Exogenous protein kinases A and C, but not endogenous prostasome-associated protein kinase, phosphorylate semenogelins I and II from human semen
Ek, P ; Malm, Johan LU ; Lilja, Hans LU
; Carlsson, L
and Ronquist, G
(2002)
In Journal of Andrology
23(6).
p.806-814
- Abstract
- Semenogelins I and II are the quantitatively dominating proteins in human semen. They comprise the major part of the sperm-entrapping gel formed at ejaculation, which subsequently liquefies due to proteolysis of the gel-forming proteins by prostate-specific antigen (PSA). The mechanism behind gel formation and its physiological significance is not known. We have studied phosphorylation and dephosphorylation of human semenogelins. Both were phosphorylated by protein kinases A and C (PKA and PKC, respectively) at a rate about 5 times less than that of histone. For PKA, incorporated ( P)phosphate into semenogelin approached a maximum above 1 mol/mol. Corresponding values for phosphorylation of the semenogelins with PKC were greater than 10.... (More)
- Semenogelins I and II are the quantitatively dominating proteins in human semen. They comprise the major part of the sperm-entrapping gel formed at ejaculation, which subsequently liquefies due to proteolysis of the gel-forming proteins by prostate-specific antigen (PSA). The mechanism behind gel formation and its physiological significance is not known. We have studied phosphorylation and dephosphorylation of human semenogelins. Both were phosphorylated by protein kinases A and C (PKA and PKC, respectively) at a rate about 5 times less than that of histone. For PKA, incorporated ( P)phosphate into semenogelin approached a maximum above 1 mol/mol. Corresponding values for phosphorylation of the semenogelins with PKC were greater than 10. There was no change in the sensitivity of phosphosemenogelins to proteolysis by PSA. Serine (PKA) and serine and threonine (PKC) were the phosphate-accepting amino acid residues, and all incorporated (P-32)phosphate could be removed from the semenogelins with human acid phosphatase. Nil or very little phosphate could be detected in purified semenogelins isolated from seminal plasma. In vivo, about half the protein kinase activity in seminal plasma was bound to prostasomes. PKA but not PKC purified from prostasomes could phosphorylate specific substrates, but they could phosphorylate either of the semenogelins. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/324240
- author
- Ek, P
; Malm, Johan
LU
; Lilja, Hans
LU
; Carlsson, L
and Ronquist, G
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- prostate-specific antigen, acid phosphatase, histone, vasectomy
- in
- Journal of Andrology
- volume
- 23
- issue
- 6
- pages
- 806 - 814
- publisher
- American Society of Andrology
- external identifiers
-
- wos:000179179700013
- scopus:0036868434
- ISSN
- 0196-3635
- language
- English
- LU publication?
- yes
- id
- ea09e266-114f-452b-87b1-dfcca2bac13e (old id 324240)
- alternative location
- http://www.andrologyjournal.org/cgi/content/abstract/23/6/806
- date added to LUP
- 2016-04-01 16:29:24
- date last changed
- 2022-02-27 21:34:54
@article{ea09e266-114f-452b-87b1-dfcca2bac13e,
abstract = {{Semenogelins I and II are the quantitatively dominating proteins in human semen. They comprise the major part of the sperm-entrapping gel formed at ejaculation, which subsequently liquefies due to proteolysis of the gel-forming proteins by prostate-specific antigen (PSA). The mechanism behind gel formation and its physiological significance is not known. We have studied phosphorylation and dephosphorylation of human semenogelins. Both were phosphorylated by protein kinases A and C (PKA and PKC, respectively) at a rate about 5 times less than that of histone. For PKA, incorporated ( P)phosphate into semenogelin approached a maximum above 1 mol/mol. Corresponding values for phosphorylation of the semenogelins with PKC were greater than 10. There was no change in the sensitivity of phosphosemenogelins to proteolysis by PSA. Serine (PKA) and serine and threonine (PKC) were the phosphate-accepting amino acid residues, and all incorporated (P-32)phosphate could be removed from the semenogelins with human acid phosphatase. Nil or very little phosphate could be detected in purified semenogelins isolated from seminal plasma. In vivo, about half the protein kinase activity in seminal plasma was bound to prostasomes. PKA but not PKC purified from prostasomes could phosphorylate specific substrates, but they could phosphorylate either of the semenogelins.}},
author = {{Ek, P and Malm, Johan and Lilja, Hans and Carlsson, L and Ronquist, G}},
issn = {{0196-3635}},
keywords = {{prostate-specific antigen; acid phosphatase; histone; vasectomy}},
language = {{eng}},
number = {{6}},
pages = {{806--814}},
publisher = {{American Society of Andrology}},
series = {{Journal of Andrology}},
title = {{Exogenous protein kinases A and C, but not endogenous prostasome-associated protein kinase, phosphorylate semenogelins I and II from human semen}},
url = {{http://www.andrologyjournal.org/cgi/content/abstract/23/6/806}},
volume = {{23}},
year = {{2002}},
}