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Available structures
PDBOrtholog search: PDBe RCSB
AliasesCAMP, IPR001894, CAP-18, CAP18, CRAMP, HSD26, gene FALL39, gene LL37, FALL39, LL37, FALL-39, cathelicidin antimicrobial peptide, Cathelicidins
External IDsOMIM: 600474 MGI: 108443 HomoloGene: 110678 GeneCards: CAMP
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for CAMP
Genomic location for CAMP
Band3p21.31Start48,223,347 bp[1]
End48,225,491 bp[1]
RNA expression pattern
PBB GE CAMP 210244 at fs.png
More reference expression data
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 3: 48.22 – 48.23 Mbn/a
PubMed search[2][3]
View/Edit HumanView/Edit Mouse

Cathelicidin antimicrobial peptides (CAMP) LL-37 and FALL-39 are polypeptides that are primarily stored in the lysosomes of macrophages and polymorphonuclear leukocytes (PMNs); in humans, the CAMP gene encodes the peptide precursor CAP-18, which is cleaved into the active forms LL-37 and FALL-39.[4][5]

Cathelicidins serve a critical role in mammalian innate immune defense against invasive bacterial infection.[6] 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.[6] Members of the cathelicidin family of antimicrobial polypeptides are characterized by a highly conserved region (cathelin domain) and a highly variable cathelicidin peptide domain.[6]

Cathelicidin peptides have been isolated from many different species of mammals. Cathelicidins were originally found in neutrophils, but have since been found in many other cells including epithelial cells and macrophages after activation by bacteria, viruses, fungi, or the hormone 1,25-D, which is the hormonally active form of vitamin D.[7]

Mechanism of antimicrobial activity[edit]

The general rule of the mechanism triggering cathelicidin action, like that of other antimicrobial peptides, involves the disintegration (damaging and puncturing) of cell membranes of organisms toward which the peptide is active.[8] Cathelicidin rapidly destroys the lipoprotein membranes of microbes enveloped in phagosomes after fusion with lysosomes in macrophages.


Cathelicidins range in size from 12 to 80 amino acid residues and have a wide range of structures.[9] Most cathelicidins are linear peptides with 23-37 amino acid residues, and fold into amphipathic α-helices. Additionally cathelicidins may also be small-sized molecules (12-18 residues) with beta-hairpin structures, stabilized by one or two disulphide bonds. Even larger cathelicidin peptides (39-80 amino acid residues) are also present. These larger cathelicidins display repetitive proline motifs forming extended polyproline-type structures.[6]

The cathelicidin family shares primary sequence homology with the cystatin[10] family of cysteine proteinase inhibitors, although amino acid residues thought to be important in such protease inhibition are usually lacking.

Non-human orthologs[edit]

Cathelicidin peptides have been found in humans, monkeys, mice, rats, rabbits, guinea pigs, pandas, pigs, cattle, frogs, sheep, goats, chickens, and horses.

Currently identified cathelicidin peptides include the following:[6]

  • Human: hCAP-18 (cleaved into LL-37 and FALL-39)
  • Rhesus monkey: RL-37
  • Mice:CRAMP-1/2, (Cathelicidin-related Antimicrobial Peptide[11]
  • Rats: rCRAMP
  • Rabbits: CAP-18
  • Guinea pig: CAP-11
  • Pigs: PR-39, Prophenin, PMAP-23,36,37
  • Cattle: BMAP-27,28,34 (Bovine Myeloid Antimicrobial Peptides); Bac5, Bac7
  • Frogs: cathelicidin-AL (found in Amolops loloensis)[12]
  • Chickens: Four cathelicidins, fowlicidins 1,2,3 and cathelicidin Beta-1 [13]
  • Tasmanian Devil: Saha-CATH5 [14]
  • Salmonids: CATH1 and CATH2

Clinical significance[edit]

Patients with rosacea have elevated levels of cathelicidin and elevated levels of stratum corneum tryptic enzymes (SCTEs). Cathelicidin is cleaved into the antimicrobial peptide LL-37 by both kallikrein 5 and kallikrein 7 serine proteases. Excessive production of LL-37 is suspected to be a contributing cause in all subtypes of Rosacea.[15] Antibiotics have been used in the past to treat rosacea, but antibiotics may only work because they inhibit some SCTEs.[16]

Higher plasma levels of human cathelicidin antimicrobial protein (hCAP18) appear to significantly reduce the risk of death from infection in dialysis patients. Patients with a high level of this protein were 3.7 times more likely to survive kidney dialysis for a year without a fatal infection.[17] The production of cathelicidin is up-regulated by Vitamin D.[18][19]

SAAP-148 (a synthetic antimicrobial and antibiofilm peptide) is a modified version of LL-37 that has enhanced antimicrobial activities compared to LL-37. In particular, SAAP-148 was more efficient in killing bacteria under physiological conditions.[20]

LL-37 is thought to play a role in psoriasis pathogenesis (along with other anti-microbial peptides). In psoriasis, damaged keratinocytes release LL-37 which forms complexes with self-genetic material (DNA or RNA) from other cells. These complexes stimulate dendritic cells (a type of antigen presenting cell) which then release interferon α and β which contributes to differentiation of T-cells and continued inflammation.[21] LL-37 has also been found to be a common auto-antigen in psoriasis; T-cells specific to LL-37 were found in the blood and skin in two thirds of patients with moderate to severe psoriasis.[21]

See also[edit]


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000164047 - Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Entrez Gene: CAMP cathelicidin antimicrobial peptide".
  5. ^ UniProt entry: P49913 Retrieved 29 November 2019
  6. ^ a b c d e Zanetti M (January 2004). "Cathelicidins, multifunctional peptides of the innate immunity". Journal of Leukocyte Biology. 75 (1): 39–48. doi:10.1189/jlb.0403147. PMID 12960280. S2CID 14902156.
  7. ^ Liu PT, Stenger S, Li H, Wenzel L, Tan BH, Krutzik SR, Ochoa MT, Schauber J, Wu K, Meinken C, Kamen DL, Wagner M, Bals R, Steinmeyer A, Zügel U, Gallo RL, Eisenberg D, Hewison M, Hollis BW, Adams JS, Bloom BR, Modlin RL (March 2006). "Toll-like receptor triggering of a vitamin D-mediated human antimicrobial response". Science. 311 (5768): 1770–3. Bibcode:2006Sci...311.1770L. doi:10.1126/science.1123933. PMID 16497887. S2CID 52869005.
  8. ^ Kościuczuk EM, Lisowski P, Jarczak J, Strzałkowska N, Jóźwik A, Horbańczuk J, Krzyżewski J, Zwierzchowski L, Bagnicka E (December 2012). "Cathelicidins: family of antimicrobial peptides. A review". Molecular Biology Reports. 39 (12): 10957–70. doi:10.1007/s11033-012-1997-x. PMC 3487008. PMID 23065264.
  9. ^ Gennaro R, Zanetti M (2000). "Structural features and biological activities of the cathelicidin-derived antimicrobial peptides". Biopolymers. 55 (1): 31–49. doi:10.1002/1097-0282(2000)55:1<31::AID-BIP40>3.0.CO;2-9. PMID 10931440.
  10. ^ Zaiou M, Nizet V, Gallo RL (May 2003). "Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence". The Journal of Investigative Dermatology. 120 (5): 810–6. doi:10.1046/j.1523-1747.2003.12132.x. PMID 12713586.
  11. ^ Gallo RL, Kim KJ, Bernfield M, Kozak CA, Zanetti M, Merluzzi L, Gennaro R (May 1997). "Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse". The Journal of Biological Chemistry. 272 (20): 13088–93. doi:10.1074/jbc.272.20.13088. PMID 9148921.
  12. ^ Hao X, Yang H, Wei L, Yang S, Zhu W, Ma D, Yu H, Lai R (August 2012). "Amphibian cathelicidin fills the evolutionary gap of cathelicidin in vertebrate". Amino Acids. 43 (2): 677–85. doi:10.1007/s00726-011-1116-7. PMID 22009138. S2CID 2794908.
  13. ^ Achanta M, Sunkara LT, Dai G, Bommineni YR, Jiang W, Zhang G (May 2012). "Tissue expression and developmental regulation of chicken cathelicidin antimicrobial peptides". Journal of Animal Science and Biotechnology. 3 (1): 15. doi:10.1186/2049-1891-3-15. PMC 3436658. PMID 22958518.
  14. ^ Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K (October 2016). "Cathelicidins in the Tasmanian devil (Sarcophilus harrisii)". Scientific Reports. 6: 35019. Bibcode:2016NatSR...635019P. doi:10.1038/srep35019. PMC 5057115. PMID 27725697.
  15. ^ Reinholz M, Ruzicka T, Schauber J (May 2012). "Cathelicidin LL-37: an antimicrobial peptide with a role in inflammatory skin disease". Annals of Dermatology. 24 (2): 126–35. doi:10.5021/ad.2012.24.2.126. PMC 3346901. PMID 22577261.
  16. ^ Yamasaki K, Di Nardo A, Bardan A, Murakami M, Ohtake T, Coda A, Dorschner RA, Bonnart C, Descargues P, Hovnanian A, Morhenn VB, Gallo RL (August 2007). "Increased serine protease activity and cathelicidin promotes skin inflammation in rosacea". Nature Medicine. 13 (8): 975–80. doi:10.1038/nm1616. PMID 17676051. S2CID 23470611.
  17. ^ Gombart AF, Bhan I, Borregaard N, Tamez H, Camargo CA, Koeffler HP, Thadhani R (February 2009). "Low plasma level of cathelicidin antimicrobial peptide (hCAP18) predicts increased infectious disease mortality in patients undergoing hemodialysis". Clinical Infectious Diseases. 48 (4): 418–24. doi:10.1086/596314. PMC 6944311. PMID 19133797.
  18. ^ Zasloff M (January 2002). "Antimicrobial peptides of multicellular organisms". Nature. 415 (6870): 389–95. Bibcode:2002Natur.415..389Z. doi:10.1038/415389a. PMID 11807545. S2CID 205028607.
  19. ^ Kamen DL, Tangpricha V (May 2010). "Vitamin D and molecular actions on the immune system: modulation of innate and autoimmunity". Journal of Molecular Medicine. 88 (5): 441–50. doi:10.1007/s00109-010-0590-9. PMC 2861286. PMID 20119827.
  20. ^ Breij, Anna de; Riool, Martijn; Cordfunke, Robert A.; Malanovic, Nermina; Boer, Leonie de; Koning, Roman I.; Ravensbergen, Elisabeth; Franken, Marnix; Heijde, Tobias van der (2018-01-10). "The antimicrobial peptide SAAP-148 combats drug-resistant bacteria and biofilms". Science Translational Medicine. 10 (423): eaan4044. doi:10.1126/scitranslmed.aan4044. ISSN 1946-6234. PMID 29321257.
  21. ^ a b Rendon, Adriana; Schäkel, Knut (23 March 2019). "Psoriasis Pathogenesis and Treatment". International Journal of Molecular Sciences. 20 (6): 1475. doi:10.3390/ijms20061475. PMC 6471628. PMID 30909615.

Further reading[edit]

External links[edit]

  • Overview of all the structural information available in the PDB for UniProt: P49913 (Human Cathelicidin) at the PDBe-KB.