Enzymatic activity of prostate-specific antigen and its reactions with extracellular serine proteinase inhibitors
Christensson, A LU ; Laurell, C B LU and Lilja, H LU
(1990)
In European Journal of Biochemistry
194(3).
p.63-755
- Abstract
Prostate-specific antigen (PSA) is one of the three most abundant prostatic-secreted proteins in human semen. It is a serine proteinase that, in its primary structure, manifests extensive similarities with that of the Arg-restricted glandular kallikrein-like proteinases. When isolated from semen by the addition of chromatography on aprotinin-Sepharose to a previously described procedure, PSA displayed chymotrypsin-like activity and cleaved semenogelin and the semenogelin-related proteins in a rapid and characteristic pattern, but had no trypsin-like activity. About one third of the purified protein was found to be enzymatically inactive, due to cleavage carboxy-terminal of Lys145. Active PSA formed SDS-stable complexes with alpha... (More)
Prostate-specific antigen (PSA) is one of the three most abundant prostatic-secreted proteins in human semen. It is a serine proteinase that, in its primary structure, manifests extensive similarities with that of the Arg-restricted glandular kallikrein-like proteinases. When isolated from semen by the addition of chromatography on aprotinin-Sepharose to a previously described procedure, PSA displayed chymotrypsin-like activity and cleaved semenogelin and the semenogelin-related proteins in a rapid and characteristic pattern, but had no trypsin-like activity. About one third of the purified protein was found to be enzymatically inactive, due to cleavage carboxy-terminal of Lys145. Active PSA formed SDS-stable complexes with alpha 1-antichymotrypsin, alpha 2-macroglobulin-analogue pregnancy zone protein. PSA formed inhibitory complexes with alpha 1-antichymotrypsin at a molar ratio of 1:1, a reaction in which PSA cleaved the inhibitor in a position identical to that reported from the reaction between chymotrypsin and alpha 1-antichymotrypsin. The formation of stable complexes between PSA and alpha 1-antichymotrypsin occurred at a much slower rate than that between chymotrypsin and alpha 1-antichymotrypsin, and at a similar or slightly slower rate than that between PSA and alpha 2-macroglobulin. When added to normal blood plasma in vitro, active PSA formed stable complexes both with alpha 2-macroglobulin and alpha 1-antichymotrypsin. This complex formation may be a crucial determinant of the turnover of active PSA in intercellular fluid or blood plasma in vivo.
(Less)
- author
- Christensson, A
LU
; Laurell, C B
LU
and Lilja, H
LU
- publishing date
- 1990-12-27
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Amino Acid Sequence, Antigens, Neoplasm/isolation & purification, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Humans, Hydrolysis, Male, Molecular Sequence Data, Prostate-Specific Antigen, Serine Proteinase Inhibitors/metabolism, alpha 1-Antichymotrypsin/metabolism, alpha-Macroglobulins/metabolism
- in
- European Journal of Biochemistry
- volume
- 194
- issue
- 3
- pages
- 63 - 755
- publisher
- Wiley-Blackwell
- external identifiers
-
- pmid:1702714
- scopus:0025671852
- ISSN
- 0014-2956
- DOI
- 10.1111/j.1432-1033.1990.tb19466.x
- language
- English
- LU publication?
- no
- id
- 18af08f1-c9f2-42b4-9054-525497068371
- date added to LUP
- 2019-05-16 14:11:20
- date last changed
- 2024-05-29 09:50:38
@article{18af08f1-c9f2-42b4-9054-525497068371,
abstract = {{<p>Prostate-specific antigen (PSA) is one of the three most abundant prostatic-secreted proteins in human semen. It is a serine proteinase that, in its primary structure, manifests extensive similarities with that of the Arg-restricted glandular kallikrein-like proteinases. When isolated from semen by the addition of chromatography on aprotinin-Sepharose to a previously described procedure, PSA displayed chymotrypsin-like activity and cleaved semenogelin and the semenogelin-related proteins in a rapid and characteristic pattern, but had no trypsin-like activity. About one third of the purified protein was found to be enzymatically inactive, due to cleavage carboxy-terminal of Lys145. Active PSA formed SDS-stable complexes with alpha 1-antichymotrypsin, alpha 2-macroglobulin-analogue pregnancy zone protein. PSA formed inhibitory complexes with alpha 1-antichymotrypsin at a molar ratio of 1:1, a reaction in which PSA cleaved the inhibitor in a position identical to that reported from the reaction between chymotrypsin and alpha 1-antichymotrypsin. The formation of stable complexes between PSA and alpha 1-antichymotrypsin occurred at a much slower rate than that between chymotrypsin and alpha 1-antichymotrypsin, and at a similar or slightly slower rate than that between PSA and alpha 2-macroglobulin. When added to normal blood plasma in vitro, active PSA formed stable complexes both with alpha 2-macroglobulin and alpha 1-antichymotrypsin. This complex formation may be a crucial determinant of the turnover of active PSA in intercellular fluid or blood plasma in vivo.</p>}},
author = {{Christensson, A and Laurell, C B and Lilja, H}},
issn = {{0014-2956}},
keywords = {{Amino Acid Sequence; Antigens, Neoplasm/isolation & purification; Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Humans; Hydrolysis; Male; Molecular Sequence Data; Prostate-Specific Antigen; Serine Proteinase Inhibitors/metabolism; alpha 1-Antichymotrypsin/metabolism; alpha-Macroglobulins/metabolism}},
language = {{eng}},
month = {{12}},
number = {{3}},
pages = {{63--755}},
publisher = {{Wiley-Blackwell}},
series = {{European Journal of Biochemistry}},
title = {{Enzymatic activity of prostate-specific antigen and its reactions with extracellular serine proteinase inhibitors}},
url = {{http://dx.doi.org/10.1111/j.1432-1033.1990.tb19466.x}},
doi = {{10.1111/j.1432-1033.1990.tb19466.x}},
volume = {{194}},
year = {{1990}},
}