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Collagen Synthesis Is Suppressed in Dermal Fibroblasts by the Human Antimicrobial Peptide LL-37

Authors
Park, Hyun JeongCho, Dae HoKim, Hee JungLee, Jun YoungCho, Baik KeeBang, Sa IkSong, Sang YongYamasaki, KenshiDi Nardo, AnnaGallo, Richard L.
Issue Date
Apr-2009
Publisher
NATURE PUBLISHING GROUP
Citation
JOURNAL OF INVESTIGATIVE DERMATOLOGY, v.129, no.4, pp.843 - 850
Journal Title
JOURNAL OF INVESTIGATIVE DERMATOLOGY
Volume
129
Number
4
Start Page
843
End Page
850
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/13789
DOI
10.1038/jid.2008.320
ISSN
0022-202X
Abstract
LL-37 is a human cathelicidin antimicrobial peptide that is released in the skin after injury and acts to defend against infection and modulate the local cellular immune response. We observed in human dermal keloids that fibrosis was inversely related to the expression of cathelicidin and sought to determine how LL-37 influenced expression of types I and III collagen genes in dermal fibroblasts. At nano-molar concentrations, LL-37 inhibited baseline and transforming growth factor-beta-induced collagen expression. At these concentrations, LL-37 also induced phosphorylation of extracellular signal-regulated kinase (ERK) within 30 minutes. Activation of ERK, and the activation of a G-protein-dependent pathway, was essential for inhibition of collagen expression as pertussis toxin or an inhibitor of ERK blocked the inhibitory effects of LL-37. c-Jun N-terminal kinase and p38 mitogen-activated protein kinase inhibitors did not alter the effects of cathelicidin. Silencing of the Ets-1 reversed inhibitory effects of LL-37. Taken together, these findings show that LL-37 can directly act on dermal fibroblasts and may have antifibrotic action during the wound repair process.
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