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Isolation of human cationic antimicrobial protein-18 from seminal plasma and its association with prostasomes.

Andersson, E. ; Sørensen, O.E. LU ; Frohm, Birgitta LU ; Borregaard, N. ; Egesten, Arne LU and Malm, Johan LU (2002) In Human Reproduction 17(10). p.34-2529
Abstract
BACKGROUND: Cathelicidins are a group of antibiotic peptides with broad antimicrobial activity. They are considered to be an essential part of the innate immune system. The only known human cathelicidin is the human cationic antimicrobial protein (hCAP-18), from which the antimicrobial peptide LL-37 is released. METHODS AND RESULTS: In the present study, we purified hCAP-18 from seminal plasma and confirmed its identity by N-terminal amino acid sequencing. Gel filtration of seminal plasma showed the presence of hCAP-18 in both a low and a high molecular weight peak. Fractions corresponding to the high molecular form of hCAP-18 also contained dipeptidyl peptidase IV (CD26), a prostasome marker. This finding suggested that hCAP-18 found in... (More)
BACKGROUND: Cathelicidins are a group of antibiotic peptides with broad antimicrobial activity. They are considered to be an essential part of the innate immune system. The only known human cathelicidin is the human cationic antimicrobial protein (hCAP-18), from which the antimicrobial peptide LL-37 is released. METHODS AND RESULTS: In the present study, we purified hCAP-18 from seminal plasma and confirmed its identity by N-terminal amino acid sequencing. Gel filtration of seminal plasma showed the presence of hCAP-18 in both a low and a high molecular weight peak. Fractions corresponding to the high molecular form of hCAP-18 also contained dipeptidyl peptidase IV (CD26), a prostasome marker. This finding suggested that hCAP-18 found in fractions corresponding to high molecular weight molecules, is prostasome-associated. Flow cytometry confirmed the association of hCAP-18 with prostasomes and indicated that the molecule is surface bound. Western blot showed the presence of intact hCAP-18 in sperm, prostasomes and ultracentrifuged seminal plasma. CONCLUSIONS: These findings suggest that hCAP-18 may have an important role in antimicrobial defence during human reproduction. The binding of hCAP-18 to prostasomes indicates that protasomes can serve as a reservoir of this precursor of the antibiotic peptide LL-37. (Less)
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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Antimicrobial Cationic Peptides/chemistry, Blotting, Western, Cathelicidins, Cell Membrane/chemistry, Chromatography, Gel, Dipeptidyl Peptidase 4/analysis, Epithelial Cells/chemistry, Flow Cytometry, Humans, Male, Molecular Weight, Prostate/ultrastructure, Semen/chemistry, Sequence Analysis, Protein, Spermatozoa/chemistry, Ultracentrifugation
in
Human Reproduction
volume
17
issue
10
pages
6 pages
publisher
Oxford University Press
external identifiers
  • wos:000179726200007
  • pmid:12351523
  • scopus:0036796148
  • pmid:12351523
ISSN
0268-1161
DOI
10.1093/humrep/17.10.2529
language
English
LU publication?
yes
id
9421c0bf-5fe2-488e-a103-8746d11797f4 (old id 110154)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12351523&dopt=Abstract
date added to LUP
2016-04-01 11:58:02
date last changed
2022-01-26 20:54:58
@article{9421c0bf-5fe2-488e-a103-8746d11797f4,
  abstract     = {{BACKGROUND: Cathelicidins are a group of antibiotic peptides with broad antimicrobial activity. They are considered to be an essential part of the innate immune system. The only known human cathelicidin is the human cationic antimicrobial protein (hCAP-18), from which the antimicrobial peptide LL-37 is released. METHODS AND RESULTS: In the present study, we purified hCAP-18 from seminal plasma and confirmed its identity by N-terminal amino acid sequencing. Gel filtration of seminal plasma showed the presence of hCAP-18 in both a low and a high molecular weight peak. Fractions corresponding to the high molecular form of hCAP-18 also contained dipeptidyl peptidase IV (CD26), a prostasome marker. This finding suggested that hCAP-18 found in fractions corresponding to high molecular weight molecules, is prostasome-associated. Flow cytometry confirmed the association of hCAP-18 with prostasomes and indicated that the molecule is surface bound. Western blot showed the presence of intact hCAP-18 in sperm, prostasomes and ultracentrifuged seminal plasma. CONCLUSIONS: These findings suggest that hCAP-18 may have an important role in antimicrobial defence during human reproduction. The binding of hCAP-18 to prostasomes indicates that protasomes can serve as a reservoir of this precursor of the antibiotic peptide LL-37.}},
  author       = {{Andersson, E. and Sørensen, O.E. and Frohm, Birgitta and Borregaard, N. and Egesten, Arne and Malm, Johan}},
  issn         = {{0268-1161}},
  keywords     = {{Antimicrobial Cationic Peptides/chemistry; Blotting, Western; Cathelicidins; Cell Membrane/chemistry; Chromatography, Gel; Dipeptidyl Peptidase 4/analysis; Epithelial Cells/chemistry; Flow Cytometry; Humans; Male; Molecular Weight; Prostate/ultrastructure; Semen/chemistry; Sequence Analysis, Protein; Spermatozoa/chemistry; Ultracentrifugation}},
  language     = {{eng}},
  number       = {{10}},
  pages        = {{34--2529}},
  publisher    = {{Oxford University Press}},
  series       = {{Human Reproduction}},
  title        = {{Isolation of human cationic antimicrobial protein-18 from seminal plasma and its association with prostasomes.}},
  url          = {{http://dx.doi.org/10.1093/humrep/17.10.2529}},
  doi          = {{10.1093/humrep/17.10.2529}},
  volume       = {{17}},
  year         = {{2002}},
}