LL37

CAMP
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4EYC, 2FBS, 2FBU, 2FCG, 2K6O, 2LMF
Identifiers
Aliases	CAMP, CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, cathelicidin antimicrobial peptide
External IDs	OMIM: 600474 MGI: 108443 HomoloGene: 110678 GeneCards: CAMP
Gene location (Human)
Chr.	Chromosome 3 (human)[1]
End	48,225,491 bp[1]
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)[2]
End	109,849,617 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• protein binding;
Cellular component	• extracellular region; • specific granule; • intracellular; • extracellular exosome; • extracellular space; • specific granule lumen; • tertiary granule lumen;
Biological process	• positive regulation of interleukin-8 secretion; • defense response; • negative regulation of growth of symbiont on or near host surface; • innate immune response in mucosa; • innate immune response; • killing by host of symbiont cells; • chronic inflammatory response; • defense response to bacterium; • antimicrobial humoral response; • neutrophil degranulation; • antimicrobial humoral immune response mediated by antimicrobial peptide; • cytolysis by host of symbiont cells;
	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

LL-37 (or CAP-18 for cathelicidin antimicrobial peptide, 18 kDa) is a gene encoding for the only member of the human cathelicidin family. Cathelicidin-related antimicrobial peptides are a family of polypeptides found in lysosomes of macrophages and polymorphonuclear leukocytes (PMNs), and keratinocytes.^[5] Cathelicidins serve a critical role in mammalian innate immune defense against invasive bacterial infection.^[6]

Clinical significance

NOTE: This article appears to be split into two parts; more on cathelicidin's clinical significance can be found on the cathelicidin page.

Patients with rosacea have elevated levels of cathelicidin. 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.^[7]

Higher plasma levels of LL-37, which are up-regulated by vitamin D, appear to significantly reduce the risk of death from infection in dialysis patients. Patients with a high level of LL-37 were 3.7 times more likely to survive kidney dialysis for a year without a fatal infection.^[8] Vitamin D up-regulates genetic expression of cathelicidin, which exhibits broad-spectrum microbicidal activity against bacteria, fungi, and viruses.^[9]^[10]

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.^[11]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000164047 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000038357 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ "Entrez Gene: CAMP cathelicidin antimicrobial peptide".
↑ Zanetti M (Jan 2004). "Cathelicidins, multifunctional peptides of the innate immunity". Journal of Leukocyte Biology. 75 (1): 39–48. doi:10.1189/jlb.0403147. PMID 12960280.
↑ Reinholz M, Ruzicka T, Schauber J (2012). "Cathelicidin LL-37: an antimicrobial peptide with a role in inflammatory skin disease". Ann Dermatol. 24 (2): 126–35. doi:10.5021/ad.2012.24.2.126. PMC 3346901. PMID 22577261.
↑ Gombart AF, Bhan I, Borregaard N, Tamez H, Camargo CA, Koeffler HP, Thadhani R (Feb 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. PMID 19133797.
↑ Zasloff M (Jan 2002). "Antimicrobial peptides of multicellular organisms". Nature. 415 (6870): 389–95. doi:10.1038/415389a. PMID 11807545.
↑ Kamen DL, Tangpricha V (May 2010). "Vitamin D and molecular actions on the immune system: modulation of innate and autoimmunity". Journal of Molecular Medicine (Berlin, Germany). 88 (5): 441–50. doi:10.1007/s00109-010-0590-9. PMC 2861286. PMID 20119827.
↑ 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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000164047 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000038357 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[5] "Entrez Gene: CAMP cathelicidin antimicrobial peptide".

[Zanetti_2004-6] Zanetti M (Jan 2004). "Cathelicidins, multifunctional peptides of the innate immunity". Journal of Leukocyte Biology. 75 (1): 39–48. doi:10.1189/jlb.0403147. PMID 12960280.

[pmid22577261-7] Reinholz M, Ruzicka T, Schauber J (2012). "Cathelicidin LL-37: an antimicrobial peptide with a role in inflammatory skin disease". Ann Dermatol. 24 (2): 126–35. doi:10.5021/ad.2012.24.2.126. PMC 3346901. PMID 22577261.

[pmid19133797-8] Gombart AF, Bhan I, Borregaard N, Tamez H, Camargo CA, Koeffler HP, Thadhani R (Feb 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. PMID 19133797.

[pmid11807545-9] Zasloff M (Jan 2002). "Antimicrobial peptides of multicellular organisms". Nature. 415 (6870): 389–95. doi:10.1038/415389a. PMID 11807545.

[pmid20119827-10] Kamen DL, Tangpricha V (May 2010). "Vitamin D and molecular actions on the immune system: modulation of innate and autoimmunity". Journal of Molecular Medicine (Berlin, Germany). 88 (5): 441–50. doi:10.1007/s00109-010-0590-9. PMC 2861286. PMID 20119827.

[11] 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.

LL37

Clinical significance

See also

References