Molecular mechanisms of LL-37-induced receptor activation: An overview
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- 作者：Eddy-Tim Verjans ; Eddytim.Verjans@bio.kuleuven.be" class="auth_mail" title="E-mail the corresponding author ; Sven Zels ; Walter Luyten ; Bart Landuyt ; Liliane Schoofs
- 关键词：AMP ; antimicrobial peptide ; APD ; antimicrobial peptide database ; IFN ; interferon ; DC ; dendritic cell ; NK-cells ; natural killer cells ; GPCR ; G protein-coupled receptor ; RTK ; receptor tyrosine kinase ; LGIC ; ligand-gated ion channel ; TLR ; toll-like receptor ; EGFR ; epidermal growth factor receptor ; DNA ; deoxyribonucleic acid ; LPS ; lipopolysaccharide ; GAPDH ; glyceraldehyde-3-phosphate dehydrogenase ; FPR2 ; N-formyl peptide receptor 2 ; LTB4 ; leukotriene B4 ; ROS ; reactive oxygen species ; NET ; neutrophil
- 刊名：Peptides
- 出版年：2016
- 出版时间：November 2016
- 年：2016
- 卷：85
- 期：Complete
- 页码：16-26
- 全文大小：1066 K
文摘
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The human cathelicidin LL-37 is an antimicrobial peptide able to selectively modulate host immune responses.
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LL-37 activates various putative cell surface receptors and/or intracellular targets in a wide variety of cell lines.
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It is unclear how one single ligand can activate multiple structurally unrelated receptors.
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Models include direct and indirect mechanisms of action by which LL-37 modifies the physicochemical state of the membrane.
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Improved knowledge on the interaction mechanism of LL-37 with its putative receptors is imperative.