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beta-Microseminoprotein binds CRISP-3 in human seminal plasma

Udby, L; Lundwall, Åke LU ; Johnsen, A H; Fernlund, Per LU ; Valtonen-André, Camilla LU ; Blom, Anna LU ; Lilja, Hans LU ; Borregaard, N; Kieldsen, L and Bjartell, Anders LU (2005) In Biochemical and Biophysical Research Communications 333(2). p.555-561
Abstract
P-Microseminoprotein (MSP) and cysteine-rich secretory protein 3 (CRISP-3) are abundant constituents of human seminal plasma. Immunoprecipitation and gel filtration of seminal plasma proteins combined with examination of the proteins in their pure form showed that MSP and CRISP-3 form stable, non-covalent complexes. CRISP-3 binds MSP with very high affinity, as evidenced by surface plasmon resonance. Due to far higher abundance of MSP in prostatic fluid, it manifests large overcapacity for CRISP-3 binding. Structural similarity with an MSP-binding protein from blood plasma suggests that CRISP-3 binds MSP through its ami-terminal SCP-domain.
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
mass, spectrometry, surface plasmon resonance, SCP-domain, protein complex, prostate cancer, seminal plasma, PSP94, cysteine-rich secretory protein, beta-microseminoprotein
in
Biochemical and Biophysical Research Communications
volume
333
issue
2
pages
555 - 561
publisher
Elsevier
external identifiers
  • wos:000230418700039
  • pmid:15950934
  • scopus:20544459894
ISSN
1090-2104
DOI
10.1016/j.bbrc.2005.05.139
language
English
LU publication?
yes
id
eb056506-9840-4bce-9b89-ed0a9b3a2c0b (old id 233179)
date added to LUP
2007-08-07 09:15:07
date last changed
2017-04-09 04:23:45
@article{eb056506-9840-4bce-9b89-ed0a9b3a2c0b,
  abstract     = {P-Microseminoprotein (MSP) and cysteine-rich secretory protein 3 (CRISP-3) are abundant constituents of human seminal plasma. Immunoprecipitation and gel filtration of seminal plasma proteins combined with examination of the proteins in their pure form showed that MSP and CRISP-3 form stable, non-covalent complexes. CRISP-3 binds MSP with very high affinity, as evidenced by surface plasmon resonance. Due to far higher abundance of MSP in prostatic fluid, it manifests large overcapacity for CRISP-3 binding. Structural similarity with an MSP-binding protein from blood plasma suggests that CRISP-3 binds MSP through its ami-terminal SCP-domain.},
  author       = {Udby, L and Lundwall, Åke and Johnsen, A H and Fernlund, Per and Valtonen-André, Camilla and Blom, Anna and Lilja, Hans and Borregaard, N and Kieldsen, L and Bjartell, Anders},
  issn         = {1090-2104},
  keyword      = {mass,spectrometry,surface plasmon resonance,SCP-domain,protein complex,prostate cancer,seminal plasma,PSP94,cysteine-rich secretory protein,beta-microseminoprotein},
  language     = {eng},
  number       = {2},
  pages        = {555--561},
  publisher    = {Elsevier},
  series       = {Biochemical and Biophysical Research Communications},
  title        = {beta-Microseminoprotein binds CRISP-3 in human seminal plasma},
  url          = {http://dx.doi.org/10.1016/j.bbrc.2005.05.139},
  volume       = {333},
  year         = {2005},
}