Cathelicidin antimicrobial peptide

CAMP
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4EYC, 2FBS, 2FBU, 2FCG, 2K6O
Identifiers
Aliases	HGNC:11998 CAMP, IPR001894, CAP-18, CAP18, CRAMP, HSD26, gene FALL39, gene LL37, FALL39, LL37, FALL-39, cathelicidin antimicrobial peptide, Cathelicidins
External IDs	OMIM: 600474; MGI: 108443; HomoloGene: 110678; GeneCards: CAMP; OMA:CAMP - orthologs
Gene location (Human)
Chr.	Chromosome 3 (human)
End	48,225,491 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	109,678,685 bp
RNA expression pattern
	Top expressed in
	trabecular bone; ; bone marrow; ; bone marrow cell; ; tail of epididymis; ; corpus epididymis; ; blood; ; granulocyte; ; testicle; ; monocyte; ; gonad;
	Top expressed in
	granulocyte; ; tibiofemoral joint; ; femur; ; body of femur; ; fetal liver hematopoietic progenitor cell; ; ankle joint; ; vestibular membrane of cochlear duct; ; spleen; ; bone marrow; ; lumbar spinal ganglion;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	lipopolysaccharide binding; protein binding;
Cellular component	extracellular region; specific granule; extracellular exosome; extracellular space; intracellular anatomical structure; specific granule lumen; tertiary granule lumen;
Biological process	defense response; innate immune response in mucosa; innate immune response; killing by host of symbiont cells; chronic inflammatory response; defense response to bacterium; antimicrobial humoral response; antimicrobial humoral immune response mediated by antimicrobial peptide; cytolysis by host of symbiont cells; defense response to Gram-negative bacterium; defense response to Gram-positive bacterium; neutrophil degranulation;
	Sources:Amigo / QuickGO
Orthologs
	820
	12796
	ENSG00000164047
	ENSMUSG00000038357
	P49913
	P51437
	NM_004345
	NM_009921
	NP_004336
	NP_034051
	Wikidata
View/Edit Human	View/Edit Mouse

Cathelicidin antimicrobial peptide (CAMP) is an antimicrobial peptide encoded in the human by the CAMP gene. The active form is LL-37, a 37 amino acid peptide having sequence LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES. In humans, CAMP encodes the peptide precursor CAP-18 (18 kDa), which is processed by proteinase 3-mediated extracellular cleavage into the active form LL-37.

The cathelicidin family includes 30 types of which LL-37 is the only cathelicidin in the human. Cathelicidins are stored in the secretory granules of neutrophils and macrophages and can be released following activation by leukocytes. Cathelicidin peptides are dual-natured molecules called amphiphiles: one end of the molecule is attracted to water and repelled by fats and proteins, and the other end is attracted to fat and proteins and repelled by water. Members of this family react to pathogens by disintegrating, damaging, or puncturing cell membranes.

Cathelicidins thus serve a critical role in mammalian innate immune defense against invasive bacterial infection. The cathelicidin family of peptides are classified as antimicrobial peptides (AMPs). The AMP family also includes the defensins. Whilst the defensins share common structural features, cathelicidin-related peptides are highly heterogeneous. Members of the cathelicidin family of antimicrobial polypeptides are characterized by a highly conserved region (cathelin domain) and a highly variable cathelicidin peptide domain.

Cathelicidin peptides have been isolated from many different species of mammals, including marsupials. Cathelicidins are mostly found in neutrophils, monocytes, mast cells, dendritic cells and macrophages after activation by bacteria, viruses, fungi, parasites or the hormone 1,25-D, which is the hormonally active form of vitamin D. They have been found in some other cells, including epithelial cells and human keratinocytes. Some viruses evolved immunomodulatory mechanisms to avoid cathelicidin exposure by downregulating the cellular vitamin D receptor.