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

Andrologia ◽  
1999 ◽  
Vol 31 (4) ◽  
pp. 217-223 ◽  
Author(s):  
F. Espana ◽  
J. Sanchez-Cuenca ◽  
P. J. Fernandez ◽  
J. Gilabert ◽  
A. Romeu ◽  
...  
Keyword(s):  
Protein C ◽  
Human Sperm ◽  
Protein C Inhibitor ◽  
Hamster Oocyte

scholarly journals Protein C Inhibitor May Modulate Human Sperm-Oocyte Interactions1

1998 ◽  
Vol 58 (3) ◽  
pp. 670-677 ◽  
Author(s):  
Marc G.L.M. Elisen ◽  
Roelof J. van Kooij ◽  
Martijn A. Nolte ◽  
J. Arnoud Marquart, ◽  
Tycho M.T.W.T. Lock ◽  
...  
Keyword(s):  
Protein C ◽  
Human Sperm ◽  
Protein C Inhibitor

Inhibition of acrosin by protein C inhibitor and localization of protein C inhibitor to spermatozoa

1994 ◽  
Vol 267 (2) ◽  
pp. C466-C472 ◽  
Author(s):  
X. Zheng ◽  
M. Geiger ◽  
S. Ecke ◽  
E. Bielek ◽  
P. Donner ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Protein C ◽  
Reproductive Tract ◽  
Human Sperm ◽  
Order Rate Constant ◽  
Enzyme Linked Immunosorbent Assay ◽  
Amidolytic Activity ◽  
Protein C Inhibitor ◽  
Seminal Plasma Proteins ◽  
High Concentrations

Protein C inhibitor (PCI) is synthesized by cells throughout the male reproductive tract and is present in high concentrations (220 micrograms/ml) in seminal plasma. Seminal plasma as well as the acrosome of spermatozoa are rich in possible target proteases for PCI. We analyzed the interaction of PCI with acrosin, a serine protease stored in its zymogen form in the acrosome of spermatozoa. Purified human PCI inhibited the amidolytic activity of purified boar acrosin with an apparent second-order rate constant of 3.7 x 10(4) M-1.s-1. Inhibition was paralleled by the degradation of PCI from its 57- to its 54-kDa form. Human PCI also inhibited the amidolytic activity of activated human sperm extracts and formed complexes with acrosin as determined by an enzyme-linked immunosorbent assay. Immunocytochemistry revealed that morphologically abnormal spermatozoa stained for PCI antigen, whereas morphologically normal spermatozoa were negative. In immunoelectron microscopy, PCI was exclusively localized in the immediate vicinity of disrupted acrosomal membranes of sperm heads. These data suggest that PCI might function as a scavenger of prematurely activated acrosin, thereby protecting intact surrounding cells and seminal plasma proteins from possible proteolytic damage.

Characterization of a cDNA for Rhesus Monkey Protein C Inhibitor – Evidence for N-Terminal Involvement in Heparin Stimulation

1995 ◽  
Vol 74 (04) ◽  
pp. 1079-1087 ◽  
Author(s):  
Klaus-P Radtke ◽  
José A Fernández ◽  
Bruno O Villoutreix ◽  
Judith S Greengard ◽  
John H Griffin
Keyword(s):  
Rhesus Monkey ◽  
Protein C ◽  
Activated Protein C ◽  
Pcr Amplification ◽  
Amino Acid Sequences ◽  
Heparin Binding ◽  
Reactive Center ◽  
Protein C Inhibitor ◽  
Polymerase Chain

SummarycDNAs for protein C inhibitor (PCI) were cloned from human and rhesus monkey 1 liver RNAs by reverse transcription and polymerase chain reaction (PCR) amplification. Sequencing showed that rhesus monkey and human PCI cDNAs were 93% identical. Predicted amino acid sequences differed at 26 of 387 residues. Pour of these differences (T352M, N359S, R362K, L3631) were in the reactive center loop that is important for inhibitory specificity, and two were in the N-terminal helix (M8T, E13K) that is implicated in glycosaminoglycan binding. PCI in human or rhesus monkey plasma showed comparable inhibitory activity towards human activated protein C in the presence of 10 U/ml heparin. However, maximal acceleration of the inhibition of activated protein C required 5-fold lower heparin concentration for rhesus monkey than for human plasma, consistent with the interpretation that the additional positive charge (E13K) in a putative-heparin binding region increased the affinity for heparin.

scholarly journals Heparin binding to protein C inhibitor.

1992 ◽  
Vol 267 (13) ◽  
pp. 8789-8794 ◽  
Author(s):  
C.W. Pratt ◽  
F.C. Church
Keyword(s):  
Protein C ◽  
Heparin Binding ◽  
Protein C Inhibitor

scholarly journals Plasma levels of activated protein C-protein C inhibitor complex in patients with hypercoagulable states

2000 ◽  
Vol 65 (1) ◽  
pp. 35-40 ◽  
Author(s):  
Rika Watanabe ◽  
Hideo Wada ◽  
Miho Sakakura ◽  
Yoshitaka Mori ◽  
Takahiro Nakasaki ◽  
...  
Keyword(s):  
Plasma Levels ◽  
Protein C ◽  
Activated Protein C ◽  
C Protein ◽  
Inhibitor Complex ◽  
Protein C Inhibitor

scholarly journals Activated protein C–protein C inhibitor complex as a prognostic marker in sepsis

Critical Care ◽  
2008 ◽  
Vol 12 (Suppl 5) ◽  
pp. P21
Author(s):  
Lars Heslet ◽  
Rikke Hald ◽  
Camilla Recke ◽  
Kristian Bangert ◽  
Lars Uttenthal
Keyword(s):  
Prognostic Marker ◽  
Protein C ◽  
Activated Protein C ◽  
C Protein ◽  
Inhibitor Complex ◽  
Protein C Inhibitor

scholarly journals Quantification of a Proteotypic Peptide from Protein C Inhibitor by Liquid Chromatography–Free SISCAPA-MALDI Mass Spectrometry: Application to Identification of Recurrence of Prostate Cancer

2013 ◽  
Vol 59 (10) ◽  
pp. 1514-1522 ◽  
Author(s):  
Morteza Razavi ◽  
Lisa DS Johnson ◽  
Julian J Lum ◽  
Gary Kruppa ◽  
N Leigh Anderson ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Liquid Chromatography ◽  
High Throughput ◽  
Protein C ◽  
Specific Antigen ◽  
Serum Concentrations ◽  
Serum Samples ◽  
Biomarker Validation ◽  
Protein C Inhibitor ◽  
Proteotypic Peptide

BACKGROUND Biomarker validation remains one of the most challenging constraints to the development of new diagnostic assays. To facilitate biomarker validation, we previously developed a chromatography-free stable isotope standards and capture by antipeptide antibodies (SISCAPA)-MALDI assay allowing rapid, high-throughput quantification of protein analytes in large sample sets. Here we applied this assay to the measurement of a surrogate proteotypic peptide from protein C inhibitor (PCI) in sera from patients with prostate cancer. METHODS A 2-plex SISCAPA-MALDI assay for quantification of proteotypic peptides from PCI and soluble transferrin receptor (sTfR) was used to measure these peptides in 159 trypsin-digested sera collected from 51 patients with prostate cancer. These patients had been treated with radiation with or without neoadjuvant androgen deprivation. RESULTS Patients who experienced biochemical recurrence of prostate cancer showed decreased serum concentrations of the PCI peptide analyte within 18 months of treatment. The PCI peptide concentrations remained increased in the sera of patients who did not experience cancer recurrence. Prostate-specific antigen concentrations had no predictive value during the same time period. CONCLUSIONS The high-throughput, liquid chromatography–free SISCAPA-MALDI assay is capable of rapid quantification of proteotypic PCI and sTfR peptide analytes in complex serum samples. Decreased serum concentrations of the PCI peptide were found to be related to recurrence of prostate cancer in patients treated with radiation with or without hormone therapy. However, a larger cohort of patients will be required for unequivocal validation of the PCI peptide as a biomarker for clinical use.

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