Human cathelicidin LL-37 increases vascular permeability in the skin via mast cell activation, and phosphorylates MAP kinases p38 and ERK in mast cells
X Chen, F Niyonsaba, H Ushio, I Nagaoka… - Journal of …, 2006 - jdsjournal.com
Human tissues express only one member of cathelicidins, which are a family of antimicrobial
peptides characterized by a highly conserved N-terminal cathelin domain and a C-terminal
cationic antimicrobial domain. This unique human cathelicidin named LL-37 is liberated
from human cationic antibacterial protein of 18 kDa (hCAP18) after cleavage by elastase or
proteinase 3 (reviewed in Ref.[1]). LL-37 was first identified in neutrophils, and later found in
epithelial cells, keratinocytes, lymphocytes, monocytes, and mast cells (reviewed in Ref.[1]) …
peptides characterized by a highly conserved N-terminal cathelin domain and a C-terminal
cationic antimicrobial domain. This unique human cathelicidin named LL-37 is liberated
from human cationic antibacterial protein of 18 kDa (hCAP18) after cleavage by elastase or
proteinase 3 (reviewed in Ref.[1]). LL-37 was first identified in neutrophils, and later found in
epithelial cells, keratinocytes, lymphocytes, monocytes, and mast cells (reviewed in Ref.[1]) …
