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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.

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author
publishing date
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
9 pages
publisher
Wiley-Blackwell
external identifiers
  • scopus:0025671852
  • pmid:1702714
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
2019-10-13 05:01:49
@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},
  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},
}