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Prostate specific antigen predominantly forms a complex with alpha1‐antichymotrypsin in blood. Implications for procedures to measure prostate specific antigen in serum

Lilja, Hans LU orcid ; Cockett, Abraham T.K. and Abrahamsson, Per‐Anders LU (1992) In Cancer 70(S1). p.230-234
Abstract

Background. Prostate specific antigen (PSA) is a zymogen of a 33‐kilodalton (kD) serine proteinase with extensive similarity to glandular kallikreins. The mechanism responsible for converting the zymogen into active proteinase has not been defined, but active PSA may be irreversibly inactivated in vitro by two of the major proteinase inhibitors in blood: alpha1‐antichymotrypsin and alpha2‐macroglobulin. Methods. Procedures have been designed to characterize the different molecular forms of PSA in serum. One assay detects PSA epitopes available on both PSA binding to serine proteinase inhibitors and PSA not binding to a proteinase inhibitor. A second assay only detects PSA in complex with... (More)

Background. Prostate specific antigen (PSA) is a zymogen of a 33‐kilodalton (kD) serine proteinase with extensive similarity to glandular kallikreins. The mechanism responsible for converting the zymogen into active proteinase has not been defined, but active PSA may be irreversibly inactivated in vitro by two of the major proteinase inhibitors in blood: alpha1‐antichymotrypsin and alpha2‐macroglobulin. Methods. Procedures have been designed to characterize the different molecular forms of PSA in serum. One assay detects PSA epitopes available on both PSA binding to serine proteinase inhibitors and PSA not binding to a proteinase inhibitor. A second assay only detects PSA in complex with alpha1‐antichymotrypsin. A third assay mainly detects PSA not binding to a proteinase inhibitor. Results. In serum samples, an 80‐kD to 90‐kD species of PSA in complex with alpha1‐antichymotrypsin is the predominant molecular form and a minor molecular form of serum PSA was an approximately 30‐kD fraction not binding to a proteinase inhibitor. Conclusions. The benefits of detecting different molecular forms of serum PSA should be investigated regarding possibilities to facilitate differential diagnosis of carcinoma of the prostate (CAP) and benign prostatic hyperplasia (BPH).

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organization
publishing date
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Contribution to journal
publication status
published
subject
keywords
alpha‐antichymotrypsin, benign prostatic hyperplasia, glandular kallikreins, immunoassays, prostate cancer, prostate specific antigen, serine proteinase inhibitors
in
Cancer
volume
70
issue
S1
pages
230 - 234
publisher
John Wiley & Sons Inc.
external identifiers
  • pmid:1376193
  • scopus:0026624757
ISSN
0008-543X
DOI
10.1002/1097-0142(19920701)70:1+<230::AID-CNCR2820701310>3.0.CO;2-Y
language
English
LU publication?
yes
id
cf8e89e0-13c0-4422-9108-2ac67afc5603
date added to LUP
2022-12-08 13:01:25
date last changed
2025-04-05 03:36:48
@article{cf8e89e0-13c0-4422-9108-2ac67afc5603,
  abstract     = {{<p>Background. Prostate specific antigen (PSA) is a zymogen of a 33‐kilodalton (kD) serine proteinase with extensive similarity to glandular kallikreins. The mechanism responsible for converting the zymogen into active proteinase has not been defined, but active PSA may be irreversibly inactivated in vitro by two of the major proteinase inhibitors in blood: alpha<sub>1</sub>‐antichymotrypsin and alpha<sub>2</sub>‐macroglobulin. Methods. Procedures have been designed to characterize the different molecular forms of PSA in serum. One assay detects PSA epitopes available on both PSA binding to serine proteinase inhibitors and PSA not binding to a proteinase inhibitor. A second assay only detects PSA in complex with alpha<sub>1</sub>‐antichymotrypsin. A third assay mainly detects PSA not binding to a proteinase inhibitor. Results. In serum samples, an 80‐kD to 90‐kD species of PSA in complex with alpha<sub>1</sub>‐antichymotrypsin is the predominant molecular form and a minor molecular form of serum PSA was an approximately 30‐kD fraction not binding to a proteinase inhibitor. Conclusions. The benefits of detecting different molecular forms of serum PSA should be investigated regarding possibilities to facilitate differential diagnosis of carcinoma of the prostate (CAP) and benign prostatic hyperplasia (BPH).</p>}},
  author       = {{Lilja, Hans and Cockett, Abraham T.K. and Abrahamsson, Per‐Anders}},
  issn         = {{0008-543X}},
  keywords     = {{alpha‐antichymotrypsin; benign prostatic hyperplasia; glandular kallikreins; immunoassays; prostate cancer; prostate specific antigen; serine proteinase inhibitors}},
  language     = {{eng}},
  month        = {{07}},
  number       = {{S1}},
  pages        = {{230--234}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{Cancer}},
  title        = {{Prostate specific antigen predominantly forms a complex with alpha<sub>1</sub>‐antichymotrypsin in blood. Implications for procedures to measure prostate specific antigen in serum}},
  url          = {{http://dx.doi.org/10.1002/1097-0142(19920701)70:1+<230::AID-CNCR2820701310>3.0.CO;2-Y}},
  doi          = {{10.1002/1097-0142(19920701)70:1+<230::AID-CNCR2820701310>3.0.CO;2-Y}},
  volume       = {{70}},
  year         = {{1992}},
}