Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 493, Issue 1, Pages 71-76Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2017.09.072
Keywords
Endothelium; Antimicrobial peptide (AMP); Cathelicidin; Innate immunity; Host defence peptide; ApoA-I
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Funding
- foundation of Gyllenstiernska Krapperupsstiftelsen
- foundation of Sigurd och Elsa Goljes Minne
- Royal Physiographic Society in Lund
- Swedish Research Council [K2014-54X-22426-01-3]
- Blanceflor Boncompagni Ludovisi
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The human cathelicidin peptide LL-37 has antimicrobial and anti-biofilm functions, but LL-37 may also damage the host by triggering inflammation and exerting a cytotoxic effect, thereby reducing host cell, viability. Human plasma mitigates LL-37-induced host cell cytotoxicity but the underlying mechanisms' are not completely understood. Apolipoprotein A-I (ApoA-I) is a plasma protein endowed with athero-protective effects. Here, we investigate the interaction between ApoA-I and LL-37 by biochemical techniques, and furthermore assess if ApoA-I protects against LL-37-evoked cytotoxicity in human umbilical vein endothelial cells (HUVEC). Our results demonstrated that ApoA-I effectively binds LL-37. The binding of ApoA-I to LL-37 resulted in a structural rearrangement of the protein, but this interaction did not cause lower ApoA-I stability. Recombinant ApoA-I protected against LL-37-induced cytotoxicity in HUVEC and endogenous ApoA-I knockdown in HepG2 cells made the cells more sensitive to LL-37-evoked cytotoxicity. We conclude that ApoA-I physically interacts with LL-37 and antagonizes LL-37-induced down-regulation of endothelial cell viability suggesting that this mechanism counteracts endothelial cell dysfunction. (c) 2017 Elsevier Inc. All rights reserved.
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