A kallikrein-like serine protease in prostatic fluid cleaves the predominant seminal vesicle protein
(1985) In Journal of Clinical Investigation 76(5). p.1899-1903- Abstract
A 33-kD glycoprotein, known as the 'prostate-specific antigen', was purified to homogeneity from human seminal plasma. The prostatic protein was identified as a serine protease, and its NH2-terminal sequence strongly suggests that it belongs to the family of glandular kallikreins. The structural protein of human seminal coagulum, the predominant protein in seminal vesicle secretion, was rapidly cleaved by the prostatic enzyme, which suggests that this seminal vesicle protein may serve as the physiological substrate for the protease. The prostatic enzyme hydrolyzed arginine- and lysine-containing substrates with a distinct preference for the former. All synthetic substrates tested were poor substrates for the enzyme. Synthetic... (More)
A 33-kD glycoprotein, known as the 'prostate-specific antigen', was purified to homogeneity from human seminal plasma. The prostatic protein was identified as a serine protease, and its NH2-terminal sequence strongly suggests that it belongs to the family of glandular kallikreins. The structural protein of human seminal coagulum, the predominant protein in seminal vesicle secretion, was rapidly cleaved by the prostatic enzyme, which suggests that this seminal vesicle protein may serve as the physiological substrate for the protease. The prostatic enzyme hydrolyzed arginine- and lysine-containing substrates with a distinct preference for the former. All synthetic substrates tested were poor substrates for the enzyme. Synthetic Factor XI(a) substrate (pyroglutamyl-prolyl-arginine-p-nitroanilide), and the synthetic kallikrein substrate (H-D-prolyl-phenylalanyl-arginine-p-nitroanilide) were hydrolyzed with maximum specific activities at 23°C of 79 and 34 nmol/min per mg and K(m) values of 1.0 and 0.45 mM, respectively. Synthetic substrates for plasmin, chymotrypsin, and elastase were either not hydrolyzed by the enzyme at all, or only hydrolyzed very slowly.
(Less)
- author
- Lilja, H. LU
- organization
- publishing date
- 1985
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Clinical Investigation
- volume
- 76
- issue
- 5
- pages
- 1899 - 1903
- publisher
- The American Society for Clinical Investigation
- external identifiers
-
- pmid:3902893
- scopus:0022357088
- ISSN
- 0021-9738
- DOI
- 10.1172/JCI112185
- language
- English
- LU publication?
- yes
- id
- 87ff7009-c17c-4cf3-8d79-b2656960b68a
- date added to LUP
- 2022-12-06 16:52:04
- date last changed
- 2024-04-04 12:15:25
@article{87ff7009-c17c-4cf3-8d79-b2656960b68a, abstract = {{<p>A 33-kD glycoprotein, known as the 'prostate-specific antigen', was purified to homogeneity from human seminal plasma. The prostatic protein was identified as a serine protease, and its NH<sub>2</sub>-terminal sequence strongly suggests that it belongs to the family of glandular kallikreins. The structural protein of human seminal coagulum, the predominant protein in seminal vesicle secretion, was rapidly cleaved by the prostatic enzyme, which suggests that this seminal vesicle protein may serve as the physiological substrate for the protease. The prostatic enzyme hydrolyzed arginine- and lysine-containing substrates with a distinct preference for the former. All synthetic substrates tested were poor substrates for the enzyme. Synthetic Factor XI(a) substrate (pyroglutamyl-prolyl-arginine-p-nitroanilide), and the synthetic kallikrein substrate (H-D-prolyl-phenylalanyl-arginine-p-nitroanilide) were hydrolyzed with maximum specific activities at 23°C of 79 and 34 nmol/min per mg and K(m) values of 1.0 and 0.45 mM, respectively. Synthetic substrates for plasmin, chymotrypsin, and elastase were either not hydrolyzed by the enzyme at all, or only hydrolyzed very slowly.</p>}}, author = {{Lilja, H.}}, issn = {{0021-9738}}, language = {{eng}}, number = {{5}}, pages = {{1899--1903}}, publisher = {{The American Society for Clinical Investigation}}, series = {{Journal of Clinical Investigation}}, title = {{A kallikrein-like serine protease in prostatic fluid cleaves the predominant seminal vesicle protein}}, url = {{http://dx.doi.org/10.1172/JCI112185}}, doi = {{10.1172/JCI112185}}, volume = {{76}}, year = {{1985}}, }