Cell biology of semenogelin
Lilja, H. LU
(1990)
In Andrologia
22(1 S).
p.132-141
- Abstract
Summary Semenogelin is the predominant protein in human semen. It is synthetised by the secretory epithelium of the seminal vesicles as a 461 amino acid precursor protein. Following cleavage of a predominantly hydrophobic signal peptide, the secreted protein contains 439 amino acid residues. The amino acid sequence of semenogelin has a repetitive structure, but it displays no significant homology to any other characterized translation product. In the seminal vesicle secretion, semenogelin occurs in disulphide‐linked high molecular mass complexes together with two less abundant 71 and 76 kDa proteins. These proteins have a very close antigenic and structural relationship to semenogelin, but contrary to semenogelin one or both of these... (More)
Summary Semenogelin is the predominant protein in human semen. It is synthetised by the secretory epithelium of the seminal vesicles as a 461 amino acid precursor protein. Following cleavage of a predominantly hydrophobic signal peptide, the secreted protein contains 439 amino acid residues. The amino acid sequence of semenogelin has a repetitive structure, but it displays no significant homology to any other characterized translation product. In the seminal vesicle secretion, semenogelin occurs in disulphide‐linked high molecular mass complexes together with two less abundant 71 and 76 kDa proteins. These proteins have a very close antigenic and structural relationship to semenogelin, but contrary to semenogelin one or both of these semenogelin‐related proteins are also expressed by the secretory epithelium of the epididymis. Semenogelin and the semenogelin‐related proteins are the major proteins involved in the gelatinous entrapment of ejaculated spermatozoa. Antigenic epitopes common to these proteins are localised to the locomotive parts of the spermatozoa. The spermatozoa become progressively motile when gel‐forming proteins are fragmented by the kallikrein‐like protease, prostate‐specific antigen, and the gel dissolves.
(Less)
- author
- Lilja, H.
LU
- organization
- publishing date
- 1990-07
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Kallikreins, prostate, semen, seminal vesicle, spermatozoa
- in
- Andrologia
- volume
- 22
- issue
- 1 S
- pages
- 132 - 141
- publisher
- Wiley-Blackwell
- external identifiers
-
- scopus:0025564292
- pmid:2132066
- ISSN
- 0303-4569
- DOI
- 10.1111/j.1439-0272.1990.tb02079.x
- language
- English
- LU publication?
- yes
- additional info
- Abstract in German Zusammenfassung Semenogelin ist das vorherrschende Protein im menschlichem Samen. Es wird als ein 461 Aminosäuren enthaltendes Vorläuferprotein im sekretorischen Epithel der Bläschendrüse synthetisiert. Nach der Abspaltung eines vorwiegend hydrophoben Signalpeptids enthält das sezernierte Protein 439 Aminosäurereste. Die Aminosäurese‐quenz hat eine repetitive Struktur, aber es zeigt keine signifikante Homologie mit irgendeinem anderen charakterisierten Translationsprodukt. Im Sekret der Bläschendrüse erscheint Semenogelin in Disulfid‐verknüpften hochmolekularen Komplexen zusammen mit zwei weniger massenhaften 71 und 76 kDa Proteinen. Diese Proteine haben eine sehr enge Antigen‐ und Strukturverwandtschaft mit Semenogelin, aber im Gegensatz zu Semenogelin erscheinen beide oder mindestens eines dieser Semenogelin‐verwandten Proteine im sekretorischen Epithel des Nebenhodens. Semenogelin und die Semenogelin‐verwandten Proteine sind die wichtigsten Faktoren bei der gelatinösen Fixierung ejakulierter Spermien. Antigene Epitope, die diesen Proteinen gemeinsam sind, sind auch auf den lokomotorischen Abschnitten der Spermien lokalisiert. Die Spermien werden zunehmend motil, wenn diese Gel‐bildenden Proteine durch eine Kallikrein‐ähnliche Protease, das Prostate‐Specific‐Antigen, fragmentiert werden und das Gel sich auflöst. 1990 Blackwell Verlag GmbH
- id
- 8dc5bfb8-0977-4a6e-b9e6-caa01c4ab093
- date added to LUP
- 2022-12-08 13:07:50
- date last changed
- 2024-01-02 13:39:45
@article{8dc5bfb8-0977-4a6e-b9e6-caa01c4ab093,
abstract = {{<p>Summary Semenogelin is the predominant protein in human semen. It is synthetised by the secretory epithelium of the seminal vesicles as a 461 amino acid precursor protein. Following cleavage of a predominantly hydrophobic signal peptide, the secreted protein contains 439 amino acid residues. The amino acid sequence of semenogelin has a repetitive structure, but it displays no significant homology to any other characterized translation product. In the seminal vesicle secretion, semenogelin occurs in disulphide‐linked high molecular mass complexes together with two less abundant 71 and 76 kDa proteins. These proteins have a very close antigenic and structural relationship to semenogelin, but contrary to semenogelin one or both of these semenogelin‐related proteins are also expressed by the secretory epithelium of the epididymis. Semenogelin and the semenogelin‐related proteins are the major proteins involved in the gelatinous entrapment of ejaculated spermatozoa. Antigenic epitopes common to these proteins are localised to the locomotive parts of the spermatozoa. The spermatozoa become progressively motile when gel‐forming proteins are fragmented by the kallikrein‐like protease, prostate‐specific antigen, and the gel dissolves. <br/></p>}},
author = {{Lilja, H.}},
issn = {{0303-4569}},
keywords = {{Kallikreins; prostate; semen; seminal vesicle; spermatozoa}},
language = {{eng}},
number = {{1 S}},
pages = {{132--141}},
publisher = {{Wiley-Blackwell}},
series = {{Andrologia}},
title = {{Cell biology of semenogelin}},
url = {{http://dx.doi.org/10.1111/j.1439-0272.1990.tb02079.x}},
doi = {{10.1111/j.1439-0272.1990.tb02079.x}},
volume = {{22}},
year = {{1990}},
}