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Production and characterization of novel anti-prostate-specific antigen (PSA) monoclonal antibodies that do not detect internally cleaved Lys145-Lys146 inactive PSA

Nurmikko, P. ; Vaisanen, V. ; Piironen, T. ; Lindgren, S. and Lilja, H. LU orcid (2000) In Clinical Chemistry 46(10). p.1610-1618
Abstract

Background: The nature of free, uncomplexed prostate-specific antigen (s) in the circulation is still unknown. In this study, we developed novel anti-PSA antibodies using PSA produced by a metastasized cancer cell line, LNCaP, as an immunogen. Methods: Hybridoma cell lines were screened with different methods that aimed at finding antibodies specific for the forms of free PSA produced by LNCaP cell line. Obtained antibodies were further studied for their characteristics related to previously characterized monoclonal antibodies. Results: Numerous anti-PSA antibodies were obtained, of which four represented unique epitopes previously unrecognized by us. One free-PSA-specific antibody was bound to PSA on two distinct epitopes, and one... (More)

Background: The nature of free, uncomplexed prostate-specific antigen (s) in the circulation is still unknown. In this study, we developed novel anti-PSA antibodies using PSA produced by a metastasized cancer cell line, LNCaP, as an immunogen. Methods: Hybridoma cell lines were screened with different methods that aimed at finding antibodies specific for the forms of free PSA produced by LNCaP cell line. Obtained antibodies were further studied for their characteristics related to previously characterized monoclonal antibodies. Results: Numerous anti-PSA antibodies were obtained, of which four represented unique epitopes previously unrecognized by us. One free-PSA-specific antibody was bound to PSA on two distinct epitopes, and one antibody was bound to the carboxyl-terminal peptide of PSA. Two antibodies were found to bind to the peptide sequence adjacent to the internal cleavage site Lys145-Lys146. These antibodies failed to recognize internally cleaved PSA at Lys145-Lys146. We could not find anti-proPSA antibodies despite the fact that LNCaP PSA contained more than one-half of the zymogen form of PSA. Conclusions: We report, for the first time, novel anti-PSA antibodies that do not recognize internally cleaved PSA at Lys145-Lys146 and thus are specific for intact, unclipped PSA. (C) 2000 American Association for Clinical Chemistry.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Clinical Chemistry
volume
46
issue
10
pages
1610 - 1618
publisher
American Association for Clinical Chemistry
external identifiers
  • scopus:0033779889
  • pmid:11017939
ISSN
0009-9147
DOI
10.1093/clinchem/46.10.1610
language
English
LU publication?
yes
id
259967d8-63be-4af9-a268-5af54eba97f9
date added to LUP
2022-12-17 16:57:41
date last changed
2024-06-13 13:40:27
@article{259967d8-63be-4af9-a268-5af54eba97f9,
  abstract     = {{<p>Background: The nature of free, uncomplexed prostate-specific antigen (s) in the circulation is still unknown. In this study, we developed novel anti-PSA antibodies using PSA produced by a metastasized cancer cell line, LNCaP, as an immunogen. Methods: Hybridoma cell lines were screened with different methods that aimed at finding antibodies specific for the forms of free PSA produced by LNCaP cell line. Obtained antibodies were further studied for their characteristics related to previously characterized monoclonal antibodies. Results: Numerous anti-PSA antibodies were obtained, of which four represented unique epitopes previously unrecognized by us. One free-PSA-specific antibody was bound to PSA on two distinct epitopes, and one antibody was bound to the carboxyl-terminal peptide of PSA. Two antibodies were found to bind to the peptide sequence adjacent to the internal cleavage site Lys145-Lys146. These antibodies failed to recognize internally cleaved PSA at Lys145-Lys146. We could not find anti-proPSA antibodies despite the fact that LNCaP PSA contained more than one-half of the zymogen form of PSA. Conclusions: We report, for the first time, novel anti-PSA antibodies that do not recognize internally cleaved PSA at Lys145-Lys146 and thus are specific for intact, unclipped PSA. (C) 2000 American Association for Clinical Chemistry.</p>}},
  author       = {{Nurmikko, P. and Vaisanen, V. and Piironen, T. and Lindgren, S. and Lilja, H.}},
  issn         = {{0009-9147}},
  language     = {{eng}},
  number       = {{10}},
  pages        = {{1610--1618}},
  publisher    = {{American Association for Clinical Chemistry}},
  series       = {{Clinical Chemistry}},
  title        = {{Production and characterization of novel anti-prostate-specific antigen (PSA) monoclonal antibodies that do not detect internally cleaved Lys145-Lys146 inactive PSA}},
  url          = {{http://dx.doi.org/10.1093/clinchem/46.10.1610}},
  doi          = {{10.1093/clinchem/46.10.1610}},
  volume       = {{46}},
  year         = {{2000}},
}