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The human antibacterial cathelicidin, hCAP-18, is bound to lipoproteins in plasma

Sørensen, O LU ; Bratt, T; Johnsen, A H; Madsen, M T and Borregaard, N (1999) In Journal of Biological Chemistry 274(32). p.51-22445
Abstract

Cathelicidins are a family of antibacterial and lipopolysaccharide-binding proteins. hCAP-18, the only human cathelicidin, is a major protein of the specific granules of human neutrophils. The plasma level of hCAP-18 is >20-fold higher than that of other specific granule proteins relative to their levels within circulating neutrophils. The aim of this study was to elucidate the background for this high plasma level of hCAP-18. Plasma was subjected to molecular sieve chromatography, and hCAP-18 was found in distinct high molecular mass fractions that coeluted with apolipoproteins A-I and B, respectively. The association of hCAP-18 with lipoproteins was validated by the cofractionation of hCAP-18 with lipoproteins using two different... (More)

Cathelicidins are a family of antibacterial and lipopolysaccharide-binding proteins. hCAP-18, the only human cathelicidin, is a major protein of the specific granules of human neutrophils. The plasma level of hCAP-18 is >20-fold higher than that of other specific granule proteins relative to their levels within circulating neutrophils. The aim of this study was to elucidate the background for this high plasma level of hCAP-18. Plasma was subjected to molecular sieve chromatography, and hCAP-18 was found in distinct high molecular mass fractions that coeluted with apolipoproteins A-I and B, respectively. The association of hCAP-18 with lipoproteins was validated by the cofractionation of hCAP-18 with lipoproteins using two different methods for isolation of lipoproteins from plasma. Furthermore, the level of hCAP-18 in delipidated plasma was <1% of that in normal plasma. Immunoprecipitation of very low, low, and high density lipoprotein particles with anti-apolipoprotein antibodies resulted in coprecipitation of hCAP-18. The binding of hCAP-18 to lipoproteins was mediated by the antibacterial C-terminal part of the protein. The binding of hCAP-18 to lipoproteins suggests that lipoproteins may play an important role as a reservoir of this antimicrobial protein.

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publication status
published
keywords
Amino Acid Sequence, Antimicrobial Cationic Peptides, Binding Sites, Blood Bactericidal Activity, Blood Proteins, Carrier Proteins, Cathelicidins, Exocytosis, Humans, Lipoproteins, Lipoproteins, LDL, Lipoproteins, VLDL, Molecular Sequence Data, Neutrophils, Peptide Fragments, Protein Binding, Proteins, Recombinant Proteins, Journal Article, Research Support, Non-U.S. Gov't
in
Journal of Biological Chemistry
volume
274
issue
32
pages
51 - 22445
publisher
ASBMB
external identifiers
  • scopus:0033529627
ISSN
0021-9258
DOI
10.1074/jbc.274.32.22445
language
English
LU publication?
no
id
2b172266-2838-4fa6-9a6a-a22290526c64
date added to LUP
2018-03-07 13:55:40
date last changed
2018-05-29 11:29:57
@article{2b172266-2838-4fa6-9a6a-a22290526c64,
  abstract     = {<p>Cathelicidins are a family of antibacterial and lipopolysaccharide-binding proteins. hCAP-18, the only human cathelicidin, is a major protein of the specific granules of human neutrophils. The plasma level of hCAP-18 is &gt;20-fold higher than that of other specific granule proteins relative to their levels within circulating neutrophils. The aim of this study was to elucidate the background for this high plasma level of hCAP-18. Plasma was subjected to molecular sieve chromatography, and hCAP-18 was found in distinct high molecular mass fractions that coeluted with apolipoproteins A-I and B, respectively. The association of hCAP-18 with lipoproteins was validated by the cofractionation of hCAP-18 with lipoproteins using two different methods for isolation of lipoproteins from plasma. Furthermore, the level of hCAP-18 in delipidated plasma was &lt;1% of that in normal plasma. Immunoprecipitation of very low, low, and high density lipoprotein particles with anti-apolipoprotein antibodies resulted in coprecipitation of hCAP-18. The binding of hCAP-18 to lipoproteins was mediated by the antibacterial C-terminal part of the protein. The binding of hCAP-18 to lipoproteins suggests that lipoproteins may play an important role as a reservoir of this antimicrobial protein.</p>},
  author       = {Sørensen, O and Bratt, T and Johnsen, A H and Madsen, M T and Borregaard, N},
  issn         = {0021-9258},
  keyword      = {Amino Acid Sequence,Antimicrobial Cationic Peptides,Binding Sites,Blood Bactericidal Activity,Blood Proteins,Carrier Proteins,Cathelicidins,Exocytosis,Humans,Lipoproteins,Lipoproteins, LDL,Lipoproteins, VLDL,Molecular Sequence Data,Neutrophils,Peptide Fragments,Protein Binding,Proteins,Recombinant Proteins,Journal Article,Research Support, Non-U.S. Gov't},
  language     = {eng},
  number       = {32},
  pages        = {51--22445},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {The human antibacterial cathelicidin, hCAP-18, is bound to lipoproteins in plasma},
  url          = {http://dx.doi.org/10.1074/jbc.274.32.22445},
  volume       = {274},
  year         = {1999},
}