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Structure, function, and regulation of the enzyme activity of prostate-specific antigen

Lilja, H. LU orcid (1993) In World Journal of Urology 11(4). p.188-191
Abstract

Prostate-specific antigen (PSA) and human glandular kallikrein 1 (hGK-1) are structurally similar products of the human glandular kallikrein gene locus on chromosome 19 that become selectively expressed by human prostate tissue. PSA is one of the most abundant prostate-derived proteins in the seminal fluid. The mature form of PSA, a single-chain glycoprotein of 237 amino acids, is a serine protease manifesting restricted chymotrypsin-like activity. PSA is mainly responsible for gel dissolution in freshly ejaculated semen by proteolysis of the major gel-forming proteins semenogelin I and II and fibronectin. PSA complexed to α1-antichymotrypsin (ACT) is the predominant molecular form of serum PSA, although complex formation is... (More)

Prostate-specific antigen (PSA) and human glandular kallikrein 1 (hGK-1) are structurally similar products of the human glandular kallikrein gene locus on chromosome 19 that become selectively expressed by human prostate tissue. PSA is one of the most abundant prostate-derived proteins in the seminal fluid. The mature form of PSA, a single-chain glycoprotein of 237 amino acids, is a serine protease manifesting restricted chymotrypsin-like activity. PSA is mainly responsible for gel dissolution in freshly ejaculated semen by proteolysis of the major gel-forming proteins semenogelin I and II and fibronectin. PSA complexed to α1-antichymotrypsin (ACT) is the predominant molecular form of serum PSA, although complex formation is slow between the purified proteins in vitro. PSA also forms stable complexes with α2-macroglobulin (α2M) in vitro, but as this results in encapsulation of PSA and complete loss of the PSA epitopes, the in vivo significance of this complex formation is presently unclear. A free, noncomplexed form of PSA constitutes a minor fraction of the serum PSA, although serum ACT occurs at large molar excess.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
World Journal of Urology
volume
11
issue
4
pages
188 - 191
publisher
Springer
external identifiers
  • scopus:0027757544
  • pmid:7508781
ISSN
0724-4983
DOI
10.1007/BF00185066
language
English
LU publication?
yes
id
3bfd4934-626d-4e2c-ba20-105590019fa4
date added to LUP
2022-12-08 13:06:45
date last changed
2024-05-16 13:47:13
@article{3bfd4934-626d-4e2c-ba20-105590019fa4,
  abstract     = {{<p>Prostate-specific antigen (PSA) and human glandular kallikrein 1 (hGK-1) are structurally similar products of the human glandular kallikrein gene locus on chromosome 19 that become selectively expressed by human prostate tissue. PSA is one of the most abundant prostate-derived proteins in the seminal fluid. The mature form of PSA, a single-chain glycoprotein of 237 amino acids, is a serine protease manifesting restricted chymotrypsin-like activity. PSA is mainly responsible for gel dissolution in freshly ejaculated semen by proteolysis of the major gel-forming proteins semenogelin I and II and fibronectin. PSA complexed to α<sub>1</sub>-antichymotrypsin (ACT) is the predominant molecular form of serum PSA, although complex formation is slow between the purified proteins in vitro. PSA also forms stable complexes with α<sub>2</sub>-macroglobulin (α<sub>2</sub>M) in vitro, but as this results in encapsulation of PSA and complete loss of the PSA epitopes, the in vivo significance of this complex formation is presently unclear. A free, noncomplexed form of PSA constitutes a minor fraction of the serum PSA, although serum ACT occurs at large molar excess.</p>}},
  author       = {{Lilja, H.}},
  issn         = {{0724-4983}},
  language     = {{eng}},
  number       = {{4}},
  pages        = {{188--191}},
  publisher    = {{Springer}},
  series       = {{World Journal of Urology}},
  title        = {{Structure, function, and regulation of the enzyme activity of prostate-specific antigen}},
  url          = {{http://dx.doi.org/10.1007/BF00185066}},
  doi          = {{10.1007/BF00185066}},
  volume       = {{11}},
  year         = {{1993}},
}