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{{Infobox_gene}}
{{Infobox_gene}}
'''Cathelicidin'''-related antimicrobial peptides are a family of [[polypeptides]] found in [[lysosomes]] of [[macrophage]]s and [[Granulocyte|polymorphonuclear leukocytes]] (PMNs), and [[Keratinocytes]].<ref>{{cite web | title = Entrez Gene: CAMP cathelicidin antimicrobial peptide| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=820| accessdate = }}</ref> Cathelicidins serve a critical role in mammalian innate immune defense against invasive bacterial infection.<ref name="Zanetti_2004"/> The cathelicidin family of peptides are classified as [[antimicrobial peptide]]s (AMPs). The AMP family also includes the [[defensin]]s. Whilst the defensins share common structural features, cathelicidin-related peptides are highly heterogeneous.<ref name="Zanetti_2004"/>
'''Cathelicidin'''-related antimicrobial peptides are a family of [[polypeptides]] primarily stored in the [[lysosomes]] of [[macrophage]]s and [[Granulocyte|polymorphonuclear leukocytes]] (PMNs).<ref>{{cite web | title = Entrez Gene: CAMP cathelicidin antimicrobial peptide| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=820| accessdate = }}</ref> Cathelicidins serve a critical role in mammalian innate immune defense against invasive bacterial infection.<ref name="Zanetti_2004"/> The cathelicidin family of peptides are classified as [[antimicrobial peptide]]s (AMPs). The AMP family also includes the [[defensin]]s. Whilst the defensins share common structural features, cathelicidin-related peptides are highly heterogeneous.<ref name="Zanetti_2004"/>


Members of the cathelicidin family of antimicrobial polypeptides are characterized by a highly conserved region (cathelin domain) and a highly variable cathelicidin peptide domain.<ref name="Zanetti_2004">{{cite journal | vauthors = Zanetti M | title = Cathelicidins, multifunctional peptides of the innate immunity | journal = Journal of Leukocyte Biology | volume = 75 | issue = 1 | pages = 39–48 | date = January 2004 | pmid = 12960280 | doi = 10.1189/jlb.0403147 }}</ref>
Members of the cathelicidin family of antimicrobial polypeptides are characterized by a highly conserved region (cathelin domain) and a highly variable cathelicidin peptide domain.<ref name="Zanetti_2004">{{cite journal | vauthors = Zanetti M | title = Cathelicidins, multifunctional peptides of the innate immunity | journal = Journal of Leukocyte Biology | volume = 75 | issue = 1 | pages = 39–48 | date = January 2004 | pmid = 12960280 | doi = 10.1189/jlb.0403147 }}</ref>


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 [[Epithelium|epithelial]] cells and [[macrophage]]s after activation by bacteria, viruses, fungi, or the hormone [[1,25-D]], which is the hormonally active form of [[vitamin D]].<ref name="pmid16497887">{{cite journal | vauthors = 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 | title = Toll-like receptor triggering of a vitamin D-mediated human antimicrobial response | journal = Science | volume = 311 | issue = 5768 | pages = 1770–3 | date = March 2006 | pmid = 16497887 | doi = 10.1126/science.1123933 }}</ref>
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 [[Epithelium|epithelial]] cells and [[macrophage]]s after activation by bacteria, viruses, fungi, or the hormone [[1,25-D]], which is the hormonally active form of [[vitamin D]].<ref name="pmid16497887">{{cite journal | vauthors = 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 | title = Toll-like receptor triggering of a vitamin D-mediated human antimicrobial response | journal = Science | volume = 311 | issue = 5768 | pages = 1770–3 | date = March 2006 | pmid = 16497887 | doi = 10.1126/science.1123933 }}</ref> The protein encoded by the human cathelicidin gene, ''CAMP'', is cleaved into the [[LL-37]] peptide, which has several immunological functions.


==Characteristics==
==Characteristics==
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| SCOP = 1lyp
| SCOP = 1lyp
| TCDB =  
| TCDB =  
| OPM family = 236
| OPM family = 209
| OPM protein = 2k6o
| OPM protein = 2k6o
}}
}}
Cathelicidins range in size from 12 to 80 amino acid residues and have a wide range of structures.<ref name="pmid10931440">{{cite journal | vauthors = Gennaro R, Zanetti M | title = Structural features and biological activities of the cathelicidin-derived antimicrobial peptides | journal = Biopolymers | volume = 55 | issue = 1 | pages = 31–49 | year = 2000 | pmid = 10931440 | doi = 10.1002/1097-0282(2000)55:1<31::AID-BIP40>3.0.CO;2-9 }}</ref>  Most cathelicidins are linear peptides with 23-37 amino acid residues, and fold into amphipatic [[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.<ref name="Zanetti_2004"/>
Cathelicidins range in size from 12 to 80 amino acid residues and have a wide range of structures.<ref name="pmid10931440">{{cite journal | vauthors = Gennaro R, Zanetti M | title = Structural features and biological activities of the cathelicidin-derived antimicrobial peptides | journal = Biopolymers | volume = 55 | issue = 1 | pages = 31–49 | year = 2000 | pmid = 10931440 | doi = 10.1002/1097-0282(2000)55:1<31::AID-BIP40>3.0.CO;2-9 }}</ref>  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.<ref name="Zanetti_2004"/>


The cathelicidin family shares primary sequence homology with the [[cystatin]]<ref name="pmid12713586">{{cite journal | vauthors = Zaiou M, Nizet V, Gallo RL | title = Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence | journal = The Journal of Investigative Dermatology | volume = 120 | issue = 5 | pages = 810–6 | date = May 2003 | pmid = 12713586 | doi = 10.1046/j.1523-1747.2003.12132.x }}</ref> family of cysteine proteinase inhibitors, although amino acid residues thought to be important in such protease inhibition are usually lacking.
The cathelicidin family shares primary sequence homology with the [[cystatin]]<ref name="pmid12713586">{{cite journal | vauthors = Zaiou M, Nizet V, Gallo RL | title = Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence | journal = The Journal of Investigative Dermatology | volume = 120 | issue = 5 | pages = 810–6 | date = May 2003 | pmid = 12713586 | doi = 10.1046/j.1523-1747.2003.12132.x }}</ref> family of cysteine proteinase inhibitors, although amino acid residues thought to be important in such protease inhibition are usually lacking.
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== Mechanism of antimicrobial activity==
== Mechanism of antimicrobial activity==
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.<ref>{{cite journal | vauthors = Kościuczuk EM, Lisowski P, Jarczak J, Strzałkowska N, Jóźwik A, Horbańczuk J, Krzyżewski J, Zwierzchowski L, Bagnicka E | title = Cathelicidins: family of antimicrobial peptides. A review | language = en | journal = Molecular Biology Reports | volume = 39 | issue = 12 | pages = 10957–70 | date = December 2012 | pmid = 23065264 | pmc = 3487008 | doi = 10.1007/s11033-012-1997-x | url = https://link.springer.com/article/10.1007/s11033-012-1997-x }}</ref>
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.<ref>{{cite journal | vauthors = Kościuczuk EM, Lisowski P, Jarczak J, Strzałkowska N, Jóźwik A, Horbańczuk J, Krzyżewski J, Zwierzchowski L, Bagnicka E | title = Cathelicidins: family of antimicrobial peptides. A review | language = en | journal = Molecular Biology Reports | volume = 39 | issue = 12 | pages = 10957–70 | date = December 2012 | pmid = 23065264 | pmc = 3487008 | doi = 10.1007/s11033-012-1997-x }}</ref>


== Family members ==
== Mammalian orthologs ==


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


Currently identified cathelicidins include the following:<ref name="Zanetti_2004"/>
Currently identified cathelicidins include the following:<ref name="Zanetti_2004"/>
{{div col|colwidth=20em}}
{{div col|colwidth=20em}}
*Human: [[LL-37]] and [[hCAP-18]]
*Human: hCAP-18 (cleaved into LL-37 and FALL-39)
*Rhesus monkey: RL-37
*Rhesus monkey: RL-37
*Mice:CRAMP-1/2, (Cathelicidin-related Antimicrobial Peptide<ref name="pmid9148921">{{cite journal | vauthors = Gallo RL, Kim KJ, Bernfield M, Kozak CA, Zanetti M, Merluzzi L, Gennaro R | title = Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse | journal = The Journal of Biological Chemistry | volume = 272 | issue = 20 | pages = 13088–93 | date = May 1997 | pmid = 9148921 | doi = 10.1074/jbc.272.20.13088 }}</ref>
*Mice:CRAMP-1/2, (Cathelicidin-related Antimicrobial Peptide<ref name="pmid9148921">{{cite journal | vauthors = Gallo RL, Kim KJ, Bernfield M, Kozak CA, Zanetti M, Merluzzi L, Gennaro R | title = Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse | journal = The Journal of Biological Chemistry | volume = 272 | issue = 20 | pages = 13088–93 | date = May 1997 | pmid = 9148921 | doi = 10.1074/jbc.272.20.13088 }}</ref>
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*Horses:
*Horses:
*Pandas:
*Pandas:
*Tasmanian Devil: Saha-CATH5 <ref>{{cite journal | vauthors = Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K | title = Cathelicidins in the Tasmanian devil (Sarcophilus harrisii) | journal = Scientific Reports | volume = 6 | pages = 35019 | date = October 2016 | pmid = 27725697 | doi = 10.1038/srep35019 }}</ref>
*Tasmanian Devil: Saha-CATH5 <ref>{{cite journal | vauthors = Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K | title = Cathelicidins in the Tasmanian devil (Sarcophilus harrisii) | journal = Scientific Reports | volume = 6 | pages = 35019 | date = October 2016 | pmid = 27725697 | doi = 10.1038/srep35019 | pmc=5057115}}</ref>
*Salmonids: CATH1 and CATH2
*Salmonids: CATH1 and CATH2
{{Div col end}}
{{Div col end}}


== Clinical significance ==
== Clinical significance ==
NOTE: This article seems to be split between two pages. More about cathelicidin's clinical significance can be found on the page for its encoding gene, [[LL-37]].


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 [[KLK7|kallikrein 7]] serine proteases. Excessive production of LL-37 is suspected to be a contributing cause in all subtypes of [[Rosacea]].<ref name="pmid22577261">{{cite journal | vauthors = Reinholz M, Ruzicka T, Schauber J | title = Cathelicidin LL-37: an antimicrobial peptide with a role in inflammatory skin disease | journal = Annals of Dermatology | volume = 24 | issue = 2 | pages = 126–35 | date = May 2012 | pmid = 22577261 | pmc = 3346901 | doi = 10.5021/ad.2012.24.2.126 }}</ref> Antibiotics have been used in the past to treat rosacea, but antibiotics may only work because they inhibit some SCTEs.<ref name="pmid17676051">{{cite journal | vauthors = 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 | title = Increased serine protease activity and cathelicidin promotes skin inflammation in rosacea | journal = Nature Medicine | volume = 13 | issue = 8 | pages = 975–80 | date = August 2007 | pmid = 17676051 | doi = 10.1038/nm1616 }}</ref>
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 [[KLK7|kallikrein 7]] serine proteases. Excessive production of LL-37 is suspected to be a contributing cause in all subtypes of [[Rosacea]].<ref name="pmid22577261">{{cite journal | vauthors = Reinholz M, Ruzicka T, Schauber J | title = Cathelicidin LL-37: an antimicrobial peptide with a role in inflammatory skin disease | journal = Annals of Dermatology | volume = 24 | issue = 2 | pages = 126–35 | date = May 2012 | pmid = 22577261 | pmc = 3346901 | doi = 10.5021/ad.2012.24.2.126 }}</ref> Antibiotics have been used in the past to treat rosacea, but antibiotics may only work because they inhibit some SCTEs.<ref name="pmid17676051">{{cite journal | vauthors = 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 | title = Increased serine protease activity and cathelicidin promotes skin inflammation in rosacea | journal = Nature Medicine | volume = 13 | issue = 8 | pages = 975–80 | date = August 2007 | pmid = 17676051 | doi = 10.1038/nm1616 }}</ref>
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[[Category:Antimicrobial peptides]]
[[Category:Antimicrobial peptides]]
[[Category:Leukocytes]]
[[Category:Leukocytes]]
[[Category:Vitamin D]]
[[Category:Protein families]]
[[Category:Protein families]]

Latest revision as of 03:09, 31 December 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Cathelicidin-related antimicrobial peptides are a family of polypeptides primarily stored in the lysosomes of macrophages and polymorphonuclear leukocytes (PMNs).[1] Cathelicidins serve a critical role in mammalian innate immune defense against invasive bacterial infection.[2] 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.[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.[2]

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.[3] The protein encoded by the human cathelicidin gene, CAMP, is cleaved into the LL-37 peptide, which has several immunological functions.

Characteristics

Cathelicidin
File:PDB 1kwi EBI.jpg
Crystal Structure Analysis of the Cathelicidin Motif of Protegrins
Identifiers
SymbolCathelicidin
PfamPF00666
Pfam clanCL0121
InterProIPR001894
PROSITEPDOC00729
SCOP1lyp
SUPERFAMILY1lyp
OPM superfamily209
OPM protein2k6o

Cathelicidins range in size from 12 to 80 amino acid residues and have a wide range of structures.[4] 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.[2]

The cathelicidin family shares primary sequence homology with the cystatin[5] family of cysteine proteinase inhibitors, although amino acid residues thought to be important in such protease inhibition are usually lacking.

Mechanism of antimicrobial activity

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.[6]

Mammalian orthologs

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

Currently identified cathelicidins include the following:[2]

  • Human: hCAP-18 (cleaved into LL-37 and FALL-39)
  • Rhesus monkey: RL-37
  • Mice:CRAMP-1/2, (Cathelicidin-related Antimicrobial Peptide[7]
  • 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)[8]
  • Sheep:
  • Goats:
  • Chickens: Four cathelicidins, fowlicidins 1,2,3 and cathelicidin Beta-1 [9]
  • Horses:
  • Pandas:
  • Tasmanian Devil: Saha-CATH5 [10]
  • Salmonids: CATH1 and CATH2

Clinical significance

NOTE: This article seems to be split between two pages. More about cathelicidin's clinical significance can be found on the page for its encoding gene, LL-37.

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.[11] Antibiotics have been used in the past to treat rosacea, but antibiotics may only work because they inhibit some SCTEs.[12]

Higher plasma levels of human cathelicidin antimicrobial protein (hCAP18), 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 this protein were 3.7 times more likely to survive kidney dialysis for a year without a fatal infection.[13]

Vitamin D up-regulates genetic expression of cathelicidin, which exhibits broad-spectrum microbicidal activity against bacteria, fungi, and viruses.[14][15] Cathelicidin rapidly destroys the lipoprotein membranes of microbes enveloped in phagosomes after fusion with lysosomes in macrophages.

See also

References

  1. ↑ "Entrez Gene: CAMP cathelicidin antimicrobial peptide".
  2. ↑ 2.0 2.1 2.2 2.3 2.4 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.
  3. ↑ 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. doi:10.1126/science.1123933. PMID 16497887.
  4. ↑ 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.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ 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.
  8. ↑ 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.
  9. ↑ 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.
  10. ↑ 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. doi:10.1038/srep35019. PMC 5057115. PMID 27725697.
  11. ↑ 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.
  12. ↑ 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.
  13. ↑ 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. PMID 19133797.
  14. ↑ Zasloff M (January 2002). "Antimicrobial peptides of multicellular organisms". Nature. 415 (6870): 389–95. doi:10.1038/415389a. PMID 11807545.
  15. ↑ 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.

Further reading

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