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Seminal vesicle-secreted proteins and their reactions during gelation and liquefaction of human semen.

Lilja, H. LU orcid ; Oldbring, Jörgen ; Rannevik, G. and Laurell, C. B. LU (1987) In The Journal of clinical investigation 80(2). p.281-285
Abstract

The comparison of measurements of fibronectin and lactoferrin in ejaculates from vasectomized men, subjects with functional deficiency or aplasia of the seminal vesicles, and reference subjects provided evidence that both the fibronectin and the lactoferrin in human seminal fluid originate from the seminal vesicles and the ampullae. The fibronectin is incorporated in the framework of the seminal gel formed during the immediate postejaculatory phase, whereas the lactoferrin remains in solution. In the seminal gel fibronectin is linked to its predominant structural protein, a high molecular weight seminal vesicle protein (semenogelin). Both the gel-bound fibronectin and semenogelin are progressively fragmented and solubilized by the... (More)

The comparison of measurements of fibronectin and lactoferrin in ejaculates from vasectomized men, subjects with functional deficiency or aplasia of the seminal vesicles, and reference subjects provided evidence that both the fibronectin and the lactoferrin in human seminal fluid originate from the seminal vesicles and the ampullae. The fibronectin is incorporated in the framework of the seminal gel formed during the immediate postejaculatory phase, whereas the lactoferrin remains in solution. In the seminal gel fibronectin is linked to its predominant structural protein, a high molecular weight seminal vesicle protein (semenogelin). Both the gel-bound fibronectin and semenogelin are progressively fragmented and solubilized by the abundant prostatic kallikrein-like protease (prostate-specific antigen) during and after seminal gel liquefaction. Lactoferrin remains essentially unaffected by the seminal proteases.

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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
The Journal of clinical investigation
volume
80
issue
2
pages
281 - 285
publisher
The American Society for Clinical Investigation
external identifiers
  • pmid:3611349
  • scopus:0023392052
ISSN
0021-9738
DOI
10.1172/JCI113070
language
English
LU publication?
yes
id
56ab7f60-d032-4398-8df7-464e454af221
date added to LUP
2022-12-06 16:49:38
date last changed
2024-04-04 12:14:09
@article{56ab7f60-d032-4398-8df7-464e454af221,
  abstract     = {{<p>The comparison of measurements of fibronectin and lactoferrin in ejaculates from vasectomized men, subjects with functional deficiency or aplasia of the seminal vesicles, and reference subjects provided evidence that both the fibronectin and the lactoferrin in human seminal fluid originate from the seminal vesicles and the ampullae. The fibronectin is incorporated in the framework of the seminal gel formed during the immediate postejaculatory phase, whereas the lactoferrin remains in solution. In the seminal gel fibronectin is linked to its predominant structural protein, a high molecular weight seminal vesicle protein (semenogelin). Both the gel-bound fibronectin and semenogelin are progressively fragmented and solubilized by the abundant prostatic kallikrein-like protease (prostate-specific antigen) during and after seminal gel liquefaction. Lactoferrin remains essentially unaffected by the seminal proteases.</p>}},
  author       = {{Lilja, H. and Oldbring, Jörgen and Rannevik, G. and Laurell, C. B.}},
  issn         = {{0021-9738}},
  language     = {{eng}},
  number       = {{2}},
  pages        = {{281--285}},
  publisher    = {{The American Society for Clinical Investigation}},
  series       = {{The Journal of clinical investigation}},
  title        = {{Seminal vesicle-secreted proteins and their reactions during gelation and liquefaction of human semen.}},
  url          = {{http://dx.doi.org/10.1172/JCI113070}},
  doi          = {{10.1172/JCI113070}},
  volume       = {{80}},
  year         = {{1987}},
}