scholarly journals Presence and enzymatic activity of prostate-specific antigen in archival prostate cancer samples

1994 ◽  
Vol 20 (4) ◽  
Author(s):  
Duivenvoorden
Keyword(s):  
Prostate Cancer ◽  
Enzymatic Activity ◽  
Prostate Specific Antigen ◽  
Specific Antigen

scholarly journals Anti-Free Prostate-specific Antigen Monoclonal Antibody Epitopes Defined by Mimotopes and Molecular Modeling

1999 ◽  
Vol 45 (5) ◽  
pp. 638-650 ◽  
Author(s):  
Sandrine Michel ◽  
Gilbert Deléage ◽  
Jean-Philippe Charrier ◽  
Jacques Passagot ◽  
Nicole Battail-Poirot ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Molecular Modeling ◽  
Enzymatic Activity ◽  
Prostate Specific Antigen ◽  
Specific Antigen ◽  
Free Psa ◽  
Total Psa ◽  
Sandwich Assays ◽  
Antibody Epitopes

Abstract Background: Prostate-specific antigen (PSA) is an important marker for the diagnosis and management of prostate cancer, and the free PSA/total PSA ratio has been shown to be efficient for distinguishing prostate cancer from benign prostatic hyperplasia. We report here the characterization of seven mouse monoclonal antibodies (mAbs) and the partial localization of two conformational epitopes identified by anti-free PSA mAbs. Methods: The mAbs were studied by competition and sandwich assays, and the epitope localization of the two anti-free PSA mAbs (6C8D8 and 5D3D11) was performed using phage displayed peptide libraries and molecular modeling. Results: The seven mAbs were classified into three groups according to their recognition specificities and their ability to inhibit the enzymatic activity of PSA and the formation of PSA-α1-antichymotrypsin (ACT) complex. Among the anti-free PSA mAb group, 6C8D8 recognized the phage displayed peptide RKLRPHWLHFHPVAV, two parts of which presented similarities with two regions distant on the PSA sequence but joined in the tridimensional structure. mAb 5D3D11 recognized the peptide DTPYPWGWLLDEGYD, which is similar to a PSA region located on the board of the groove containing the PSA enzymatic site. Both epitopes were located in the theoretical ACT binding site described previously. Moreover, these mAbs were able to inhibit the enzymatic activity of PSA. Conclusions: These epitope localizations are in agreement with the ability of both mAbs to inhibit enzymatic activity and ACT fixation. The results presented here could bring information for the generation of clinically relevant PSA assays.

1267: Prostate-Specific Antigen Velocity among African-American and White Men Without Prostate Cancer

2004 ◽  
Vol 171 (4S) ◽  
pp. 334-334
Author(s):  
Walter J. Simoneaux ◽  
Caleb B. Bozeman ◽  
Brett S. Carver ◽  
Donald A. Elmajian
Keyword(s):  
Prostate Cancer ◽  
African American ◽  
Prostate Specific Antigen ◽  
Specific Antigen ◽  
White Men

1662: Volume-Based Evaluation of the Ratio of Precursor Prostate-Specific Antigen Isoforms in the Detection of Prostate Cancer

2004 ◽  
Vol 171 (4S) ◽  
pp. 439-440
Author(s):  
Yoshio Naya ◽  
Herbert A. Fritsche ◽  
Viju A. Bhadkamkar ◽  
Stephen D. Mikolajczyk ◽  
Harry G. Rittenhouse ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Prostate Specific Antigen ◽  
Specific Antigen
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