‹ Back
LL-37, Cathelicidin
How it works
LL-37 breaks microbial membranes, runs on vitamin D, grows new vessels and calls immune cells to the site; open each pathway below.
Sources
Read the original sources
- The human cathelicidin LL-37--A pore-forming antibacterial peptide and host-cell modulator. (Xhindoli · 2016 · Abstract; full methods not assumed · checked 2026-10-13)
- LL-37 membrane and host-cell biology (Abstract · checked 2026-10-13)
- Human cathelicidin antimicrobial peptide (CAMP) gene is a direct target of the vitamin D receptor and is strongly up-regulated in myeloid cells by 1,25-dihydroxyvitamin D3 (Abstract · checked 2026-10-13)
- Toll-like receptor triggering of a vitamin D-mediated human antimicrobial response (Summary · checked 2026-10-13)
- Cathelicidins, vitamin D and tuberculosis (Vestnik of Saint Petersburg University, Medicine, 2013, in Russian) (Abstract · checked 2026-10-13)
- An angiogenic role for the human peptide antibiotic LL-37/hCAP-18 (Abstract · checked 2026-10-13)
- Evidence that cathelicidin peptide LL-37 may act as a functional ligand for CXCR2 on human neutrophils. (Zhang · 2009 · Abstract; full methods not assumed · checked 2026-10-13)