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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 orcid ; Lilja, Hans LU orcid ; 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
; ; ; ; ; ; ; ; and
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
2016-04-01 16:49:49
date last changed
2022-03-15 03:16:56
@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}},
  keywords     = {{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}},
  doi          = {{10.1016/j.bbrc.2005.05.139}},
  volume       = {{333}},
  year         = {{2005}},
}