Inhibition of human sperm-zona-free hamster oocyte binding and penetration by protein C inhibitor

España, Francisco; Sánchez-Cuenca, J.M.; Fernández, Pascual; Gilabert, J.; Romeu, A.; Estellés, Amparo; Royo, Montserrat; Müller, Charles

doi:10.1046/j.1439-0272.1999.00282.x

Cited by 20 publications

(19 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…PAI-3 is a protease inhibitor that may be involved in human reproduction [31][32][33]. The precise role of this inhibitor in extracellular proteolysis has not been fully clarified, but it has been suggested that PAI-3 protects uPA from the inactivation by PAI-1 [34].…”

Section: Plasminogen Activator System In Endometriosismentioning

confidence: 99%

Expression of the Fibrinolytic Components in Endometriosis

Gilabert‐Estellés

Ramón²,

España³

et al. 2006

Pathophysiol Haemos Thromb

Self Cite

View full text Add to dashboard Cite

Section: Plasminogen Activator System In Endometriosismentioning

confidence: 99%

Expression of the Fibrinolytic Components in Endometriosis

Gilabert‐Estellés

Ramón²,

España³

et al. 2006

Pathophysiol Haemos Thromb

Self Cite

View full text Add to dashboard Cite

“…The concentration of PCI in follicular fluid is similar to that in plasma [1], [3]. In contrast, a 40-fold higher concentration (3–4 µM) is present in the seminal plasma [1].…”

Section: Introductionmentioning

confidence: 58%

“…Given that the physiological role of PSA is the degradation of the major proteins of seminal coagula, Semenogelin(Sg)-I and Sg-II, PCI also appears to be involved in the regulation of semen liquefaction [11]. In addition, seminal plasma PCI has been found to inhibit the binding and penetration of human sperm to zona-free hamster oocytes [3], [12]. The inhibitor thus appears to be necessary for several steps in fertilization.…”

Section: Introductionmentioning

confidence: 99%

N-glycans of Human Protein C Inhibitor: Tissue-Specific Expression and Function

et al. 2011

View full text Add to dashboard Cite

Protein C inhibitor (PCI) is a serpin type of serine protease inhibitor that is found in many tissues and fluids in human, including blood plasma, seminal plasma and urine. This inhibitor displays an unusually broad protease specificity compared with other serpins. Previous studies have shown that the N-glycan(s) and the NH2-terminus affect some blood-related functions of PCI. In this study, we have for the first time determined the N-glycan profile of seminal plasma PCI, by mass spectrometry. The N-glycan structures differed markedly compared with those of both blood-derived and urinary PCI, providing evidence that the N-glycans of PCI are expressed in a tissue-specific manner. The most abundant structure (m/z 2592.9) had a composition of Fuc3Hex5HexNAc4, consistent with a core fucosylated bi-antennary glycan with terminal Lewisx. A major serine protease in semen, prostate specific antigen (PSA), was used to evaluate the effects of N-glycans and the NH2-terminus on a PCI function related to the reproductive tract. Second-order rate constants for PSA inhibition by PCI were 4.3±0.2 and 4.1±0.5 M−1s−1 for the natural full-length PCI and a form lacking six amino acids at the NH2-terminus, respectively, whereas these constants were 4.8±0.1 and 29±7 M−1s−1 for the corresponding PNGase F-treated forms. The 7–8-fold higher rate constants obtained when both the N-glycans and the NH2-terminus had been removed suggest that these structures jointly affect the rate of PSA inhibition, presumably by together hindering conformational changes of PCI required to bind to the catalytic pocket of PSA.

show abstract

“…Human seminal plasma contains very high concentrations of PCI, and it was shown that semen‐derived PCI interferes with binding and penetration of human sperm to zona‐free hamster oocytes . Altogether, PCI might influence several steps of reproduction.…”

Section: Proteins Of Interest In Pci−/− Mouse Testesmentioning

confidence: 99%

Proteome analysis of testis from infertile protein C inhibitor‐deficient mice reveals novel changes in serpin processing and prostaglandin metabolism

et al. 2015

View full text Add to dashboard Cite

Serine protease inhibitors (serpin) have therapeutic potential in a variety of pathogenic processes, ranging from thrombosis and altered immune response to liver cirrhosis. To investigate the physiological effects of protein C inhibitor (PCI, serpinA5), its gene was inactivated in a mouse model, resulting in male infertility. In the present report, 2D differential gel electrophoresis was utilized to investigate the molecular mechanisms for PCI involvement in male reproduction. Comparing the testes proteomes of three PCI-knockout mice with three wild types demonstrated similar patterns with the exception of a massive upregulation of prostaglandin reductase 1 (tenfold; p < 0.002) and the complete shifts in the molecular weights of serpinA1C and serpinA3K. All these PCI-dependent proteome changes were immunologically verified. Unbiased proteome analysis indicated that inactivation of serpinA5 strongly influenced both the protein species pattern of other A-clade serpins as well as prostaglandin metabolism in the testes.

show abstract

Inhibition of human sperm-zona-free hamster oocyte binding and penetration by protein C inhibitor

Cited by 20 publications

References 28 publications

Expression of the Fibrinolytic Components in Endometriosis

Expression of the Fibrinolytic Components in Endometriosis

N-glycans of Human Protein C Inhibitor: Tissue-Specific Expression and Function

Proteome analysis of testis from infertile protein C inhibitor‐deficient mice reveals novel changes in serpin processing and prostaglandin metabolism

Contact Info

Product

Resources

About