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Characterization of epitope structure for 53 monoclonal antibodies against prostate-specific antigen

Becker, Charlotte LU ; Wigheden, Ingrid LU and Lilja, Hans LU (1999) In Tumor Biology 20(Suppl. 1). p.13-17
Abstract
Prostate-specific antigen (PSA) is the most widely used marker of prostate cancer. Assays for PSA are based on anti-PSA antibodies, and the characterization and selection of these antibodies is important for determining their optimum performance. In our study, we characterized the reactivity of 53 antibodies, submitted to the ISOBM TD-3 PSA Workshop, using free PSA, PSA complexed to alpha1-antichymotrypsin (ACT) and purified ACT. Immunoblotting was performed after native agarose gel or reducing sodium dodecyl polyacrylamide gel electrophoresis. Immunoblotting after agarose gel electrophoresis revealed 10 antibodies that recognized only the free form of PSA, and 43 antibodies that detected both free PSA and PSA-ACT. Immunoblotting of... (More)
Prostate-specific antigen (PSA) is the most widely used marker of prostate cancer. Assays for PSA are based on anti-PSA antibodies, and the characterization and selection of these antibodies is important for determining their optimum performance. In our study, we characterized the reactivity of 53 antibodies, submitted to the ISOBM TD-3 PSA Workshop, using free PSA, PSA complexed to alpha1-antichymotrypsin (ACT) and purified ACT. Immunoblotting was performed after native agarose gel or reducing sodium dodecyl polyacrylamide gel electrophoresis. Immunoblotting after agarose gel electrophoresis revealed 10 antibodies that recognized only the free form of PSA, and 43 antibodies that detected both free PSA and PSA-ACT. Immunoblotting of reducing sodium dodecyl-polyacrylamide gels showed the linear or conformation-dependent nature of the epitopes. Two antibodies specific for free PSA and 18 antibodies that recognized both free PSA and PSA-ACT complex recognized linear epitopes. Moreover, 7 antibodies also detected fragmented forms of PSA. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Monoclonal antibodies, ISOBM, TD-3, Prostate-specific antigen, alpha1-antichymotrypsin, Immunoblotting, Epitopes
in
Tumor Biology
volume
20
issue
Suppl. 1
pages
13 - 17
publisher
Springer
external identifiers
  • pmid:10628403
  • scopus:0032705024
ISSN
1423-0380
DOI
10.1159/000056524
language
English
LU publication?
yes
id
9caf6db1-d29f-402b-85b8-4c059ad82369 (old id 1115150)
date added to LUP
2008-07-07 15:02:01
date last changed
2017-01-01 06:38:35
@article{9caf6db1-d29f-402b-85b8-4c059ad82369,
  abstract     = {Prostate-specific antigen (PSA) is the most widely used marker of prostate cancer. Assays for PSA are based on anti-PSA antibodies, and the characterization and selection of these antibodies is important for determining their optimum performance. In our study, we characterized the reactivity of 53 antibodies, submitted to the ISOBM TD-3 PSA Workshop, using free PSA, PSA complexed to alpha1-antichymotrypsin (ACT) and purified ACT. Immunoblotting was performed after native agarose gel or reducing sodium dodecyl polyacrylamide gel electrophoresis. Immunoblotting after agarose gel electrophoresis revealed 10 antibodies that recognized only the free form of PSA, and 43 antibodies that detected both free PSA and PSA-ACT. Immunoblotting of reducing sodium dodecyl-polyacrylamide gels showed the linear or conformation-dependent nature of the epitopes. Two antibodies specific for free PSA and 18 antibodies that recognized both free PSA and PSA-ACT complex recognized linear epitopes. Moreover, 7 antibodies also detected fragmented forms of PSA.},
  author       = {Becker, Charlotte and Wigheden, Ingrid and Lilja, Hans},
  issn         = {1423-0380},
  keyword      = {Monoclonal antibodies,ISOBM,TD-3,Prostate-specific antigen,alpha1-antichymotrypsin,Immunoblotting,Epitopes},
  language     = {eng},
  number       = {Suppl. 1},
  pages        = {13--17},
  publisher    = {Springer},
  series       = {Tumor Biology},
  title        = {Characterization of epitope structure for 53 monoclonal antibodies against prostate-specific antigen},
  url          = {http://dx.doi.org/10.1159/000056524},
  volume       = {20},
  year         = {1999},
}