Endogenous intracellular cathelicidin enhances TLR9 activation in dendritic cells and macrophages.

ABSTRACT: Cathelicidins are a gene family best known for their antimicrobial action, but the diverse mature peptides they encode also have other host defense functions. The human cathelicidin peptide LL-37 enhances recognition of nucleic acids, an action whose significance is seen in human diseases such as psoriasis where it is associated with increased type 1 IFN production. This function has been attributed to the extracellular action of the peptide to facilitate uptake of nucleic acids. In this study, we demonstrate that the murine mature cathelicidin peptide (CRAMP), encoded by the mouse gene (Camp), is functionally distinct from the human mature peptide (LL-37), as it does not facilitate CpG entry. However, mouse cathelicidin does influence recognition of CpG as bone marrow-derived dendritic ce

SUBMITTER: Nakagawa Y 

PROVIDER: S-EPMC4297737 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature