Human Reproduction, Vol. 17, No. 10, 2529-2534,
October 2002
© 2002 European Society of Human Reproduction and Embryology
Isolation of human cationic antimicrobial protein-18 from seminal plasma and its association with prostasomes
1 Department of Laboratory Medicine, Divisions of Clinical Chemistry and 2 Medical Microbiology, Lund University, University Hospital MAS, SE- 205 02 Malmö, Sweden and 3 Granulocyte Research Laboratory, Department of Hematology, University Hospital, DK-2100 Copenhagen, Denmark
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.
Key words: cathelicidin/hCAP-18/LL-37/prostasome/semen
4 To whom correspondence should be addressed. E-mail: johan.malm{at}klkemi.mas.lu.se
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