Preferred Label : cathelicidins;
MeSH definition : Antimicrobial cationic peptides with a highly conserved amino terminal cathelin-like
domain and a more variable carboxy terminal domain. They are initially synthesized
as preproproteins and then cleaved. They are expressed in many tissues of humans and
localized to EPITHELIAL CELLS. They kill nonviral pathogens by forming pores in membranes.;
MeSH synonym : Cathelicidin; Cathelicidin Antimicrobial Peptide;
MeSH hyponym : hCAP 18; Protein, Cathelin-Like; Cathelicidin-1; Antimicrobial Peptide, Cathelin-Related; Peptide, Cathelin-Related Antimicrobial; CAP 18; CAP18 Lipopolysaccharide-Binding Protein; CAP18 Lipopolysaccharide Binding Protein; Lipopolysaccharide-Binding Protein, CAP18; Protein, CAP18 Lipopolysaccharide-Binding; FA-LL-37; FA LL 37; Antimicrobial Peptide LL-37; Antimicrobial Peptide LL 37; LL-37, Antimicrobial Peptide; Peptide LL-37, Antimicrobial; Ropocamptide; LL-37 Antibacterial Peptide; Antibacterial Peptide, LL-37; LL 37 Antibacterial Peptide; Peptide, LL-37 Antibacterial; LL-37 Peptide; LL 37 Peptide; Peptide, LL-37; CAP18; Cathelicidin LL-37; Cathelicidin LL 37; LL-37, Cathelicidin; Antibacterial Peptide LL-37; Antibacterial Peptide LL 37; LL-37, Antibacterial Peptide; Peptide LL-37, Antibacterial; ALL 38 Peptide; Peptide, ALL-38; eCATH 1; eCATH 1 protein, Equus caballus; CATH-1 Protein; CATH 1 Protein; Protein, CATH-1; Myeloid Cathelicidin 1 Protein, Equus caballus;
MeSH Related Number : 143108-26-3;
Is substance : O;
Origin ID : D054804;
UMLS CUI : C1956061;
Allowable qualifiers
Record concept(s)
Related MeSH Supplementary Concept(s)
- Art-175 [MeSH Supplementary Concept]
- D-LL-31 [MeSH Supplementary Concept]
- D-LL-37 [MeSH Supplementary Concept]
Semantic type(s)
Antimicrobial cationic peptides with a highly conserved amino terminal cathelin-like
domain and a more variable carboxy terminal domain. They are initially synthesized
as preproproteins and then cleaved. They are expressed in many tissues of humans and
localized to EPITHELIAL CELLS. They kill nonviral pathogens by forming pores in membranes.