Coagulation and liquefaction of semen. Proteolytic enzymes and citrate in prostatic fluid

Department of Surgery of The University of Chicago, Chicago.
Journal of Experimental Medicine (Impact Factor: 12.52). 12/1942; 76(6):527-41.
Source: PubMed


Certain specimens of human semen shorten the coagulation time of whole blood because of the presence of active thromboplastic agents, while other samples prolong its coagulation time. Human prostatic fluid in large amounts always delays or abolishes blood coagulation. The delay or absence of clotting is counteracted by adding calcium ions and is due to the large concentration of citrate in prostatic fluid and in some semens. While most specimens of dog semen shorten the coagulation time of blood because of their thromboplastic activity, certain specimens render blood incoagulable or delay coagulation; in contrast to human semen, this adverse effect on coagulation is not overcome with calcium ions and is due to a different mechanism, the lysis of fibrinogen. The citrate content of dog prostatic fluid is small. Human semen which has become liquefied does not contain thrombin or prothrombin, but fibrinogen and thromboplastic substances are present. Beef fibrinogen added to semen is destroyed by incubation for 18 hours, but added prothrombin and thromboplastic substances are still present after this treatment. Dog semen, in some instances, contains small amounts of thrombin. The semens of man and dog contain a fibrinolysin for human blood which seems not to differ greatly from the fibrinolysin associated with hemolytic streptococci. The blood of the donor of prostatic fluid is susceptible to fibrinolysis by this fluid. However, the blood of persons with some diseases, is absolutely resistant to the action of seminal fibrinolysin. In how many diseases this happens has not yet been determined. The semens of man and dog both contain an agent capable of inactivating fibrinogen, but in different amounts. This activity may be called fibrinogenase. Human semen is rich in fibrinolysin, poor in fibrinogenase; dog semen is rich in fibrinogenase, poor in fibrinolysin. These species differences, together with the fact that it is easy by appropriate dilution to retain the stronger proteolytic agent and eliminate the weaker one, imply that fibrinolysin and fibrinogenase are different entities. Dog semen, and less constantly human semen, contain very small amounts of trypsin. All of these proteolytic agents derive from the prostate gland; their secretion in prostatic fluid constitutes a hitherto undescribed function for the prostate gland.

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    • "Prostatic fluid is rich in enzymes, sodium, potassium, and calcium (Zaneveld and Tauber, 1981). Prostatic profibrinolysin lyses the semen coagulum, leading to increased sperm motility (Huggins and Neal, 1942). This allows sperm progression within the female reproductive system and ultimately encourages fertilization and pregnancy. "
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    ABSTRACT: The prostate gland plays an important role in male reproduction. Inflammation of the prostate gland (prostatitis) is a common health problem affecting many young and middle aged men. Prostatitis is considered a correctable cause of male infertility, but the pathophysiology and appropriate treatment options of prostatitis in male infertility remain unclear. This literature review will focus on current data regarding prostatitis and its impact on male infertility.
    Full-text · Article · Aug 2013 · Journal of Reproductive Immunology
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    • "The procoagulant activity of human seminal plasma added to blood plasma was first recognized in 1942 (Huggins and Neal, 1942). Seminal plasma diluted up to 10 000-fold significantly decreased the recalcification clotting time of blood plasma (Huggins and Neal, 1942). However, the molecular basis for this observation remains uncertain. "
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    ABSTRACT: Coagulation factor (F) IX is a zymogen of the plasma serine proteases, one that plays an essential role in the regulation of normal blood coagulation. Congenital defects of FIX synthesis or function cause hemophilia B (originally called hemophilia C). Factor IX is activated by Tissue Factor (TF):FVII/FVIIa complex and FXIa. Subsequent to its activation, FIXa combines with FVIIIa on the platelet surface and activates FX to FXa. Human semen forms a semi-solid gelatinous coagulum, which then liquefies within 5-20 minutes in vitro. In spite of evidence demonstrating the importance of the seminal coagulation and liquefaction process in terms of global fertility and despite the fact that the seminal coagulum is composed of fibrin-like material, it has always been addressed from the perspective of High Molecular Weight Seminal Vesicle (HMW-SV) proteins (Semenogelin I and II) and their cleavage by prostate-specific antigen rather than the conventional hemostatic factors. In this study and as part of our continuing investigation of human seminal clotting factors, we report here on seminal FIX and FIXa in normal, subfertile, and vasectomized subjects. Factors IX and FIXa were studied in a total of 119 semen specimens obtained from subfertile (n=18), normally fertile (n=34), and fertile sperm donors (n=27) and vasectomy subjects (n=40). Seminal FIX and FIXa levels were also measured in a group defined by normality in several parameters derived from the World Health Organization fertility criteria and termed "pooled normal semen parameters." Both FIX and FIXa were quantifiable in human semen. There was a wide individual variation in FIX and FIXa levels within groups. Despite the group size, statistically significant associations with fertility-related parameters were infrequent. There is a positive correlation between FIX and its activation product, FIXa (n=36; r=0.51; P <.05). Factor IXa elevation in the high sperm-clump group was significant (P <.05), and days of abstention correlated with FIXa levels (n=63; r=0.3; P <.05). The key finding of the present study is that both FIX and FIXa are present in concentrations that are not dissimilar to plasma levels and that are apparently functional, as the activated form is also present. This fact, taken with other reports of coagulation factors in semen, raises the likelihood that a functional set of hemostatic coagulation proteins exists in semen, potentially to interact with the HMW-SV proteins and the prostate-specific antigen system.
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    • "It is also possible that plasmin plays a part in acrosome rupture, the process of 'sperm capacitation', and in penetration of the zona pellucida. Huggins and Neal (1942) have shown that the fibrinolytic activity of semen was in the seminal plasma rather than in the spermatozoa; this has been confirmed using centrifugation methods checked by microscopy (Kester, 1970). In the present experiment no activator was demonstrated in spermatozoa, although Tympanidis and Astrup (1968) "
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    ABSTRACT: The distribution of fibrinolytic activity in the tissues of the male genital tract was studied by a histological technique. Preparations made from testis, epididymis, vas deferens, seminal vesicle, prostate, bulbo-urethral gland, and urethra showed that most activity was related to the blood vessels. However, inconsistent fibrinolytic activity related to epithelium was found in all parts of the genital tract. This epithelial activity was least in the testis, greater in the seminal vesicle and prostate gland, and was greatest in the bulbo-urethral gland and terminal urethra. No fibrinolytic activity could be demonstrated in relation to spermatozoa.
    Preview · Article · Dec 1971 · Journal of Clinical Pathology
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