Structure, function, and regulation of the enzyme activity of prostate-specific antigen
(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.
(Less)
- author
- Lilja, H. LU
- organization
- publishing date
- 1993-12
- type
- Contribution to journal
- publication status
- published
- subject
- in
- World Journal of Urology
- volume
- 11
- issue
- 4
- pages
- 188 - 191
- publisher
- Springer
- external identifiers
-
- pmid:7508781
- scopus:0027757544
- 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}}, }