Blood Coagulation Factor X (Fx) in Human Seminal Plasma

Matsuda, Yoshihisa; Shimokawa, Ken‐ichi; Katayama, Masatoki; Shimizu, Hiroshi; Umeda, Takashi; Oshio, Shigeru; Chiba, Ryoko

doi:10.1080/01485010290031600

Cited by 12 publications

(14 citation statements)

References 19 publications

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“…More recently, a number of well known components of the blood coagulation and fibrinolysis systems, including protein C inhibitor, tissue and urokinase type plasminogen activator, tissue factor, tissue factor pathway inhibitor, and blood coagulation factor X, have been identified in seminal plasma and have been associated with male fertility (42)(43)(44)(45)(46). Given the overlapping regulatory components of the seminal and blood homeostasis, this emerging evidence suggests that analogous to fibrinolysis, semen liquefaction is regulated through highly orchestrated proteolytic cascades (7,10,31,47,48).…”

Section: Discussionmentioning

confidence: 99%

Major Role of Human KLK14 in Seminal Clot Liquefaction

Emami

Deperthes

Malm

et al. 2008

Journal of Biological Chemistry

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Liquefaction of human semen involves proteolytic degradation of the seminal coagulum and release of motile spermatozoa. Several members of human kallikrein-related peptidases (KLKs) have been implicated in semen liquefaction, functioning through highly regulated proteolytic cascades. Among these, KLK3 (also known as prostate-specific antigen) is the main executor enzyme responsible for processing of the primary components of semen coagulum, semenogelins I and II. We have recently identified KLK14 as a potential activator of KLK3 and other KLKs. This study aims to elucidate the cascade-mediated role of KLK14 ex vivo. KLK14 expression was significantly lower (p ‫؍‬ 0.0252) in individuals with clinically delayed liquefaction. Concordantly, KLK14 expression was significantly (p ‫؍‬ 0.0478) lower in asthenospermic cases. Specific inhibition of KLK14 activity by the synthetic inhibitor ACT G9 resulted in a significant delay in semen liquefaction, a drop in the "early" (30 min postejaculation) "chymotrypsin-like" and KLK1 activity, and an increase in the "late" (90 min postejaculation) chymotrypsinlike activity. Conversely, the addition of recombinant active KLK14 facilitated the liquefaction process, augmented the early chymotrypsin-like activity, and lowered late chymotrypsin-like activity. Given that the observed chymotrypsin-like activity was almost completely attributed to KLK3 activity, KLK3 seems to be regulated bidirectionally. Accordingly, a higher level of KLK3 fragmentation was observed in KLK14-induced coagula, suggesting an inactivation mechanism via internal cleavage. Finally, semenogelins I and II were directly cleaved by KLK14. Semenogelins were also able to reverse KLK14 inhibition by Zn 2؉ , providing a novel regulatory mechanism for KLK14 activity. Our results show that KLK14 exerts a significant and dose-dependent effect in the process of semen liquefaction.

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Section: Discussionmentioning

confidence: 99%

Major Role of Human KLK14 in Seminal Clot Liquefaction

Emami

Deperthes

Malm

et al. 2008

Journal of Biological Chemistry

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“…The second pattern showed a significant difference between subjects in their 20s and 30s (P < 0.05), but no significant difference between subjects' samples in their 30s and 40s, as shown in Table 3 and Figure 1. The second group included LAP-like enzyme [11], plasminogen, plasmin [15,16] and FXa [12] tested in the present study, and for each of those, the sub-sexual gland responsible for its secretion has not been identified yet. These results indicate there is some functional decline of the human prostate gland in subjects in their 30s, and that this decline proceeds in subjects in their 40s.…”

Section: Resultsmentioning

confidence: 99%

“…These processes to play an important role in the capacitation of semen [8]. Some proteases in human seminal plasma, such as the active form of blood coagulation factor X (FXa, EC 3.4.21.6) [11], thrombin (EC 3.4.21.5) [14], plasminogen and plasmin (EC 3.4.21.7) [15,16], and tissue plasminogen activator (tPA, EC 3.4.21.68) [2,3], are involved in the mechanisms of the coagulation=liquefaction of human semen. Aging is also associated with decreased spermatogenesis and a decrease in the activity of some physiologically important enzymes in the seminal plasma.…”

Section: Introductionmentioning

confidence: 99%

Action of Physiologically Active Materials in Human Semen During Aging

Matsuda

Ki²,

Katayama³

et al. 2004

Archives of Andrology

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“…TF, has also been suggested to play a major role as a morphogenic factor during early embryonic development [114,115]. Some researchers speculated about the assignment of seminal TF for other functions rather than blood coagulation due to its very high expression in semen in comparison to other coagulation proteins [110,[116][117][118]. Prostasomal TF may protect against anti-sperm antibody development and against transmission of infectious agents [108].…”

Section: Prostasomal Tissue Factor (Tf) and Seminal Clottingmentioning

confidence: 99%

Prostasome Involvement in the Development and Growth of Prostate Cancer~!2009-07-10~!2009-12-09~!2010-02-11~!

Babiker¹,

Ronquist²,

Nilsson³

et al. 2010

TOPCANJ

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Prostasomes are extracellularly occurring submicron, membrane-surrounded organelles produced by the epithelial cells of the prostate and present in semen after secretion. Even dedifferentiated prostate cancer cells have preserved their ability to produce and export prostasomes to the extracellular space. The precise physiological role of prostasomes is not known, although some of their properties assign them to important physiological and patho-physiological functions that could be exploited in prostate cancer growth and development. In this review, some new properties of seminal and malignant cell line (DU145, PC-3 and LNCaP) prostasomes will be discussed.There are typical differences in the expressions and activities of prostasomal CD59, ATPase, protein kinases and tissue factor (TF) as well as in the transfer of prostasomal CD59 to CD59-deficient erythrocytes (rabbit and human PNH erythrocytes). CD59, protein kinases and TF exhibit characteristic patterns of overexpression by malignant cell prostasomes. A high ATPase activity is recognized on seminal prostasomes with minimal activity on malignant cell prostasomes resulting in more residual ATP available for phosphorylation reactions. Several proteins are phosphorylated by prostasomal protein kinases, namely, complement component C3, fibrinogen, vitronectin and E-cadherin. Furthermore, TF is identified as the main endogenous phosphorylation substrate on prostasomes. In addition, prothrombotic effects of prostasomes are demonstrated. DU145 and PC-3 cell-derived prostasomes exert a higher clotting effect on whole blood and plasma compared to LNCaP cell-derived and seminal prostasomes.In conclusion, malignant cell prostasomes show an increased ability to interact with the biological system in favor of prostate cancer cell promotion and survival. The roles played by prostasomes in this context may improve the understanding of the mechanisms that help the prostate cancer cells to avoid the complement attack (CD59 transfer and phosphorylation and inactivation of C3), to promote angiogenesis (TF) and to metastasize. It may also provide a better understanding of some of the complications usually seen in some terminal prostate cancer patients like thrombotic events and tendency to develop disseminated intravascular coagulation.Keywords: ATPase, CD59, CK, complement, DU145, Extracellular phosphorylation, LNCaP, PC-3, PKA, PKC, prostasomes, prostate cancer, protein kinases, tissue factor. I. GENERAL BACKGROUND A. Prostate CancerProstate cancer is the most prevalent noncutaneous cancer in many of the Western countries and is the second leading cause of cancer death in men in USA [1]. The introduction of prostate specific antigen (PSA) in the latter half of 1980s as a biochemical marker of prostate cancer in serum signified a radical change of the pattern of prostate cancer diagnosis. It meant that more cases were detected at an early stage and substantially fewer at advanced stages [2] [3]. There are also studies showing that increasing incidence of prostate can...

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Blood Coagulation Factor X (Fx) in Human Seminal Plasma

Cited by 12 publications

References 19 publications

Major Role of Human KLK14 in Seminal Clot Liquefaction

Major Role of Human KLK14 in Seminal Clot Liquefaction

Action of Physiologically Active Materials in Human Semen During Aging

Prostasome Involvement in the Development and Growth of Prostate Cancer~!2009-07-10~!2009-12-09~!2010-02-11~!

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