|Homo sapiens Gene: CAMP|
|Last Modified||2014-10-13 [Report errors or provide feedback]|
|Gene Name||cathelicidin antimicrobial peptide|
|Synonyms||CAP-18; CAP18; CRAMP; FALL-39; FALL39; LL37;|
cathelicidin antimicrobial peptide
|Useful resources||Stemformatics EHFPI ImmGen|
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.
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]
|Genomic Location||Chromosome 3:48223347-48225491|
|Number of Interactions||
This gene and/or its encoded proteins are associated with 20 experimentally validated interaction(s) in this database.
|No orthologs found for this gene|
Phagosomal maturation (early endosomal stage) pathway
Latent infection of Homo sapiens with Mycobacterium tuberculosis pathway
Salivary secretion pathway
|UniProt Splice Variant|
|RNA Seq Atlas|