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Structure, function...
Structure, function, and regulation of the enzyme activity of prostate-specific antigen
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- Lilja, H. (author)
- Lund University,Lunds universitet,Klinisk kemi, Malmö,Forskargrupper vid Lunds universitet,Clinical Chemistry, Malmö,Lund University Research Groups,Skåne University Hospital
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(creator_code:org_t)
- 1993
- 1993
- English.
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In: World Journal of Urology. - 0724-4983. ; 11:4, s. 188-191
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http://dx.doi.org/10...
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Abstract
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- 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.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Läkemedelskemi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Medicinal Chemistry (hsv//eng)
Publication and Content Type
- art (subject category)
- ref (subject category)
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