1-proteinase inhibitor gene family: Polymorphism, chromosomal location, and structure. Genomics 80 (2002) 515-522
4. Beatty K., Bieth J., and Travis J. Kinetics of associattion of serine proteinases with native and oxidized α-1-proteinase Inhibitor and α-1-antichymotrypsin. J. Biol. Chem. 255 (1980) 3931-3934
5. Bieth J.G. Pathophysiological interpretation of kinetic constants of proteinase inhibitors. Bull. Eur. Physiopathol. Respir. 16 (1980) 183-193
6. Bradford 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
7. Breton B., Menezo Y., and Billard R. Mise en évidence de quelques enzymes dans le sperme de la carpe Cyprinus carpio L. et de la truite Salmo gairdneri Richardson et dans le liquide coelomatique de la truite. Serie D 278, Comptes Rendus de L'academie des Sciences, Paris (1974) 1285-1288
8. Carrell R.W., Jeppsson J.O., and Laurell C.B. Structure and variation of human alpha-1-antitrypsin. Nature 298 (1983) 329-334
9. Charron Y., Madani R., Nef S., Combepine C., Govin J., Khochbin S., and Vassalli J.D. Expression of Serpin b6 serpins in germ and somatic cells of mouse gonads. Mol. Reprod. Dev. 73 (2006) 9-19
10. Chase T., and Show E. Titration of trypsin, plasmin and thrombin with p-nitrophenyl-p'guanidinobenzoate HCl. In: Colowic S.P., and Kaplan N.O. (Eds). Methods of Enzymology vol. 19 (1970), Academic Press, New York & London 20-27
11. Ciereszko A., Kwasnik M., Dabrowski K., Piros B., and Głogowski J. Chromatographic separation of trypsin-inhibitory activity of rainbow trout blood and seminal plasma. Fish Shellfish Immunol. 10 (2000) 91-94
12. Ciereszko A., Piros B., Dabrowski K., Kucharczyk D., Łuczyński M.J., Dobosz S., and Glogowski J. Serine proteinase inhibitors of seminal plasma of teleost fish: distribution of activity, electrophoretic profiles and relation to proteinase inhibitors of blood. J. Fish Biol. 53 (1998) 1292-1305
13. Ciereszko A., Własow T., Dobosz S., Goryczko K., and Głogowski J. Blood cells in rainbow trout Oncorhynchus mykiss milt: relation to milt collection method and sampling period. Theriogenology 62 (2004) 1353-1364
14. Dabbagh K., Laurent G.J., Shock A., Leoni P., Papakrivopoulou J., and Chambers R.C. Alpha-1-antitrypsin stimulates fibroblast proliferation and procollagen production and activates classical MAP kinase signalling pathways. J. Cell. Physiol. 186 (2001) 73-81
15. Dacheux J.L., Belghazi M., Lanson Y., and Dacheux F. Human epididymal secretome and proteome. Mol. Cell. Endocrinol. 250 (2006) 36-42
16. Evans J.P. Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization. Bioessays 23 (2001) 628-639
17. Geiger R., and Fritz H.T. In: Bergmeyer H.U. (Ed). Methods of Enzymatic Analysis vol. 5. (1983), Verlag Chemie, Weinheim 121-124
18. Griswold M. Interactions between germ cells and Sertoli cells in the testis. Biol. Reprod. 52 (1995) 211-216
19. Huang C.J., Chen C., Chen H.J., Huang F.L., and Chang G.D. A protease inhibitor of the serpin family is a major protein in carp perimeningeal fluid: I. Protein purification and characterization. J. Neurochem. 64 (1995) 1715-1720
20. Huang C.J., Lee M.S., Huang F.L., and 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. 64 (1995) 1721-1727
21. Ikari Y., Mulvihill E., and Schwartz S.M. Alpha 1-proteinase inhibitor, alpha 1-antichymotrypsin, and alpha 2-macroglobulin are the antiapoptotic factors of vascular smooth muscle cells. J. Biol. Chem. 276 (2001) 11798-11803
22. Irving J.A., Pike R.N., Lesk A.M., and Whisstock J.C. Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function. Genome Res. 10 (2000) 1845-1864
23. Janciauskiene S. Conformational properties of serine proteinase inhibitors (serpins) confer multiple pathophysiological roles. Biochim. Biophys. Acta 153 (2001) 221-235
24. Jonáková V., Cechová D., Töpfer-Petersen E., Calvete J.J., and Veselský L. Variability of acrosin inhibitors in boar reproductive tract. Biomed. Biochem. Acta 50 (1991) 691-695
25. Koj A., Hatton M.W., Wong K.L., and Regoeczi E. Isolation and partial characterization of rabbit plasma alpha1-antitrypsin. Biochem. J. 169 (1978) 589-596
26. Kowalski R., Glogowski J., Kucharczyk D., Goryczko K., Dobosz S., and Ciereszko A. Proteolytic activity and electrophoretic profiles of proteases from seminal plasma of teleosts. J. Fish Biol. 63 (2003) 1008-1019
27. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
28. Lahnsteiner F., Patzner R.A., and Weismann T. The spermatic duct of salmonid fishes (Salmonidae, Teleostei). Morphology, histochemistry and composition of the secretion. J. Fish Biol. 42 (1993) 79-93
29. Lahnsteiner F., Berger B., Patzner R., and Weismann T. Fine structure and motility of spermatozoa and composition of the seminal plasma in the perch. J. Fish. Biol. 47 (1995) 492-508
30. Laurell M., Christensson A., Abrahamsson P.A., Stenflo J., and Lilja H. Protein C inhibitor in human body fluids. Seminal plasma is rich in inhibitor antigen deriving from throughout the male reproductive system. J. Clin. Invest. 89 (1992) 1094-1101
31. Lilja H., Oldbring J., Rannevik G., and Laurell C.B. Seminal vesiclesecreted proteins and their reactions during gelation and liquefaction of human semen. J. Clin. Invest. 80 (1987) 281-285
32. Mak M., Mak P., Olczak M., Szalewicz A., Glogowski J., Dubin A., Watorek W., and Ciereszko A. Isolation, characterization, and cDNA sequencing of alpha-1-antiproteinase-like protein from rainbow trout seminal plasma. Biochim. Biophys. Acta 1671 (2004) 93-105
33. Mattes E., Matthiessen H.P., Tureck P.L., and Schwarz H.P. Preparation and properties of an alpha-1-protease inhibitor concentrate with high specific activity. Vox Sang. 81 (2001) 29-36
34. McGilligan K., and Thomas D.W. Evaluation of assays for detecting alpha-1-protease inhibitor during purification from rat serum. Anal. Biochem. 193 (1991) 260-265
35. Mickowska, B. Characterization and comparison of inhibitory profile of rainbow trout (Oncorhynchus mykiss) and common carp (Cyprinus carpio) blood plasma. Doctoral thesis (2004).
36. Niemann M.A., Baggott J.E., and Miller E.J. Binding of SPAAT, the 44-residue C-terminal peptide of alpha 1-antitrypsin, to proteins of the extracellular matrix. J. Cell Biochem. 66 (1997) 346-357
37. Olson T.S., Swanson R., Patston P.A., and Bjork I. Ammarent formation of sodium dodecyl sulfate-stable complexes between serpins and 3,4-dichloroisocoumarin-inactivated proteases is due to regeneration of active proteinase from the inactivated enzyme. J. Biol. Chem. 272 (1997) 13338-13342
38. Ouchterlony O. Antigen-antibody reactions in gels. IV. Types of reactions in coordinated systems of diffusion. Acta Pathol. Mocrobiol. Scand., Suppl. 32 (1953) 230-240
39. Patson P.A. Serpins and other serine proteinase inhibitors. Immunol. Today 21 (2000) 354
40. Patterson S.D. Mammalian α1-antitrypsins: comparative biochemistry and genetics of the major plasma serpin. Comp. Biochem. Physiol. B 100 (1991) 439-454
41. Potempa J., Korzus E., and Travis J. The serpin superfamily of proteinase inhibitors: structure, function and regulation. J. Biol. Chem. 269 (1994) 15957-15960
42. Roberts R.M., Mathialagan N., Duffy J.Y., and Smith G.W. Regulation and regulatory role of proteinase inhibitors. Crit. Rev. Eukaryot. Gene Expr. 5 (1995) 385-436
43. Schagger H., and Von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166 (1987) 368-379
44. Silverman G., Bird P., Carrell R., Church F.C., Coughlin P.B., Gettins G.W., Irving J.A., Lomas D.A., Luke C.J., Moyer R.W., Pemberton P.A., Remold-O'Donnell E., Salvesen G., Travis J., and Whisstock J.C. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. J. Biol. Chem. 276 (2001) 33293-33296
45. Sunderman F.W., Varghese A.H., Kroftova O.S., Grbac-Ivankovic S., Kotyza J., Datta A.K., Davis M., Bal W., and Kasparzak K.S. Characterization of pNiXa, a serpin of Xenopus laevis oocytes and embryos, and its histidine-rich Ni(II)-binding domain. Mol. Reprod. Dev. 44 (1996) 507-524
46. Suzuki Y., Yoshida K., Ichimiya T., Yamamoto T., and Sinohara H. Trypsin inhibitors in guinea pig plasma: isolation and characterization of contrapsin and two isoforms of α-1 antiproteinase and acute phase response of four major trypsin inhibitors. J. Biochem. 107 (1990) 173-179
47. Travis J., and Salvesen G.S. Human plasma proteinase inhibitors. Ann. Rev. Biochem. 52 (1983) 655-709
48. Uriel J., and Berges J. Characterization of natural inhibitors of trypsin and chymotrypsin by electrophoresis in acrylamide-agarose gels. Nature 218 (1968) 578-580
49. van Gent D., Sharp P., Morgan K., and Kalsheker N. Serpins: structure, function and molecular evolution. Int. J. Biochem. Cell Biol. 35 (2003) 1536-1547
50. Vassalli J.D., Huarte J., Bosco D., Sappino A.P., Sappino N., Velardi A., Wohlwend A., Erno H., Monard D., and Belin D. Protease-nexin I as an androgen-dependent secretory product of the murine seminal vesicle. EMBO J. 12 (1993) 1871-1878
51. Vila N., Millan M., Ferrer X., Riutort N., and Escudero D. Related Levels of alpha1-antitrypsin in plasma and risk of spontaneous cervical artery dissections: a case-control study. Stroke 34 (2003) 168-169
52. Wilson M.J., Garcia B., Woodson M., and Sinha A.A. Gelanolytic and caseinolytic proteinase activities in the secretions of the ventral, lateral, and dorsal lobes of the rat prostrate. Biol. Reprod. 48 (1993) 1174-1184
53. Wojtczak M., Glogowski J., Koldras M., Kucharczyk D., and Ciereszko A. Characterization of protease inhibitors of seminal plasma of cyprinids. Aquat. Living Resour. 16 (2003) 461-465
54. Yoshida K., Suzuki Y., and Sinohara H. Cloning and comparative sequence analysis of Xenopus laevis alpha1-antiproteinase. J. Biochem. 3 (1999) 59-63
55. Zhang T., Zhou H.M., and Liu Y.X. Expression of plasminogen activator and inhibitor, urokinase receptor and inhibin subunits in rhesus monkey testes. Mol. Hum. Reprod. 3 (1997) 223-231