Semenogelin, the predominant protein in human semen. Primary structure and identification of closely related proteins in the male accessory sex glands and on the spermatozoa
Lilja, Hans LU
; Abrahamsson, Per-Anders
LU
and Lundwall, Åke
LU
(1989)
In Journal of Biological Chemistry
264(3).
p.900-1894
- Abstract
- The predominant protein in human semen, semenogelin, was characterized by lambda gt11 clones isolated from a seminal vesicular cDNA library. One clone, carrying a cDNA insert of 1606 nucleotides and a polyadenylated tail, coded for the entire semenogelin precursor. An open reading frame of 1386 nucleotides encodes a signal peptide and the mature protein of 439 amino acid residues, in which residues 85-136 are identical with a previously characterized semenogelin fragment. The polypeptide chain displays a most conspicuous region of internal sequence homology where 46 of the 58 amino acid residues at positions 259-316 are repeated at positions 319-376. An abundant seminal vesicular transcript of 1.8 kilobases (kb) codes for semenogelin. Two... (More)
- The predominant protein in human semen, semenogelin, was characterized by lambda gt11 clones isolated from a seminal vesicular cDNA library. One clone, carrying a cDNA insert of 1606 nucleotides and a polyadenylated tail, coded for the entire semenogelin precursor. An open reading frame of 1386 nucleotides encodes a signal peptide and the mature protein of 439 amino acid residues, in which residues 85-136 are identical with a previously characterized semenogelin fragment. The polypeptide chain displays a most conspicuous region of internal sequence homology where 46 of the 58 amino acid residues at positions 259-316 are repeated at positions 319-376. An abundant seminal vesicular transcript of 1.8 kilobases (kb) codes for semenogelin. Two additional transcripts, one seminal vesicular 2.2-kb species and one epididymal 2.0-kb species, code for related proteins that have a close structural relationship as well as antigenic epitopes in common with semenogelin. Semenogelin and the semenogelin-related proteins are the major proteins involved in the gelatinous entrapment of ejaculated spermatozoa. Antigenic epitopes common to these proteins are localized to the parts of the spermatozoa involved in locomotion. The spermatozoa become progressively motile as the gel-forming proteins are fragmented by the kallikrein-like protease, prostate-specific antigen, and the gel dissolves. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3965173
- author
- Lilja, Hans
LU
; Abrahamsson, Per-Anders
LU
and Lundwall, Åke
LU
- organization
- publishing date
- 1989
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Molecular Sequence Data, Male, Immunohistochemistry, Humans, Gonadal Steroid Hormones/*analysis/genetics, Male/*analysis, Genitalia, DNA/analysis, Amino Acid Sequence, Base Sequence, Research Support, Non-U.S. Gov't, Semen/*analysis, *Seminal Vesicle Secretory Proteins, Spermatozoa/*analysis
- in
- Journal of Biological Chemistry
- volume
- 264
- issue
- 3
- pages
- 900 - 1894
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- scopus:0024562089
- ISSN
- 0021-9258
- language
- English
- LU publication?
- yes
- additional info
- 3
- id
- 651031fa-943c-4866-804d-2cc47d190a2d (old id 3965173)
- alternative location
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2912989
- date added to LUP
- 2016-04-04 13:24:11
- date last changed
- 2021-09-19 05:18:03
@article{651031fa-943c-4866-804d-2cc47d190a2d,
abstract = {{The predominant protein in human semen, semenogelin, was characterized by lambda gt11 clones isolated from a seminal vesicular cDNA library. One clone, carrying a cDNA insert of 1606 nucleotides and a polyadenylated tail, coded for the entire semenogelin precursor. An open reading frame of 1386 nucleotides encodes a signal peptide and the mature protein of 439 amino acid residues, in which residues 85-136 are identical with a previously characterized semenogelin fragment. The polypeptide chain displays a most conspicuous region of internal sequence homology where 46 of the 58 amino acid residues at positions 259-316 are repeated at positions 319-376. An abundant seminal vesicular transcript of 1.8 kilobases (kb) codes for semenogelin. Two additional transcripts, one seminal vesicular 2.2-kb species and one epididymal 2.0-kb species, code for related proteins that have a close structural relationship as well as antigenic epitopes in common with semenogelin. Semenogelin and the semenogelin-related proteins are the major proteins involved in the gelatinous entrapment of ejaculated spermatozoa. Antigenic epitopes common to these proteins are localized to the parts of the spermatozoa involved in locomotion. The spermatozoa become progressively motile as the gel-forming proteins are fragmented by the kallikrein-like protease, prostate-specific antigen, and the gel dissolves.}},
author = {{Lilja, Hans and Abrahamsson, Per-Anders and Lundwall, Åke}},
issn = {{0021-9258}},
keywords = {{Molecular Sequence Data; Male; Immunohistochemistry; Humans; Gonadal Steroid Hormones/*analysis/genetics; Male/*analysis; Genitalia; DNA/analysis; Amino Acid Sequence; Base Sequence; Research Support; Non-U.S. Gov't; Semen/*analysis; *Seminal Vesicle Secretory Proteins; Spermatozoa/*analysis}},
language = {{eng}},
number = {{3}},
pages = {{900--1894}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{Semenogelin, the predominant protein in human semen. Primary structure and identification of closely related proteins in the male accessory sex glands and on the spermatozoa}},
url = {{http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2912989}},
volume = {{264}},
year = {{1989}},
}