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Chemical characterization of the predominant proteins secreted by mouse seminal vesicles

Lundwall, Åke LU ; Peter, A. ; Lövgren, J. ; Lilja, Hans LU orcid and Malm, J. (1997) In Eur J Biochem 249(1). p.39-44
Abstract
Mouse seminal vesicles secrete four major protein components with estimated molecular masses of 95, 38, 17, and 16 kDa. Amino acid sequencing revealed that the 95-kDa component represents a protein with an unknown structure, while the 38-kDa component was identified as semenoclotin, the 17-kDa component as seminal-vesicle-secreted protein IV, and the 16-kDa component as seminal-vesicle-secreted protein V. Semenoclotin and the 95-kDa component were readily cross-linked by transglutaminase, suggesting that the two proteins are involved in the formation of the mouse copulatory plug. Treatment of mouse seminal vesicle fluid with human prostate-specific antigen rapidly degraded semenoclotin, indicating a structural resemblance of this protein... (More)
Mouse seminal vesicles secrete four major protein components with estimated molecular masses of 95, 38, 17, and 16 kDa. Amino acid sequencing revealed that the 95-kDa component represents a protein with an unknown structure, while the 38-kDa component was identified as semenoclotin, the 17-kDa component as seminal-vesicle-secreted protein IV, and the 16-kDa component as seminal-vesicle-secreted protein V. Semenoclotin and the 95-kDa component were readily cross-linked by transglutaminase, suggesting that the two proteins are involved in the formation of the mouse copulatory plug. Treatment of mouse seminal vesicle fluid with human prostate-specific antigen rapidly degraded semenoclotin, indicating a structural resemblance of this protein to human semenogelins, despite the vast difference in primary structure. As previously reported for other seminal-vesicle-secreted proteins, the semenoclotin transcripts are shown to be under androgen control. (Less)
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organization
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Contribution to journal
publication status
published
subject
keywords
RNA, Proteins/*chemistry/genetics/*secretion, Post-Translational, Protein Processing, Molecular Weight, Inbred BALB C, Mice, Male, Humans, Gonadal Steroid Hormones/chemistry/genetics, Cross-Linking Reagents, Amino Acid Sequence, Animals, Messenger/genetics/metabolism, Research Support, Non-U.S. Gov't, *Seminal Vesicle Secretory Proteins, Seminal Vesicles/chemistry/drug effects/*secretion, Testosterone/pharmacology, Transglutaminases
in
Eur J Biochem
volume
249
issue
1
pages
39 - 44
publisher
Wiley-Blackwell
external identifiers
  • scopus:0030819922
language
English
LU publication?
yes
additional info
1
id
2fd412b7-59a1-4eda-8896-5f4707fd633e (old id 3965273)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9363751
date added to LUP
2016-04-04 13:59:34
date last changed
2022-01-30 01:18:01
@article{2fd412b7-59a1-4eda-8896-5f4707fd633e,
  abstract     = {{Mouse seminal vesicles secrete four major protein components with estimated molecular masses of 95, 38, 17, and 16 kDa. Amino acid sequencing revealed that the 95-kDa component represents a protein with an unknown structure, while the 38-kDa component was identified as semenoclotin, the 17-kDa component as seminal-vesicle-secreted protein IV, and the 16-kDa component as seminal-vesicle-secreted protein V. Semenoclotin and the 95-kDa component were readily cross-linked by transglutaminase, suggesting that the two proteins are involved in the formation of the mouse copulatory plug. Treatment of mouse seminal vesicle fluid with human prostate-specific antigen rapidly degraded semenoclotin, indicating a structural resemblance of this protein to human semenogelins, despite the vast difference in primary structure. As previously reported for other seminal-vesicle-secreted proteins, the semenoclotin transcripts are shown to be under androgen control.}},
  author       = {{Lundwall, Åke and Peter, A. and Lövgren, J. and Lilja, Hans and Malm, J.}},
  keywords     = {{RNA; Proteins/*chemistry/genetics/*secretion; Post-Translational; Protein Processing; Molecular Weight; Inbred BALB C; Mice; Male; Humans; Gonadal Steroid Hormones/chemistry/genetics; Cross-Linking Reagents; Amino Acid Sequence; Animals; Messenger/genetics/metabolism; Research Support; Non-U.S. Gov't; *Seminal Vesicle Secretory Proteins; Seminal Vesicles/chemistry/drug effects/*secretion; Testosterone/pharmacology; Transglutaminases}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{39--44}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{Eur J Biochem}},
  title        = {{Chemical characterization of the predominant proteins secreted by mouse seminal vesicles}},
  url          = {{http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9363751}},
  volume       = {{249}},
  year         = {{1997}},
}