Cathelicidin

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Cathelicidin antimicrobial peptide
Identifiers
Symbol(s) CAMP; CAP18; FALL-39; FALL39; HSD26; LL37
External IDs OMIM: 600474 MGI: 108443 HomoloGene: 3206
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 820 12796
Ensembl ENSG00000164047 ENSMUSG00000038357
Uniprot P49913 Q0VB78
Refseq NM_004345 (mRNA)
NP_004336 (protein)		 NM_009921 (mRNA)
NP_034051 (protein)
Location Chr 3: 48.24 - 48.24 Mb Chr 9: 109.7 - 109.71 Mb
Pubmed search [1] [2]

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. Cathelicidins were originally found in neutrophils but have since been found in many other cells including epithelial cells and macrophages activated by bacteria, viruses, fungi, or the hormone 1,25-D.[1] The cathelicidin family shares primary sequence homology with the cathepsin family of cysteine proteinase inhibitors, although amino acid residues thought to be important in such protease inhibition are usually lacking. Cathelicidins serve a critical role in mammalian innate immune defense against invasive bacterial infection. [2]

Richard L. Gallo and colleagues recently noticed that patients with rosacea had elevated levels of cathelicidin and elevated levels of stratum corneum tryptic enzymes (SCTEs). Antibiotics have been used in the past to treat rosacea, but antibiotics may only work because they inhibit some SCTEs.[3]

Cathelicidin antimicrobial protein is an antimicrobial protein found in specific granules of polymorphonuclear leukocytes (PMNs).[supplied by OMIM][4]

[edit] See also

[edit] References

  1. ^ Liu, Philip T., et al. Toll-like receptor triggering of a vitamin D-mediated human antimicrobial response. Science (March 24, 2006) 311, 1770-1773. - http://www.sciencemag.org/cgi/content/abstract/311/5768/1770.
  2. ^ Nizet, V. et al. Innate antimicrobial peptide protects the skin from invasive bacterial infection. Nature 2001 Nov 22 44(6862):454-7.
  3. ^ August 5, 2007 issue of Nature Medicine.
  4. ^ Entrez Gene: CAMP cathelicidin antimicrobial peptide.

[edit] Further reading

  • Chromek, M., et al. The antimicrobial cathelicidin protects the urinary tract against invasive bacterial infection. Nature Medicine (June 2006) 12, 636-641. - http://dx.doi.org/10.1038/nm1407.
  • Gombart, A.F., et al. Human cathelicidin antimicrobial peptide (CAMP) gene is a direct target of the vitamin D receptor and is strongly upregulated in myeloid cells by 1,25-dihydroxyvitamin D3. FASEB Journal (July 2005) 19, 1067-1077. - http://www.fasebj.org/cgi/content/full/19/9/1067.
  • López-García, B., et al. Expression and potential function of cathelicidin antimicrobial peptides in dermatophytosis and tinea versicolor. Journal of Antimicrobial Chemotherapy (May 2006) 57, 877-882. - http://dx.doi.org/10.1093/jac/dkl078.
  • Lehrer RI, Ganz T (2002). "Cathelicidins: a family of endogenous antimicrobial peptides.". Curr. Opin. Hematol. 9 (1): 18–22. PMID 11753073. 
  • Niyonsaba F, Hirata M, Ogawa H, Nagaoka I (2003). "Epithelial cell-derived antibacterial peptides human beta-defensins and cathelicidin: multifunctional activities on mast cells.". Current drug targets. Inflammation and allergy 2 (3): 224–31. PMID 14561157. 
  • van Wetering S, Tjabringa GS, Hiemstra PS (2005). "Interactions between neutrophil-derived antimicrobial peptides and airway epithelial cells.". J. Leukoc. Biol. 77 (4): 444–50. doi:10.1189/jlb.0604367. PMID 15591123. 
  • Agerberth B, Gunne H, Odeberg J, et al. (1995). "FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis.". Proc. Natl. Acad. Sci. U.S.A. 92 (1): 195–9. PMID 7529412. 
  • Cowland JB, Johnsen AH, Borregaard N (1995). "hCAP-18, a cathelin/pro-bactenecin-like protein of human neutrophil specific granules.". FEBS Lett. 368 (1): 173–6. PMID 7615076. 
  • Gudmundsson GH, Magnusson KP, Chowdhary BP, et al. (1995). "Structure of the gene for porcine peptide antibiotic PR-39, a cathelin gene family member: comparative mapping of the locus for the human peptide antibiotic FALL-39.". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7085–9. PMID 7624374. 
  • Larrick JW, Hirata M, Balint RF, et al. (1995). "Human CAP18: a novel antimicrobial lipopolysaccharide-binding protein.". Infect. Immun. 63 (4): 1291–7. PMID 7890387. 
  • Gudmundsson GH, Agerberth B, Odeberg J, et al. (1996). "The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes.". Eur. J. Biochem. 238 (2): 325–32. PMID 8681941. 
  • Larrick JW, Lee J, Ma S, et al. (1997). "Structural, functional analysis and localization of the human CAP18 gene.". FEBS Lett. 398 (1): 74–80. PMID 8946956. 
  • Frohm M, Agerberth B, Ahangari G, et al. (1997). "The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders.". J. Biol. Chem. 272 (24): 15258–63. PMID 9182550. 
  • Bals R, Wang X, Zasloff M, Wilson JM (1998). "The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface.". Proc. Natl. Acad. Sci. U.S.A. 95 (16): 9541–6. PMID 9689116. 
  • Frohm Nilsson M, Sandstedt B, Sørensen O, et al. (1999). "The human cationic antimicrobial protein (hCAP18), a peptide antibiotic, is widely expressed in human squamous epithelia and colocalizes with interleukin-6.". Infect. Immun. 67 (5): 2561–6. PMID 10225921. 
  • Malm J, Sørensen O, Persson T, et al. (2000). "The human cationic antimicrobial protein (hCAP-18) is expressed in the epithelium of human epididymis, is present in seminal plasma at high concentrations, and is attached to spermatozoa.". Infect. Immun. 68 (7): 4297–302. PMID 10858248. 
  • De Yang , Chen Q, Schmidt AP, et al. (2000). "LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells.". J. Exp. Med. 192 (7): 1069–74. PMID 11015447. 
  • Agerberth B, Charo J, Werr J, et al. (2000). "The human antimicrobial and chemotactic peptides LL-37 and alpha-defensins are expressed by specific lymphocyte and monocyte populations.". Blood 96 (9): 3086–93. PMID 11049988. 
  • Bals R, Lang C, Weiner DJ, et al. (2001). "Rhesus monkey (Macaca mulatta) mucosal antimicrobial peptides are close homologues of human molecules.". Clin. Diagn. Lab. Immunol. 8 (2): 370–5. doi:10.1128/CDLI.8.2.370-375.2001. PMID 11238224. 
  • Sørensen OE, Follin P, Johnsen AH, et al. (2001). "Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3.". Blood 97 (12): 3951–9. PMID 11389039. 
  • Nagaoka I, Hirota S, Niyonsaba F, et al. (2001). "Cathelicidin family of antibacterial peptides CAP18 and CAP11 inhibit the expression of TNF-alpha by blocking the binding of LPS to CD14(+) cells.". J. Immunol. 167 (6): 3329–38. PMID 11544322. 
  • Hase K, Eckmann L, Leopard JD, et al. (2002). "Cell differentiation is a key determinant of cathelicidin LL-37/human cationic antimicrobial protein 18 expression by human colon epithelium.". Infect. Immun. 70 (2): 953–63. PMID 11796631. 
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