Homo sapiens Gene: CAMP
InnateDB Gene IDBG-32341.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol CAMP
Gene Name cathelicidin antimicrobial peptide
Synonyms CAP-18; CAP18; CRAMP; FALL-39; FALL39; LL37;
Species Homo sapiens
Ensembl Gene ENSG00000164047
Encoded Proteins
cathelicidin antimicrobial peptide
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
InnateDB Annotation
CAMP represents a potent antimicrobial and cell-stimulating agent, most abundantly expressed in peripheral organs such as lung and skin during inflammation.
CAMP, a protein that has direct antimicrobial activity, serves as a mediator of vitamin D3-induced autophagy.
CAMP (LL-37) modulates IFN-gamma responses during both the innate and adaptive phases of immune responses, indicating an immunomodulatory role for this endogenous peptide.
CAMP has both antimicrobial and regenerative capabilities and promotes high glucose-attenuated epithelial wound healing via EGFR transactivation in organ cultured corneas.
CAMP is involved in various aspects of skin biology, including protection against infection, wound healing, and also in psoriasis where it suppresses apoptosis in keratinocytes.
CAMP induces endothelium-dependent relaxation in human omental veins, or vasodilation, mediated via an effect on endothelial ALX.
CAMP enhances delivery of CpG oligodeoxynucleotides to stimulate immune cells and this is independent of its amphipathic structure and its bactericidal property.
CAMP has dual function as an antimicrobial agent against bacterial target cells and a cell penetrating peptide that can deliver nucleic acids into the host cells.
CAMP decreases collagen expression at mRNA and protein levels in human dermal fibroblasts (HDFs) and this inhibition is dependent on phosphorylation of extracellular signal-regulated kinase (ERK). Vitamin C attenuates ERK signalling to inhibit the regulation of collagen production by CAMP in HDFs.
CAMP and human beta-defensins (hBDs) antimicrobial peptides induce the secretion of a pruritogenic cytokine IL-31 by human mast cells.
CAMP (LL37) directs macrophage differentiation toward macrophages with a pro-inflammatory signature and this requires internalization of the peptide, resulting in low production of IL-10 and profound production of IL-12p40 upon LPS stimulation.
CAMP (LL37) converts self-RNA into a trigger of TLR7 and TLR8 in human dendritic cells (DC), leading to production of TNF-alpha and IL6 and the differentiation of myeloid DCs into mature DCs.
CAMP (LL-37) attenuates lethal sepsis/endotoxin shock by suppressing the LPS-induced apoptosis of vascular and hepatic endothelial cells. LL-37 was found to inhibit the binding of LPS to the LPS receptors expressed on the cells.
CAMP (LL37) is found in high concentrations within neutrophil extracellular traps (NETs). CAMP is a neutrophil protein that facilitates the uptake and recognition of mammalian DNA by plasmacytoid dendritic cells, and may play a role in Systemic Lupus Erthermatosus autoimmunity.
CAMP (LL-37) dramatically reduced TNFA and nitric oxide levels produced by LPS and IFNG-polarized M1 macrophages, in addition LL-37-treated M1 macrophages were more efficient at suppressing tumour growth in vitro. This demonstrates the selective ability of LL-37 to decrease production of LPS-induced pro-inflammatory cytokines in macrophages, while leaving other crucial anti-inflammatory M1 and M2 macrophage functions unaltered.
CAMP (LL-37), at sufficiently low concentrations, is able to reduce fungal infectivity by inhibiting C. albicans adhesion to plastic surfaces, oral epidermoid cells, and the urinary bladders of female mice. The inhibitory effects of LL-37 on cell adhesion and aggregation were mediated by its preferential binding to mannan and chitin in the fungal cell wall.
CAMP (LL-37) translocates across the E. coli outer membrane and halts bacterial growth by interfering cell wall biogenesis.
CAMP (LL-37) confers protective immunity against psoriasis by neutralizing cytosolic DNA in keratinocytes and blocking the formation of AIM2 inflammasomes.
CAMP protects against colitis induction in mice. The increased expression of CAMP in monocytes involves the activation of TLR9/ERK signalling pathway by bacterial DNA. (Demonstrated in mouse)
CAMP expression is induced upon endoplasmic reticulum stress via NF-kB-C/EBP-alpha activation.
LL-37 (CAMP) reduces influenza A viral load and disease severity in mice.
CAMP (LL-37) is downregulated during septic shock.
(S)-methyl 2-(hexanamide)-3-(4-hydroxyphenyl) propanoate (MHP) activates SPHK1 to stimulate CAMP production and enhance epidermal antimicrobial defence.
Cleavage of CAMP by cathepsins CTSS and CTSK impairs its antimicrobial activity against Pseudomonas aeruginosa and Staphylococcus aureus.
Carbamylation of CAMP affects its bactericidal, cytotoxic and immunomodulatory function.
CAMP modulates the response of macrophages during mycobacterial infection controlling the expression of pro-inflammatory and anti-inflammatory cytokines.
Entrez Gene
Summary This gene encodes a member of an antimicrobial peptide family, characterized by a highly conserved N-terminal signal peptide containing a cathelin domain and a structurally variable cationic antimicrobial peptide, which is produced by extracellular proteolysis from the C-terminus. The encoded protein has several functions in addition to antimicrobial activity, including cell chemotaxis, immune mediator induction and inflammatory response regulation. [provided by RefSeq, Aug 2011]
This gene encodes a member of an antimicrobial peptide family, characterized by a highly conserved N-terminal signal peptide containing a cathelin domain and a structurally variable cationic antimicrobial peptide, which is produced by extracellular proteolysis from the C-terminus. In addition to its antibacterial, antifungal, and antiviral activities, the encoded protein functions in cell chemotaxis, immune mediator induction, and inflammatory response regulation. [provided by RefSeq, Sep 2014]
Gene Information
Type Protein coding
Genomic Location Chromosome 3:48223347-48225491
Strand Forward strand
Band p21.31
ENST00000296435 ENSP00000296435
Number of Interactions This gene and/or its encoded proteins are associated with 20 experimentally validated interaction(s) in this database.
Experimentally validated
Total 20 [view]
Protein-Protein 15 [view]
Protein-DNA 5 [view]
Protein-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0005515 protein binding
Biological Process
GO:0001934 positive regulation of protein phosphorylation
GO:0002227 innate immune response in mucosa
GO:0006952 defense response
GO:0008284 positive regulation of cell proliferation
GO:0019731 antibacterial humoral response
GO:0042742 defense response to bacterium
GO:0044130 negative regulation of growth of symbiont in host
GO:0044140 negative regulation of growth of symbiont on or near host surface
GO:0045087 innate immune response (InnateDB)
GO:0045766 positive regulation of angiogenesis
GO:0050829 defense response to Gram-negative bacterium
GO:0050830 defense response to Gram-positive bacterium
GO:0051701 interaction with host
GO:0051873 killing by host of symbiont cells
GO:0071222 cellular response to lipopolysaccharide
GO:0071224 cellular response to peptidoglycan
GO:0071347 cellular response to interleukin-1
GO:0071354 cellular response to interleukin-6
GO:0071356 cellular response to tumor necrosis factor
GO:0090382 phagosome maturation
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005618 cell wall
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0042581 specific granule
GO:0042995 cell projection
GO:0070062 extracellular vesicular exosome
No orthologs found for this gene
Phagosomal maturation (early endosomal stage) pathway
Latent infection of Homo sapiens with Mycobacterium tuberculosis pathway
Disease pathway
Salivary secretion pathway
UniProt Splice Variant
Entrez Gene
RefSeq NM_004345
HPRD 02722
RNA Seq Atlas