The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

CAMP  -  cathelicidin antimicrobial peptide

Homo sapiens

Synonyms: 18 kDa cationic antimicrobial protein, CAP-18, CAP18, CRAMP, Cathelicidin antimicrobial peptide, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of CAMP


Psychiatry related information on CAMP


High impact information on CAMP

  • Here, we describe the production and function of the cathelicidin antimicrobial peptides LL-37, its precursor hCAP-18 and its ortholog CRAMP in epithelial cells of human and mouse urinary tract, respectively [10].
  • In addition, clinical E. coli strains that were more resistant to LL-37 caused more severe urinary tract infections than did susceptible strains [10].
  • The mature human (LL-37) and mouse (CRAMP) peptides are encoded by similar genes (CAMP and Cnlp, respectively), and have similar alpha-helical structures, spectra of antimicrobial activity and tissue distribution [11].
  • Moreover, erythrocytes coated with supernatant antigens from the Camp or FCR-3 strain were invaded normally by merozoites of the homologous strain but were partially resistant to invasion by merozoites of the heterologous strain [12].
  • IL-4/IL-13 enhanced VV replication while downregulating LL-37 in VV-stimulated keratinocytes [13].

Chemical compound and disease context of CAMP


Biological context of CAMP

  • Taken together, these findings demonstrate that LL-37/hCAP-18 is a multifunctional antimicrobial peptide with a central role in innate immunity by linking host defense and inflammation with angiogenesis and arteriogenesis [1].
  • Of note, LL-37 dose dependently (0.01-5 microg/ml) suppressed neutrophil apoptosis, accompanied with the phosphorylation of ERK-1/2, expression of Bcl-x(L) (an antiapoptotic protein), and inhibition of caspase 3 activity [3].
  • Transfection of this active form, ASK1-DeltaN, significantly enhanced the expression of hBD1-3 and LL37 [19].
  • Increased levels of inflammatory markers in bronchoalveolar lavage fluid were associated with elevated concentrations of LL-37/hCAP-18 (total cell count, P = 0.006; relative neutrophil count, P = 0.002) [20].
  • Deterioration of lung function, measured by MEF25 (maximal flow rate at 25% of residual forced vital capacity), correlated with decreased hBD-2 (P = 0.026), but increased LL-37/hCAP-18 concentrations (P = 0.016) [20].

Anatomical context of CAMP


Associations of CAMP with chemical compounds


Physical interactions of CAMP


Co-localisations of CAMP


Regulatory relationships of CAMP


Other interactions of CAMP

  • Here we report that LL-37 is chemotactic for, and can induce Ca(2+) mobilization in, human monocytes and formyl peptide receptor-like 1 (FPRL1)-transfected human embryonic kidney 293 cells [21].
  • Pulmonary or systemic infections were associated with significantly increased concentrations of LL-37, hBD-1, and hBD-2 [31].
  • Among the bacteria tested in this study, F. nucleatum was highly susceptible to hBD3 and LL37, and S. mutans was highly susceptible to hBD3 [32].
  • CAP18 and PAI-1 negatively correlated with pulmonary function [33].
  • However, we found that hCAP18 and GPI-PLD, along with apoA-I, are common components of both lytic and non-lytic primate HDLs [34].

Analytical, diagnostic and therapeutic context of CAMP


  1. An angiogenic role for the human peptide antibiotic LL-37/hCAP-18. Koczulla, R., von Degenfeld, G., Kupatt, C., Krötz, F., Zahler, S., Gloe, T., Issbrücker, K., Unterberger, P., Zaiou, M., Lebherz, C., Karl, A., Raake, P., Pfosser, A., Boekstegers, P., Welsch, U., Hiemstra, P.S., Vogelmeier, C., Gallo, R.L., Clauss, M., Bals, R. J. Clin. Invest. (2003) [Pubmed]
  2. Selective killing of vaccinia virus by LL-37: implications for eczema vaccinatum. Howell, M.D., Jones, J.F., Kisich, K.O., Streib, J.E., Gallo, R.L., Leung, D.Y. J. Immunol. (2004) [Pubmed]
  3. An antimicrobial cathelicidin peptide, human CAP18/LL-37, suppresses neutrophil apoptosis via the activation of formyl-peptide receptor-like 1 and P2X7. Nagaoka, I., Tamura, H., Hirata, M. J. Immunol. (2006) [Pubmed]
  4. The human beta-defensins (-1, -2, -3, -4) and cathelicidin LL-37 induce IL-18 secretion through p38 and ERK MAPK activation in primary human keratinocytes. Niyonsaba, F., Ushio, H., Nagaoka, I., Okumura, K., Ogawa, H. J. Immunol. (2005) [Pubmed]
  5. Structural requirements for association of neurofascin with ankyrin. Zhang, X., Davis, J.Q., Carpenter, S., Bennett, V. J. Biol. Chem. (1998) [Pubmed]
  6. Evaluation of the asthma camp experience for children. Punnett, A.F., Thurber, S. The Journal of asthma : official journal of the Association for the Care of Asthma. (1993) [Pubmed]
  7. Personality disorder in young women with treated phenylketonuria. Waisbren, S.E., Zaff, J. J. Inherit. Metab. Dis. (1994) [Pubmed]
  8. The burn camp experience: variables that influence the enhancement of self-esteem. Biggs, K.S., Heinrich, J.J., Jekel, J.F., Cuono, C.B. The Journal of burn care & rehabilitation. (1997) [Pubmed]
  9. The effectiveness of a peer support camp for siblings of children with cancer. Sidhu, R., Passmore, A., Baker, D. Pediatric blood & cancer. (2006) [Pubmed]
  10. The antimicrobial peptide cathelicidin protects the urinary tract against invasive bacterial infection. Chromek, M., Slamová, Z., Bergman, P., Kovács, L., Podracká, L., Ehrén, I., Hökfelt, T., Gudmundsson, G.H., Gallo, R.L., Agerberth, B., Brauner, A. Nat. Med. (2006) [Pubmed]
  11. Innate antimicrobial peptide protects the skin from invasive bacterial infection. Nizet, V., Ohtake, T., Lauth, X., Trowbridge, J., Rudisill, J., Dorschner, R.A., Pestonjamasp, V., Piraino, J., Huttner, K., Gallo, R.L. Nature (2001) [Pubmed]
  12. A Plasmodium falciparum antigen that binds to host erythrocytes and merozoites. Camus, D., Hadley, T.J. Science (1985) [Pubmed]
  13. Cytokine milieu of atopic dermatitis skin subverts the innate immune response to vaccinia virus. Howell, M.D., Gallo, R.L., Boguniewicz, M., Jones, J.F., Wong, C., Streib, J.E., Leung, D.Y. Immunity (2006) [Pubmed]
  14. Evaluation of the effects of peptide antibiotics human beta-defensins-1/-2 and LL-37 on histamine release and prostaglandin D(2) production from mast cells. Niyonsaba, F., Someya, A., Hirata, M., Ogawa, H., Nagaoka, I. Eur. J. Immunol. (2001) [Pubmed]
  15. Immunomodulatory activities of small host defense peptides. Bowdish, D.M., Davidson, D.J., Scott, M.G., Hancock, R.E. Antimicrob. Agents Chemother. (2005) [Pubmed]
  16. Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence. Zaiou, M., Nizet, V., Gallo, R.L. J. Invest. Dermatol. (2003) [Pubmed]
  17. Interaction of CAP18-derived peptides with membranes made from endotoxins or phospholipids. Gutsmann, T., Hagge, S.O., Larrick, J.W., Seydel, U., Wiese, A. Biophys. J. (2001) [Pubmed]
  18. Augmentation of innate host defense by expression of a cathelicidin antimicrobial peptide. Bals, R., Weiner, D.J., Moscioni, A.D., Meegalla, R.L., Wilson, J.M. Infect. Immun. (1999) [Pubmed]
  19. New mechanisms of skin innate immunity: ASK1-mediated keratinocyte differentiation regulates the expression of beta-defensins, LL37, and TLR2. Sayama, K., Komatsuzawa, H., Yamasaki, K., Shirakata, Y., Hanakawa, Y., Ouhara, K., Tokumaru, S., Dai, X., Tohyama, M., Ten Dijke, P., Sugai, M., Ichijo, H., Hashimoto, K. Eur. J. Immunol. (2005) [Pubmed]
  20. Beta-defensins and LL-37 in bronchoalveolar lavage fluid of patients with cystic fibrosis. Chen, C.I., Schaller-Bals, S., Paul, K.P., Wahn, U., Bals, R. J. Cyst. Fibros. (2004) [Pubmed]
  21. 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. De Yang, n.u.l.l., Chen, Q., Schmidt, A.P., Anderson, G.M., Wang, J.M., Wooters, J., Oppenheim, J.J., Chertov, O. J. Exp. Med. (2000) [Pubmed]
  22. Bacterial products increase expression of the human cathelicidin hCAP-18/LL-37 in cultured human sinus epithelial cells. Nell, M.J., Sandra Tjabringa, G., Vonk, M.J., Hiemstra, P.S., Grote, J.J. FEMS Immunol. Med. Microbiol. (2004) [Pubmed]
  23. FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis. Agerberth, B., Gunne, H., Odeberg, J., Kogner, P., Boman, H.G., Gudmundsson, G.H. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  24. Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Sørensen, O.E., Follin, P., Johnsen, A.H., Calafat, J., Tjabringa, G.S., Hiemstra, P.S., Borregaard, N. Blood (2001) [Pubmed]
  25. The human cationic peptide LL-37 induces activation of the extracellular signal-regulated kinase and p38 kinase pathways in primary human monocytes. Bowdish, D.M., Davidson, D.J., Speert, D.P., Hancock, R.E. J. Immunol. (2004) [Pubmed]
  26. Apolipoprotein A-I binds and inhibits the human antibacterial/cytotoxic peptide LL-37. Wang, Y., Agerberth, B., Löthgren, A., Almstedt, A., Johansson, J. J. Biol. Chem. (1998) [Pubmed]
  27. The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils. Sørensen, O., Arnljots, K., Cowland, J.B., Bainton, D.F., Borregaard, N. Blood (1997) [Pubmed]
  28. Induction of keratinocyte migration via transactivation of the epidermal growth factor receptor by the antimicrobial peptide LL-37. Tokumaru, S., Sayama, K., Shirakata, Y., Komatsuzawa, H., Ouhara, K., Hanakawa, Y., Yahata, Y., Dai, X., Tohyama, M., Nagai, H., Yang, L., Higashiyama, S., Yoshimura, A., Sugai, M., Hashimoto, K. J. Immunol. (2005) [Pubmed]
  29. The antimicrobial peptide LL-37 enhances IL-8 release by human airway smooth muscle cells. Zuyderduyn, S., Ninaber, D.K., Hiemstra, P.S., Rabe, K.F. J. Allergy Clin. Immunol. (2006) [Pubmed]
  30. A novel P2X7 receptor activator, the human cathelicidin-derived peptide LL37, induces IL-1 beta processing and release. Elssner, A., Duncan, M., Gavrilin, M., Wewers, M.D. J. Immunol. (2004) [Pubmed]
  31. Increased levels of antimicrobial peptides in tracheal aspirates of newborn infants during infection. Schaller-Bals, S., Schulze, A., Bals, R. Am. J. Respir. Crit. Care Med. (2002) [Pubmed]
  32. Susceptibilities of periodontopathogenic and cariogenic bacteria to antibacterial peptides, {beta}-defensins and LL37, produced by human epithelial cells. Ouhara, K., Komatsuzawa, H., Yamada, S., Shiba, H., Fujiwara, T., Ohara, M., Sayama, K., Hashimoto, K., Kurihara, H., Sugai, M. J. Antimicrob. Chemother. (2005) [Pubmed]
  33. Sputum cathelicidin, urokinase plasminogen activation system components, and cytokines discriminate cystic fibrosis, COPD, and asthma inflammation. Xiao, W., Hsu, Y.P., Ishizaka, A., Kirikae, T., Moss, R.B. Chest (2005) [Pubmed]
  34. Characterization of primate trypanosome lytic factors. Lugli, E.B., Pouliot, M., Portela, M.d.e.l. .P., Loomis, M.R., Raper, J. Mol. Biochem. Parasitol. (2004) [Pubmed]
  35. Structure-function relationships among human cathelicidin peptides: dissociation of antimicrobial properties from host immunostimulatory activities. Braff, M.H., Hawkins, M.A., Di Nardo, A., Lopez-Garcia, B., Howell, M.D., Wong, C., Lin, K., Streib, J.E., Dorschner, R., Leung, D.Y., Gallo, R.L. J. Immunol. (2005) [Pubmed]
  36. 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. Bals, R., Wang, X., Zasloff, M., Wilson, J.M. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  37. The human antimicrobial and chemotactic peptides LL-37 and alpha-defensins are expressed by specific lymphocyte and monocyte populations. Agerberth, B., Charo, J., Werr, J., Olsson, B., Idali, F., Lindbom, L., Kiessling, R., Jörnvall, H., Wigzell, H., Gudmundsson, G.H. Blood (2000) [Pubmed]
WikiGenes - Universities