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Thromb Haemost 2004; 92(04): 752-766
DOI: 10.1160/TH04-03-0142
Review Article
Schattauer GmbH

Seminal clotting and fibrinolytic balance: a possible physiological role in the male reproductive system

Bashir A. Lwaleed
1   Department of Urology, Southampton University Hospitals, Tremona Road, Southampton, UK
,
Robert Greenfield
2   American Diagnostic Inc, Stamford, Connecticut, USA
,
Alistair Stewart
1   Department of Urology, Southampton University Hospitals, Tremona Road, Southampton, UK
,
Brian Birch
1   Department of Urology, Southampton University Hospitals, Tremona Road, Southampton, UK
,
Alan J. Cooper
1   Department of Urology, Southampton University Hospitals, Tremona Road, Southampton, UK
› Institutsangaben
Weitere Informationen

Publikationsverlauf

Received 05. März 2004

Accepted after revision 04. Juli 2004

Publikationsdatum:
06. Dezember 2017 (online)

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Summary

Semen contains enzymes and inhibitors of the haemostatic system as well as the high molecular weight seminal vesicle (HMW-SV) proteins. The former may have roles in seminal clotting and in liquefaction through “fibrinolytic” activity, which may ultimately affect fertility. Although a limited number of studies have addressed the subject, the role of clotting and fibrinolytic factors in semen remains poorly understood. The liquefaction time and the distribution of components vary across split ejaculates. This may have an important bearing on the way clotting/fibrinolytic factors in semen are assessed. Semen contains tissue factor (TF, Thromboplastin, CD142), which originates from the prostate and is associated with prostasomes. The function of TF (and prostasomes) in semen is still a matter for speculation. Recently the presence of minute amounts of factor VII in semen has been demonstrated but its importance is uncertain. Semen also contains a thrombin-like enzyme, prothrombin fragments 1 and 2 (F1+2), D-dimer (DD) and thrombin-antithrombin (TAT) complexes. The presence of several fibrinolytic factors has been demonstrated in semen but few questions about their potential impact on semen quality have been raised. Factors found include tissue plasminogen activator (t-PA), urinary plasminogen activator (u-PA) and plasmin. There are also traces of fibrinogen, plasminogen, plasminogen activator inhibitor-1 (PAI-1), factorVIII coagulant activity (VIII:c) and fibrin monomers. The co-ordinate expression of both TF and PAI-1 by decidual cells of the endometrium is believed to be important in maintaining haemostasis during endovascular trophoblast invasion. Kallikrein-like serine protease inhibitors including prostate specific antigen (PSA) are known to be present in semen at high concentrations. In semen PSA is also found in a complex form with protein C inhibitor (PCI) with mutually inhibitory consequences. A better understanding of the spectrum of coagulating and liquefaction agents in semen to include classical haemostatic processes and the pathogenesis resulting from any imbalances between or within either system may provide the basis for the development of more selective and efficient agents affecting global fertility. Here we review aspects of male reproductive physiology in the light of recent findings concerning conventional clotting/fibrinolytic systems in human semen with a view to stimulating further research.

Keywords

Human seminal plasma - haemostasis - fertilization - implantation - prostasomes - semen quality - review
 

  • References

  • 1 Huggins C, Neal W. Coagulation and liquefaction of semen. Proteolytic enzymes and citrate in prostatic fluid. J Exp Med 1942; 76: 527-41.
    CrossrefPubMedGoogle Scholar
  • 2 Tauber PF, Zaneveld LJD. Coagulation and liquefaction of human semen. In Hafez ESE. Human Semen and Fertility Regulation in Men. C V Mosby Co, Saint Louis; 1976: 153.
    Google Scholar
  • 3 Mandal A, Bhattacharyya AK. Grouping of human ejaculates according to the degree of coagulation and the relationship to the levels of choline and cholinesterase. Int J Androl 1986; 09: 407-15.
    CrossrefPubMedGoogle Scholar
  • 4 Masaki J. Biochemistry of semen. In: Spermatology. Mohri H, Morisawa M, Hoshi M. (Eds). Tokyo: University of Tokyo Press; 1992: 121-37.
    Google Scholar
  • 5 Lilja H. A kallikrein-like serine protease in prostatic fluid cleaves the predominant seminal vesicle protein. J Clin Invest 1985; 76: 1899-903.
    CrossrefPubMedGoogle Scholar
  • 6 Malm J, Hellman J, Hogg P. et al. Enzymatic action of prostate-specific antigen (PSA or hK3): substrate specificity and regulation by Zn (2+), a tight-binding inhibitor. Prostate 2000; 45: 132-9.
    CrossrefPubMedGoogle Scholar
  • 7 Tauber PF, Zaneveld LJD, Propping D. et al. A new technique to measure the liquefaction rate of human semen: the bag method. Fertil Steril 1980; 33: 567-70.
    CrossrefPubMedGoogle Scholar
  • 8 Wetterauer U. Recommended biochemical parameters for routine semen analysis. Urology Research 1986; 14: 241-6.
    PubMedGoogle Scholar
  • 9 van Wersch JWJ, de Vries-Hanje JC, Ubachs JMH. Coagulation and fibrinolysis markers in seminal plasma of patients under evaluation for involuntary childlessness. Eur J Clin Chem Clin Biochem 1992; 30: 467-71.
    PubMedGoogle Scholar
  • 10 Syner FN, Moghissi KS, Yanez J. Isolation of a factor from normal human semen that accelerates dissolution of abnormally liquefying semen. Fertil Steril 1975; 11: 1064-9.
    PubMedGoogle Scholar
  • 11 Lukac J, Koren E. Mechanism of liquefaction of the human ejaculate. II. Role of collagenase-like peptidase and seminal proteinase. J Reprod Fert 1979; 56: 501-6.
    CrossrefPubMedGoogle Scholar
  • 12 Lilja H, Laurell CB. Liquefaction of coagulated human semen. Scand J Clin Lab Invest 1984; 44: 447-52.
    CrossrefPubMedGoogle Scholar
  • 13 Lilja H, Laurell CB. The predominant protein in human seminal coagulate. Scand J Clin Lab Invest 1985; 45: 635-41.
    CrossrefPubMedGoogle Scholar
  • 14 Laurell CB, Weiber H, Ohlsson K. et al. A zinc-dependent peptidase in prostatic organelles present in seminal plasma. Clin Chim Acta 1982; 126: 161-70.
    CrossrefPubMedGoogle Scholar
  • 15 Mann T. The biochemistry of semen and of the mail reproductive tract. London: Methuen; 1984
    Google Scholar
  • 16 Edwards JJ, Tollaksen SI, Andersson NG. Proteins of human semen. 1. Two-dimensional mapping of human seminal fluid. Clin Chem 1981; 27: 1335-40.
    PubMedGoogle Scholar
  • 17 Lilja H, Laurell CB, Jeppsson JO. Characterization of the predominant basic protein in human seminal plasma, one cleavage product of the major seminal vesicle protein. Scand J Clin Lab Invest 1984; 44: 439-46.
    CrossrefPubMedGoogle Scholar
  • 18 Notides AC, Williams-Ashman HG. The basic proteins responsible for clotting of guinea pig semen. Proc Nat Acad Sci (wash) 1967; 58: 1991-5.
    CrossrefPubMedGoogle Scholar
  • 19 Polak B, Daunter B. Seminal plasma biochemistry. IV: enzymes involved in the liquefaction of human seminal plasma. Int J Androl 1989; 12: 187-94.
    CrossrefPubMedGoogle Scholar
  • 20 Mandal A, Batabyal SK, Bhattacharyya AK. Glycerylphosphorylcholine levels in the coagulational groups of human ejaculates. Indian J Med Res 1989; 90: 186-90.
    PubMedGoogle Scholar
  • 21 España F, Gilabert J, Estellés A. et al. Functionally active protein C inhibitor/plasminogen activator inhibitor-3 (PCI/PAI-3) is secreted in seminal vesicles, occurs at high concentrations in human seminal plasma and complexes with prostate-specific antigen. Thromb Res 1991; 64: 309-20.
    CrossrefPubMedGoogle Scholar
  • 22 Laurell M, Christensson A, Abrahamsson PA. et al. Protein C inhibitor is present at micromolar concentrations in seminal plasma (Abstract). Thromb Haemost 1991; 65: 854.
    PubMedGoogle Scholar
  • 23 Laurell M, Christensson A, Abrahamsson PA. et al. Protein C inhibitor in human body fluids. Seminal plasma is rich in inhibitor antigen deriving from cells throughout the male reproductive system. J Clin Invest 1992; 89: 1094-101.
    CrossrefPubMedGoogle Scholar
  • 24 van Dreden P, Gonzalez J, Poirot C. Human seminal fibrinolytic activity: specific determinations of tissue plasminogen activator and urokinase. Andrologia 1991; 23: 29-33.
    PubMedGoogle Scholar
  • 25 Bronson RA, Preissner KT. Measurement of vitronectin content of human spermatozoa and vitronectin concentration within seminal fluid. Fertil Steril 1997; 68: 709-13.
    CrossrefPubMedGoogle Scholar
  • 26 Preissner KT, Seiffert D. Role of vitronectin and its receptors in haemostasis and vascular remodeling. Thromb Res 1998; 89: 1-21.
    CrossrefPubMedGoogle Scholar
  • 27 Schvartz I, Seger D, Shaltiel S. Vitronectin. Int J Biochem Cell Biol 1999; 05: 539-44.
    PubMedGoogle Scholar
  • 28 Fernandez JA, Heeb MJ, Radtke K-P. et al. Potent blood coagulant activity of human semen due to prostasome-bound tissue factor. Biol Reprod 1997; 56: 757-63.
    CrossrefPubMedGoogle Scholar
  • 29 van Wersch JWJ, Ubachs JHM, Dalaere KPJ. Fibrinolysis and coagulation markers in seminal plasma before and after vasectomy. Fibrinolysis 1993; 07: 135-8.
    PubMedGoogle Scholar
  • 30 Park JY, Yoshimara Y, Nozawa S. et al. Fibrinogen-like substance and thrombin like enzyme in human seminal plasma: coagulation of human semen. Arch Androl 1997; 38: 29-36.
    PubMedGoogle Scholar
  • 31 Christ G, Binder BR. Components of the fibrinolytic system in spermatozoa and seminal plasma of fertile and infertile men (Abstract). Thromb Haemost 1989; 62: 396.
    PubMedGoogle Scholar
  • 32 Williams-Ashman HG, Notides AC, Pabalan SS. et al. Transamidase reactions involved in the enzymic coagulation of semen: isolation of -glutamyl-lysine dipeptide from clotted secretion protein of guinea pig seminal vesicle. Proc Natl Acad Sci USA 1972; 69: 2322-5.
    CrossrefPubMedGoogle Scholar
  • 33 Williams-Ashman HG, Wilson J, Beil RE. et al. Transglutaminase reactions associated with the rat semen clotting system: modulation by macromolecular polyanions. Biochem Biophys Res Commun 1977; 79: 1192-8.
    CrossrefPubMedGoogle Scholar
  • 34 Tauber PF, Zaneveld LJD, Propping D. et al. Components of human split ejaculates. II. Enzymes and proteinase inhibitors. J Reprod Fertil 1976; 46: 165-71.
    CrossrefPubMedGoogle Scholar
  • 35 Murakami J, Yoshiike M, Satoh M. et al. Characterization of recombinant precursor proteins of the human seminal plasma sperm motility inhibitor synthesized in insect cells. Int J Mol Med 1998; 06: 693-700.
    PubMedGoogle Scholar
  • 36 Peter A, Lilja H, Lundwall A. et al. Semenogelin I and semenogelin II, the major gel-forming proteins in human semen, are substrates for transglutaminase. Eur J Biochem 1998; 252: 216-21.
    CrossrefPubMedGoogle Scholar
  • 37 Lilja H. Cell biology of semenogelin. Andrologia 1990; 22: 132-41.
    PubMedGoogle Scholar
  • 38 Fareed J, Callas DD, Hoppensteadt D. et al. Tissue factor antigen levels in various biological fluids. Blood Coag Fibrinol 1995; 06: 32-6.
    PubMedGoogle Scholar
  • 39 Carson SD, de-Jonge CJ. Activation of coagulation factor X in human semen. J Androl 1998; 19: 289-94.
    PubMedGoogle Scholar
  • 40 Nemerson Y. The tissue factor pathway of blood coagulation. Semin Haematol 1992; 29: 170-6.
    PubMedGoogle Scholar
  • 41 Minhas BS, Robertson JL, Kumar R. et al. The presence of platelet-activating factor-like activity in human spermatozoa. Fertil Steril 1991; 55: 372-6.
    CrossrefPubMedGoogle Scholar
  • 42 Lwaleed BA, Bass PS, Francis JL. et al. Functional and structural properties of urinary tissue factor. Nephrol Dial Transplant 1999; 14: 588-96.
    CrossrefPubMedGoogle Scholar
  • 43 Funakoshi T, Heimark RL, Hendrickson LE. et al. Human placental anticoagulant protein: Isolation and characterization. Biochemistry 1987; 26: 5572-8.
    CrossrefPubMedGoogle Scholar
  • 44 Satta N, Toti F, Feugeas O. et al. Monocytes Vesiculation. A mechanism for dissemination of membrane-associated procoagulant activity and adhesion molecules after stimulation by LPS. J Immunol 1994; 153: 3245-55.
    PubMedGoogle Scholar
  • 45 Ronquist G, Brody I. The prostasome: Its secretion and function in man. Biochim Biophys Acta 1985; 822: 203-18.
    CrossrefPubMedGoogle Scholar
  • 46 Brody I, Ronquist G, Gottfries A. Ultrastructural localisation of the prostasome-an organelle in human seminal plasma. Upsala J Med Sci 1983; 88: 63-80.
    CrossrefPubMedGoogle Scholar
  • 47 Callander NS, Varki N, Mohan LVRao. Immunohistochemical identification of tissue factor in solid tumours. Cancer 1992; 70: 1194-201.
    CrossrefPubMedGoogle Scholar
  • 48 Skibinski G, Kelley RW, Harkiss D. et al. Immunosupression by human seminal plasma-extracellular organelles (prostasomes) modulate activity of phagocytic cells. Am J Rerod Immunol 1992; 28: 97-103.
    PubMedGoogle Scholar
  • 49 Fabiani R, Johansson L, Lundkvist Ö. et al. Enhanced recruitment of motile spermatozoa by prostasome inclusion in swim-up medium. Hum Reprod 1994; 09: 1485-9.
    CrossrefPubMedGoogle Scholar
  • 50 Ronquist G, Nilsson BO, Hjertën S. Interaction between prostasomes and spermatozoa from human semen. Arch Androl 1990; 24: 147-57.
    PubMedGoogle Scholar
  • 51 Kelly RW, Holland P, Skibinski G. et al. Extracellular organelles (prostasomes) are immunosuppressive components of human semen. Clin Exp Immunol 1991; 86: 550-6.
    CrossrefPubMedGoogle Scholar
  • 52 Arienti G, Carlini E, Palmerini CA. Fusion of human sperm to prostasomes at acidic pH. J Membrane Biol 1997; 155: 89-94.
    CrossrefPubMedGoogle Scholar
  • 53 Kelly RW. Immunomodulators in human seminal plasma: a vital protection for spermatozoa in the presence of infection?. Int J Androl 1999; 22: 2-12.
    CrossrefPubMedGoogle Scholar
  • 54 Allegrucci C, Ronquist G, Nilsson BO. et al. Circulating human antisperm antibodies recognize prostasomes. Am J Reprod Immunol 2001; 46: 211-9.
    CrossrefPubMedGoogle Scholar
  • 55 Ronquist G, Nilsson BO. Prostasomes. Wennergren International Serious. London: Portland Press; 2002: 1-157.
    Google Scholar
  • 56 Kobayashi T, Matsuda Y, Park JY. et al. Trypsin-like arginine amidases including plasminogen and plasmin in human seminal plasma by affinity adsorption and elution. Arch Androl 1992; 28: 165-70.
    PubMedGoogle Scholar
  • 57 Abderson RA, Berler SA, Mark SR. et al. Characterization of a high molecular weight form of human acrosin. Biochem J 1981; 199: 307-16.
    CrossrefPubMedGoogle Scholar
  • 58 Elce JS, McIntyre J. Purification of bovine and human acrosin. Can J Biochem 1982; 60: 8-14.
    PubMedGoogle Scholar
  • 59 Matsuda Y, Oshio S, Yazaki T. et al. The effect of some proteinase inhibitors on liquefaction of human semen. Hum Reprod 1994; 09: 664-8.
    CrossrefPubMedGoogle Scholar
  • 60 McGee RS, Herr JC. Human seminal vesicles specific antigen is a substrate for prostate specific antigen (or P-30). Biol Reprod 1988; 39: 499-510.
    CrossrefPubMedGoogle Scholar
  • 61 Watt KWK, Lee PJ, Timkulu TM. et al. Human prostate specific antigen: structural and functional similarity with serine proteinases. Proc Nalt Acad Sci USA 1986; 83: 3166-70.
    CrossrefPubMedGoogle Scholar
  • 62 Nilsson BO, Jin M, Einarsson B. et al. Monoclonal antibodies against human prostasomes. Prostate 1998; 35: 178-84.
    CrossrefPubMedGoogle Scholar
  • 63 Carlsson L, Lennartsson L, Nilsson BO. et al. Growth-inhibitory effect of prostasomes on prostatic cancer cell lines in culture. Eur Urol 2000; 38: 468-74.
    CrossrefPubMedGoogle Scholar
  • 64 Tauber PF, Zaneveld LJD, Propping D. et al. Components of human split ejaculates. I. Spermatozoa, fructose, immunoglobulins, albumin, lactoferrin, transferrin and other plasma proteins. J Reprod Fertil 1975; 43: 249-67.
    CrossrefPubMedGoogle Scholar
  • 65 Lazure C, Leduc R, Seidah NG. et al. The major androgen-dependent protease in dog prostate belongs to the kallikrein family: confirmation by partial amino acid sequencing. FEBS (Fed Eur Biochem Soc) Lett 1984; 175: 1-7.
    CrossrefPubMedGoogle Scholar
  • 66 Ban Y, Wang MC, Watt KWK. et al. The proteolytic activity of human prostate specific antigen. Biochem Biophys Res Commun 1984; 123: 482-8.
    CrossrefPubMedGoogle Scholar
  • 67 William-Ashman HG. Transglutaminases and the clotting of mammalian seminal fluids. In: Molecular and Cellular Biochemistry. Martinus Nijhoff publishers; Boston: 1984. 58 51-61.
    Google Scholar
  • 68 Uhrin P, Dewerchin M, Hilpert M. et al. Disruption of the protein C inhibitor gene results in impaired spermatogenesis and male fertility. J Clin Invest 2000; 106: 1531-9.
    CrossrefPubMedGoogle Scholar
  • 69 Nakamura S, Kamikubo Y, Okajima K. et al. Plasma tissue factor: Its sensitive assay and characterization (Abstract). Thromb Haemost 1993; 69: 744.
    PubMedGoogle Scholar
  • 70 Lwaleed BA, Chisholm M, Francis JL. Development and Validation of an assay for urinary tissue factor activity. J Clin Pathol 1999; 52: 219-24.
    CrossrefPubMedGoogle Scholar
  • 71 Rapaport SI. Introduction to hematology. 2nd ed. Philadelphia: JB Lippincott; 1987
    Google Scholar
  • 72 MacGregor IR, Hargreave TB, Elton RA. Seminal plasma plasminogen activator and fertility. Andrologia 1987; 19: 452-5.
    PubMedGoogle Scholar
  • 73 van Dreden P, Gonzales J, Richard P. Determination of tissue plasminogen activator (t-PA) antigen in seminal plasma by modified enzyme-linked immunosorbant assay (ELISA). Andrologia 1988; 20: 48-51.
    PubMedGoogle Scholar
  • 74 Kumar R, Harper MJK, Hanahan DJ. Occurrence of platelet activating factor in rabbit spermatozoa. Arch Biochem Biophys 1988; 260: 497-502.
    CrossrefPubMedGoogle Scholar
  • 75 Mandal A, Bhattacharyya AK. Differences in osmolality, pH, buffering capacity, superoxide dismutase and maintenance of sperm motility in human ejaculates according to the degree of coagulation. Int J Androl 1988; 11: 45-51.
    CrossrefPubMedGoogle Scholar
  • 76 Mandal A, Bhattacharyya AK. Studies on the coagulational characteristics of human ejaculates. Andrologia 1985; 17: 80-6.
    PubMedGoogle Scholar
  • 77 Mandal A, Bhattacharyya AK. Relationship between the coagulation-liquefaction property of human ejaculates and their volume, sperm count and motility. Clin Reprod Fertil 1987; 05: 367-71.
    PubMedGoogle Scholar
  • 78 Zhang Y, Deng Y, Luther T. et al. Tissue factor controls the balance of angiogenic and antiangeogenic properties of tumor cells in mice. J Clin Invest 1994; 94: 1320-7.
    CrossrefPubMedGoogle Scholar
  • 79 Folkman J. Tumour angiogenesis and tissue factor. Nature Med 1996; 02: 167-8.
    CrossrefPubMedGoogle Scholar
  • 80 Nakagawa K, Zhang Y, Tsuji H. et al. The angiogenic effect of tissue factor on tumours and wounds Semin. Thromb Hemost 1998; 24: 207-10.
    Artikel in Thieme ConnectPubMedGoogle Scholar
  • 81 Luther T, Flossel C, Mackman N. et al. Tissue factor expression during human and mouse development. Am J Pathol 1996; 149: 101-13.
    PubMedGoogle Scholar
  • 82 Carmeliet P, Mackman N, Moons L. et al. Role of tissue factor in embryonic blood vessel development. Nature 1996; 383: 73-5.
    CrossrefPubMedGoogle Scholar
  • 83 Bunge RG, Sherman JK. Liquefaction of human semen by alpha-amylase. Fertil Steril 1954; 05: 353-6.
    CrossrefPubMedGoogle Scholar
  • 84 Ying SH, Day E, Whitmore Jr WF. et al. Fibrinolytic activity in human prostatic fluid and semen. Fertil Steril 1956; 07: 80-7.
    CrossrefPubMedGoogle Scholar
  • 85 Syner FN, Moghissi KS. Purification and properties of a human seminal proteinase. Biochem J 1972; 126: 1135-40.
    CrossrefPubMedGoogle Scholar
  • 86 Hirschhäuser C, Eliasson R. Origin and possible function of muramidase (lysozyme) in human seminal plasma. Life Sci 1972; 11: 149-54.
    CrossrefPubMedGoogle Scholar
  • 87 Tauber PF, Propping D, Zaneveld LJD. et al. Biochemical studies on the lysis of human split ejaculates (Abstract). Biol Reprod 1973; 09: 62.
    PubMedGoogle Scholar
  • 88 Daunter B, Hill R, Hennessey J. et al. Seminal plasma biochemistry I. Preliminary report: A possible mechanism for the liquefaction of human seminal plasma and its relationship to spermatozoal motility. Andrologia 1981; 13: 131-41.
    PubMedGoogle Scholar
  • 89 Rasmussen J, Albrechtsen OK. Fibrinolytic activity in human seminal plasma. Fertil Steril 1960; 11: 264-77.
    CrossrefPubMedGoogle Scholar
  • 90 Kester RC. Plasminogen activator in human prostate. J Clin Path 1969; 22: 442-6.
    CrossrefPubMedGoogle Scholar
  • 91 Maier U, Kirchheimer JC, Hienert G. et al. Fibrinolytic parameters in spermatozoas and seminal plasma. J Urol 1991; 146: 906-8.
    CrossrefPubMedGoogle Scholar
  • 92 Smokovitis A, Kokolis N, Taitzoglou I. et al. Plasminogen activator: The identification of an additional proteinase at the outer acrosomal membrane of human and boar spermatozoa. Int J Fertil 1992; 37: 308-14.
    PubMedGoogle Scholar
  • 93 Taitzoglou I, Kokolis N, Smokovitis A. Release of plasminogen activator and plasminogen activator inhibitor from spermatozoa of man, bull, ram and boar during acrosome reaction. Mol Androl 1996; 08: 187-97.
    PubMedGoogle Scholar
  • 94 Hong CY, Chiang BN, Huang JJ. et al. Two plasminogen activators, streptokinase and urokinase, stimulate human sperm motility. Andrologia 1985; 17: 317-20.
    PubMedGoogle Scholar
  • 95 Mac Gregor IR, Hargreave TB, Elton RA. Seminal plasma plasminogen activator and fertility. Andrologia 1987; 19: 452-5.
    PubMedGoogle Scholar
  • 96 Kirchheimer JC, Hienert G, Christ G. et al. Components of the fibrinolytic system in spermatozoa and seminal plasma of fertile and infertile men (Abstract). Thromb Haemost 1989; 62: 396.
    PubMedGoogle Scholar
  • 97 Campbell WB. Vasectomy and arterial disease. J R Soc Med 1988; 81: 683-5.
    CrossrefPubMedGoogle Scholar
  • 98 Samuel T, Kolk AH, Rumke P. et al. Autoimmunity to sperm antigens in vasectomized men. Clin Exp Immunol 1975; 21: 65-74.
    PubMedGoogle Scholar
  • 99 Whithy RM, Gordon RD, Blair BR. The endocrine effects of vasectomy: a prospective five-years study. Fertil Steril 1979; 31: 518-20.
    CrossrefPubMedGoogle Scholar
  • 100 Liu K, Liu YX, Du Q. et al. Preliminary studies on the role of plasminogen activator in seminal plasma of human and rhesus monkey. Mol Hum Reprod 1996; 02: 99-104.
    CrossrefPubMedGoogle Scholar
  • 101 Zheng X, Geiger M, Ecke S. et al. Inhibition of acrosin by protein C inhibitor and localization of protein C inhibitor to spermatozoa. Am J Physiol 1994; 267: 466-72.
    CrossrefPubMedGoogle Scholar
  • 102 Ben Rhouma K, Marrakchi H, Khouja H. et al. Outcome of intracytoplasmic injection of fresh and frozen-thawed testicular spermatozoa. A comparative study. J Reprod Med 2003; 48: 349-54.
    PubMedGoogle Scholar
  • 103 Lwaleed BA, Cooper AJ. Tissue factor expression and multidrug resistance in cancer: two aspects of a common cellular response to a hostile milieu. Med Hypotheses 2000; 55: 470-3.
    CrossrefPubMedGoogle Scholar
  • 104 Glander HJ, Schaller J. Binding of annexin V to plasma membranes of human spermatozoa: a rapid assay for detection of membrane changes after cryostorage. Mol Hum Reprod 1999; 05: 109-15.
    CrossrefPubMedGoogle Scholar
  • 105 Glantz SA. Primer of biostatistics. 2 Edition. New York: McGraw-Hill; 1987: 138-63.
    Google Scholar
  • 106 de Jonge CJ, Mack SR, Zaneveld LJD. Inhibition of the human sperm acrosome reaction by proteinase inhibitors. Gamete Res 1989; 23: 287-97.
    PubMedGoogle Scholar
  • 107 Rao LV, Pendurthi UR. Factor VIIa-induced gene expression: potential implications in pathophysiology. Trends Cardiovasc Med 2001; 11: 14-21.
    CrossrefPubMedGoogle Scholar
  • 108 Cargill DI, Cohen DS, Vawvalen RG. et al. Aggregation, release and desensitization induced in platelets from five species by platelet activating factor (PAF). Thromb Haemost 1983; 49: 204-7.
    Artikel in Thieme ConnectPubMedGoogle Scholar
  • 109 Hwang SB, Li CL, Lam MH. et al. Characterization of cutaneous vascular permeability induced by platelet activating factor receptor antagonist. Lab Invest 1985; 52: 617-30.
    PubMedGoogle Scholar
  • 110 O’Neill C. Embryo-derived platelet activating: a preimplantation embryo mediator of maternal recognition of pregnancy. Domest Anim Endocrinol 1987; 04: 69-85.
    CrossrefPubMedGoogle Scholar
  • 111 Johnston JM, Bleasdale JE, Hoffman DR. Functions of PAF in reproduction and development: involvement of PAF in fetal lung maturation and parturition. In platelet Activating Factor. Edited by Snyder F. New York: Plenum Press; 1987: 375.
    Google Scholar
  • 112 Minhas BS, Kumar R, Ricker DD. et al. Effects of platelet activating factor on mouse oocyte fertilization in vitro. Am J Obstet Gynecol 1989; 161: 1714-7.
    CrossrefPubMedGoogle Scholar
  • 113 Roudebush WE, Minhas BS, Ricker DD. et al. Platelet activating factor treatment of rabbit spermatozoa induces hyperactivated motility and fertilizability in vitro (Abstract). Bio Reprod 1989; 40: 343.
    CrossrefPubMedGoogle Scholar
  • 114 Angle MJ, Tom RA, McClure RD. The effect of platelet activating factor on sperm-egg interactions. The American Fertility Society 1989; S46.
    PubMedGoogle Scholar
  • 115 Minhas BS, Palmmer TV, Roudebush WE. et al. Platelet activating factor treatment of human spermatozoa enhances fertilization potential. The Society for Gynecologic Investigation 1990; 215.
    PubMedGoogle Scholar
  • 116 Moghissi KS, Syner FN. The effect of seminal protease on sperm migration through cervical mucus. Int J Fertil 1970; 15: 43-9.
    PubMedGoogle Scholar
  • 117 Liedholm P. On fibrinolysis in reproduction. Acta Obstet Gynecol Scand Suppl 1975; 41: 1-47.
    PubMedGoogle Scholar
  • 118 Liedholm P, Astedt B, Kullander S. Passage of tranexamic acid (AMCA) to semen in man and its effect on the fibrinolytic activity and on migration of spermatozoa. Fertil Steril 1973; 24: 517-20.
    CrossrefPubMedGoogle Scholar
  • 119 Dunn CL, Kelly RW, Critchley HO. Decidualization of the human endometrial stromal cell: an enigmatic transformation. Reprod Biomed Online 2003; 07: 151-61.
    CrossrefPubMedGoogle Scholar
  • 120 Lockwood CJ, Krikun G, Papp C. et al. The role of progestationally regulated stromal cell tissue factor and type-1 plasminogen activator inhibitor (PAI-1) in endometrial hemostasis and menstruation. Ann N Y Acad Sci 1994; 734: 57-79.
    CrossrefPubMedGoogle Scholar
  • 121 Lockwood CJ, Schatz FA. biological model for the regulation of peri-implantational hemostasis and menstruation. J Soc Gynecol Investig 1996; 03: 159-65.
    CrossrefPubMedGoogle Scholar
  • 122 Lockwood CJ, Nemerson Y, Guller S. et al. Progestational regulation of human endometrial stromal cell tissue factor expression during decidualization. J Clin Endocrinol Metab 1993; 76: 231-6.
    PubMedGoogle Scholar
  • 123 Schatz F, Krikun G, Caze R. et al. Progestinregulated expression of tissue factor in decidual cells: implications in endometrial hemostasis, menstruation and angiogenesis. Steroids 2003; 68: 849-60.
    CrossrefPubMedGoogle Scholar
  • 124 Lockwood CJ, Krikun G, Schatz F. The decidua regulates hemostasis in human endometrium. Semin Reprod Endocrinol 1999; 17: 45-51.
    Artikel in Thieme ConnectPubMedGoogle Scholar
  • 125 Salonen EM, Vaheri A, Pollanen J. et al. Interaction of plasminogen activator inhibitor (PAI-1) with vitronectin. J Biol Chem 1989; 264: 6339-43.
    PubMedGoogle Scholar
  • 126 Pierleoni C, Samuelsen GB, Graem N. et al. Immunohistochemical identification of the receptor for urokinase plasminogen activator associated with fibrin deposition in normal and ectopic human placenta. Placenta 1998; 19: 501-8.
    CrossrefPubMedGoogle Scholar
  • 127 Feng Q, Liu K, Liu YX. et al. Plasminogen activators and inhibitors are transcribed during early macaque implantation. Placenta 2001; 22: 186-99.
    CrossrefPubMedGoogle Scholar
  • 128 Zini JM, Murray SC, Graham CH. et al. Characterization of urokinase receptor expression by human placental trophoblasts. Blood 1992; 79: 2917-29.
    PubMedGoogle Scholar
  • 129 Strickland S, Richards WG. Invasion of the trophoblasts. Cell 1992; 71: 355-7.
    CrossrefPubMedGoogle Scholar
  • 130 Feinberg RF, Kao LC, Haimowitz JE. et al. Plasminogen activator inhibitor types 1 and 2 in human trophoblasts. PAI-1 is an immunocytochemical marker of invading trophoblasts. Lab Invest 1989; 61: 20-6.
    PubMedGoogle Scholar
  • 131 Casslen B. Mechanisms and regulation of plasminogen activation in the endometrium. Reproduction Humaine et Hormones 1999; 12: 521-5.
    PubMedGoogle Scholar
  • 132 Floridon C, Nielsen O, Holund B. et al. Localization and significance of urokinase plasminogen activator and its receptor in placental tissue from intrauterine, ectopic and molar pregnancies. Placenta 1999; 20: 711-21.
    CrossrefPubMedGoogle Scholar
  • 133 Wang MC, Valenzuela LA, Murrphy GP. et al. Purification of a human prostate specific antigen. Invest Urol 1979; 17: 159-63.
    PubMedGoogle Scholar
  • 134 Hara M, Koyanagi Y, Inoue T. et al. Physicochemical characteristics of γ-seminoprotein, an antigenic components specific for human seminal plasma. Jap J Legal Med 1971; 25: 322-4.
    PubMedGoogle Scholar
  • 135 Wang MC, Kuriyama M, Papsidero LD. et al. Prostate antigen of human cancer patients. Methods Cancer Res 1982; 19: 179-97.
    PubMedGoogle Scholar
  • 136 Schieferstein G. Prostate-specific antigen (PSA) in human seminal plasma. Arch Androl 1999; 42: 193-7.
    PubMedGoogle Scholar
  • 137 Malm J, Lilja H. Biochemistry of prostate specific antigen, PSA. Scand J Clin Lab Invest Suppl 1995; 221: 15-22.
    PubMedGoogle Scholar
  • 138 Abrahamsson PA, Lilja H. Free and complexed forms of prostate-specific antigen in serum. Tumour Marker Update 1994; 06: 1-4.
    PubMedGoogle Scholar
  • 139 Seregni E, Botti C, Ballabio G. et al. Biochemical characteristics and recent biological knowledge on prostate-specific antigen. Tumori 1996; 82: 72-7.
    PubMedGoogle Scholar
  • 140 Christensson A, Lilja H. Complex formation between protein C inhibitor and prostatespecific antigen in vitro and in human semen. Eur J Biochem 1994; 220: 45-53.
    CrossrefPubMedGoogle Scholar
  • 141 Glander HJ, Kratzsch J, Weisbrich C. et al. Insulin-like growth factor-I and alpha 2-macroglobulin in seminal plasma correlate with semen quality. Hum Reprod 1996; 11: 2454-60.
    CrossrefPubMedGoogle Scholar
  • 142 Elzanaty S, Richthoff J, Malm J, Giwercman A. The impact of epididymal and accessory sex gland function on sperm motility. Hum Reprod 2002; 17: 2904-11.
    CrossrefPubMedGoogle Scholar
  • 143 Charlesworth MC, Young CY, Miller VM. et al. Kininogenase activity of prostate-derived human glandular kallikrein (hK2) purified from seminal fluid. J Androl 1999; 20: 220-9.
    PubMedGoogle Scholar
  • 144 Mikolajczyk SD, Millar LS, Kumar A. et al. Prostatic human kallikrein 2 inactivates and complexes with plasminogen activator inhibitor-1. Int J Cancer 1999; 81: 438-42.
    CrossrefPubMedGoogle Scholar
  • 145 Deperthes D, Frenette G, Brillard-Bourdet M. et al. Potential involvement of kallikrein hK2 in the hydrolysis of the human seminal vesicle proteins after ejaculation. J Androl 1996; 17: 659-65.
    PubMedGoogle Scholar
  • 146 Deperthes D, Chapdelaine P, Tremblay RR. et al. Isolation of prostatic kallikrein hK2, also known as hGK-1, in human seminal plasma. Biochim Biophys Acta 1995; 1245: 311-6.
    CrossrefPubMedGoogle Scholar
  • 147 Tremblay RR, Coulombe E, Cloutier S. et al. Assessment of the trypsin-like human prostatic kallikrein, also known as hK2, in the seminal plasma of infertile men: respective contributions of an ELISA procedure and of Western blotting. J Lab Clin Med 1998; 131: 330-5.
    CrossrefPubMedGoogle Scholar
  • 148 Mac Donald RJ, Margolius HS, Erd s EG. Molecular biology of tissue kallikrein. Biochem J 1988; 253: 313-21.
    CrossrefPubMedGoogle Scholar
  • 149 España F, Fink E, Sanchez-Cuenca J. et al. Complexes of tissue kallikrein with protein C inhibitor in human semen and urine. Eur J Biochem 1995; 234: 641-9.
    CrossrefPubMedGoogle Scholar
  • 150 Elisen MG, van Kooij RJ, Nolte MA. et al. Protein C inhibitor may modulate human sperm-oocyte interactions. Biol Reprod 1998; 58: 670-7.
    CrossrefPubMedGoogle Scholar
  • 151 Wagenaar GT, van-Vuuren AJ, Girma M. et al. Characterization of transgenic mice that secrete functional human protein C inhibitor into the circulation. Thromb Haemost 2000; 83: 93-101.
    Artikel in Thieme ConnectPubMedGoogle Scholar
  • 152 Cooper ST, Rezaie AR, Esmon CT. et al. Inhibition of a thrombin anion-binding exosite-2 mutant by the glycosaminoglycandependent serpins protein C inhibitor and heparin cofactor II. Thromb Res 2002; 107: 67-73.
    CrossrefPubMedGoogle Scholar
  • 153 Meijers JC, Marquart JA, Bertina RM. et al. Protein C inhibitor (plasminogen activator inhibitor-3) and the risk of venous thrombosis. Br J Haematol 2002; 118: 604-9.
    CrossrefPubMedGoogle Scholar
  • 154 Huntington JA, Kjellberg M, Stenflo J. Crystal structure of protein C inhibitor provides insights into hormone binding and heparin activation. Structure 2003; 11: 205-15.
    CrossrefPubMedGoogle Scholar
  • 155 España F, Estelles A, Fernandez PJ. et al. Evidence for the regulation of urokinase and tissue type plasminogen activators by the serpin, protein C inhibitor, in semen and blood plasma. Thromb Haemost 1993; 70: 989-94.
    Artikel in Thieme ConnectPubMedGoogle Scholar
  • 156 He S, Lin YL, Liu YX. Functionally inactive protein C inhibitor in seminal plasma may be associated with infertility. Mol Hum Reprod 1999; 05: 513-9.
    CrossrefPubMedGoogle Scholar
  • 157 Kise H, Nishioka J, Satoh K. et al. Measurement of protein C inhibitor in seminal plasma is useful for detecting agenesis of seminal vesicles or the vas deferens. J Androl 2000; 21: 207-12.
    PubMedGoogle Scholar
  • 158 España F, Sanchez-Cuenca J, Fernandez PJ. et al. Inhibition of human sperm-zona-free hamster oocyte binding and penetration by protein C inhibitor. Andrologia 1999; 31: 217-23.
    CrossrefPubMedGoogle Scholar
  • 159 Lee SL, Wei YH. The involvement of extracellular proteinases and proteinase inhibitors in mammalian fertilization. Biotechnol Appl Biochem 1994; 19: 31-40.
    PubMedGoogle Scholar
  • 160 Honda A, Siruntawineti J, Baba T. Role of acrosomal matrix proteases in sperm-zona pellucida interactions. Hum Reprod Update 2002; 08: 405-12.
    CrossrefPubMedGoogle Scholar
  • 161 Diaz-Perez E, Meizel S. Importance of mammalian sperm metalloendoprotease activity during the acrosome reaction to subsequent sperm-egg fusion: inhibitor studies with human sperm and zona-free hamster eggs. Mol Reprod Dev 1992; 31: 122-30.
    CrossrefPubMedGoogle Scholar
  • 162 Shimokawa K, Katayama M, Matsuda Y. et al. Matrix metalloproteinase (MMP)-2 and MMP-9 activities in human seminal plasma. Mol Hum Reprod 2002; 08: 32-6.
    CrossrefPubMedGoogle Scholar
  • 163 Baumgart E, Lenk SV, Loening SA. et al. Quantitative differences in matrix metalloproteinase (MMP)-2, but not in MMP-9, tissue inhibitor of metalloproteinase (TIMP)-1 or TIMP-2, in seminal plasma of normozoospermic and azoospermic patients. Hum Reprod 2002; 17: 2919-23.
    CrossrefPubMedGoogle Scholar
  • 164 Shimokawa K, Katayama M, Matsuda Y. et al. Complexes of gelatinases and tissue inhibitor of metalloproteinases in human seminal plasma. J Androl 2003; 24: 73-7.
    PubMedGoogle Scholar
  • 165 Moriyama A, Shimoya K, Kawamoto A. et al. Secretory leukocyte protease inhibitor (SLP) concentrations in seminal plasma: SLPI restores sperm motility reduced by elastase. Mol Hum Reprod 1998; 04: 946-50.
    CrossrefPubMedGoogle Scholar
  • 166 Llanos M, Vigil P, Salgado AM. et al. Inhibition of the acrosome reaction by trypsin inhibitors and prevention of penetration of spermatozoa through the human zona pellucida. J Reprod Fertil 1993; 97: 173-8.
    CrossrefPubMedGoogle Scholar
  • 167 Esmon CT, Fukudome K, Mather T. et al. Inflammation, sepsis, and coagulation. Haematologica 1999; 84: 254-9.
    PubMedGoogle Scholar
  • 168 Tapper H, Herwald H. Modulation of hemostatic mechanisms in bacterial infectious diseases. Blood 2000; 96: 2329-37.
    PubMedGoogle Scholar
  • 169 Lauw FN, Dekkers PE, te Velde AA. et al. Interleukin-12 induces sustained activation of multiple host inflammatory mediator systems in chimpanzees. J Infect Dis 1999; 179: 646-52.
    CrossrefPubMedGoogle Scholar
  • 170 Cui MZ, Parry GC, Oeth P. et al. Transcriptional regulation of the tissue factor gene in human epithelial cells is mediated by Sp1 and EGR-1. J Biol Chem 1996; 271: 2731-9.
    CrossrefPubMedGoogle Scholar
  • 171 Donovan-Peluso M, George LD, Hassett AC. Lipopolysaccharide induction of tissue factor expression in THP-1 monocytic cells. Protein-DNA interactions with the promoter. J Biol Chem 1994; 269: 1361-9.
    PubMedGoogle Scholar
  • 172 Felts SJ, Stoflet ES, Eggers CT. et al. Tissue factor gene transcription in serum-stimulated fibroblasts is mediated by recruitment of c-Fos into specific AP-1 DNA-binding complexes. Biochemistry 1995; 34: 12355-62.
    CrossrefPubMedGoogle Scholar
  • 173 Bartha K, Brisson C, Archipoff G. et al. Thrombin regulates tissue factor and thrombomodulin mRNA levels and activities in human saphenous vein endothelial cells by distinct mechanisms. J Biol Chem 1993; 268: 421-9.
    PubMedGoogle Scholar
  • 174 Oeth PA, Parry GC, Kunsch C. et al. Lipopolysaccharide induction of tissue factor gene expression in monocytic cells is mediated by binding of c-Rel/p65 heterodimers to a kappa B-like site. Mol Cell Biol 1994; 14: 3772-81.
    CrossrefPubMedGoogle Scholar
  • 175 Ledee-Bataille N. Secreted cytokines in the uterine lumina are predictive of subsequent implantation. Presence of IL18 in the uterine flushing. J Gynecol Obstet Biol Reprod (Paris) 2004; 33: 29-32.
    PubMedGoogle Scholar
  • 176 Yenugu S, Hamil KG, Birse CE. et al. Antibacterial properties of the sperm-binding proteins and peptides of human epididymis 2 (HE2) family; salt sensitivity, structural dependence and their interaction with outer and cytoplasmic membranes of Escherichia coli. Biochem J 2003; 372: 473-83.
    CrossrefPubMedGoogle Scholar
  • 177 von Horsten HH, Derr P, Kirchhoff C. Novel antimicrobial peptide of human epididymal duct origin. Biol Reprod 2002; 67: 804-13.
    CrossrefPubMedGoogle Scholar
  • 178 Sitaram N, Subbalakshmi C, Krishnakumari V. et al. Identification of the region that plays an important role in determining antibacterial activity of bovine seminalplasmin. FEBS Lett 1997; 400: 289-92.
    CrossrefPubMedGoogle Scholar
  • 179 Carlsson L, Pahlson C, Bergquist M. et al. Antibacterial activity of human prostasomes. Prostate 2000; 44: 279-86.
    CrossrefPubMedGoogle Scholar
  • 180 Kelly RW, Critchley HO. Immunomodulation by human seminal plasma: a benefit for spermatozoon and pathogen?. Hum Reprod 1997; 12: 2200-7.
    CrossrefPubMedGoogle Scholar
  • 181 Kelly RW, Carr GG, Critchley HO. A cytokine switch induced by human seminal plasma: an immune modulation with implications for sexually transmitted disease. Hum Reprod 1997; 12: 677-81.
    CrossrefPubMedGoogle Scholar